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adding manually curated annotations in BioC XML files; adding annotations extracted from curated BioC XML files as JSON and tab-separated CSV; adding manually curated annotations and corresponding sentences extracted from BioC XML as IOB formated input for training

BioC_XML/4781976_v0.xml

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+<?xml version="1.0" encoding="UTF-8"?>
+<!DOCTYPE collection SYSTEM "BioC.dtd">
+<collection>
+  <source>PMC</source>
+  <date>20201222</date>
+  <key>pmc.key</key>
+  <document>
+    <id>4781976</id>
+    <infon key="license">CC BY</infon>
+    <infon key="tt_curatable">no</infon>
+    <infon key="tt_version">0</infon>
+    <infon key="tt_round">0</infon>
+    <passage>
+      <infon key="article-id_doi">10.1016/j.dib.2016.02.042</infon>
+      <infon key="article-id_pmc">4781976</infon>
+      <infon key="article-id_pmid">26977434</infon>
+      <infon key="article-id_publisher-id">S2352-3409(16)30064-6</infon>
+      <infon key="fpage">344</infon>
+      <infon key="kwd">Tom1, GAT domain, Tollip, Ubiquitin, nuclear magnetic resonance</infon>
+      <infon key="license">This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).</infon>
+      <infon key="lpage">348</infon>
+      <infon key="name_0">surname:Xiao;given-names:Shuyan</infon>
+      <infon key="name_1">surname:Ellena;given-names:Jeffrey F.</infon>
+      <infon key="name_2">surname:Armstrong;given-names:Geoffrey S.</infon>
+      <infon key="name_3">surname:Capelluto;given-names:Daniel G.S.</infon>
+      <infon key="section_type">TITLE</infon>
+      <infon key="title">Keywords</infon>
+      <infon key="type">front</infon>
+      <infon key="volume">7</infon>
+      <infon key="year">2016</infon>
+      <offset>0</offset>
+      <text>Structure of the GAT domain of the endosomal adapter protein Tom1</text>
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+        <infon key="identifier">DUMMY:</infon>
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+        <text>Structure</text>
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+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
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+        <text>GAT</text>
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+        <infon key="identifier">MESH:</infon>
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+        <text>adapter protein</text>
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+        <text>Tom1</text>
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+      <infon key="section_type">ABSTRACT</infon>
+      <infon key="type">abstract</infon>
+      <offset>66</offset>
+      <text>Cellular homeostasis requires correct delivery of cell-surface receptor proteins (cargo) to their target subcellular compartments. The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments. Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD). In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain. The estimated protein structure exhibits a bundle of three helical elements. We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.</text>
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+        <text>cell-surface receptor</text>
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+        <text>adapter proteins</text>
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+        <text>ubiquitinated</text>
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+        <text>Tom1-binding domain</text>
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+        <infon key="identifier">SO:</infon>
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+        <text>TBD</text>
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+        <text>solution NMR</text>
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+        <text>Tom1</text>
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+        <infon key="identifier">MESH:</infon>
+        <location offset="612" length="7"/>
+        <text>compare</text>
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+        <text>Tom1</text>
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+        <text>GAT</text>
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+        <text>structure</text>
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+        <text>structures</text>
+      </annotation>
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+        <text>Tollip</text>
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+        <text>TBD-</text>
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+        <text>ubiquitin-bound</text>
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+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">title_1</infon>
+      <offset>730</offset>
+      <text>Specifications table</text>
+    </passage>
+    <passage>
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+      <infon key="xml">&lt;?xml version="1.0" encoding="UTF-8"?&gt;
+&lt;table frame="hsides" rules="groups"&gt;&lt;tbody&gt;&lt;tr&gt;&lt;td&gt;Subject area&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Biology&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;More specific subject area&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Structural biology&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Type of data&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Table, text file, graph, figures&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;How data was acquired&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Circular dichroism and NMR. NMR data was recorded using a Bruker 800 MHz&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Data format&lt;/td&gt;&lt;td&gt;&lt;italic&gt;PDB format text file. Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Experimental factors&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Recombinant human Tom1 GAT domain was purified to homogeneity before use&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Experimental features&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Solution structure of Tom1 GAT was determined from NMR chemical shift data&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Data source location&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Virginia and Colorado, United States.&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Data accessibility&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Data is available within this article. Tom1 GAT structural data is publicly available in the RCSB Protein Data Bank (http://www.rscb.org/) under the accession number PDB: 2n9d&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;/tbody&gt;&lt;/table&gt;
+</infon>
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+      <text>Table	 	</text>
+    </passage>
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+      <infon key="id">t0010</infon>
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+&lt;table frame="hsides" rules="groups"&gt;&lt;tbody&gt;&lt;tr&gt;&lt;td&gt;Subject area&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Biology&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;More specific subject area&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Structural biology&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Type of data&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Table, text file, graph, figures&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;How data was acquired&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Circular dichroism and NMR. NMR data was recorded using a Bruker 800 MHz&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Data format&lt;/td&gt;&lt;td&gt;&lt;italic&gt;PDB format text file. Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Experimental factors&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Recombinant human Tom1 GAT domain was purified to homogeneity before use&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Experimental features&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Solution structure of Tom1 GAT was determined from NMR chemical shift data&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Data source location&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Virginia and Colorado, United States.&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Data accessibility&lt;/td&gt;&lt;td&gt;&lt;italic&gt;Data is available within this article. Tom1 GAT structural data is publicly available in the RCSB Protein Data Bank (http://www.rscb.org/) under the accession number PDB: 2n9d&lt;/italic&gt;&lt;/td&gt;&lt;/tr&gt;&lt;/tbody&gt;&lt;/table&gt;
+</infon>
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+      <text>Subject area	Biology	 	More specific subject area	Structural biology	 	Type of data	Table, text file, graph, figures	 	How data was acquired	Circular dichroism and NMR. NMR data was recorded using a Bruker 800 MHz	 	Data format	PDB format text file. Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States.	 	Data accessibility	Data is available within this article. Tom1 GAT structural data is publicly available in the RCSB Protein Data Bank (http://www.rscb.org/) under the accession number PDB: 2n9d	 	</text>
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+        <text>Tom1</text>
+      </annotation>
+      <annotation id="38">
+        <infon key="score">0.5058204</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="1152" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="39">
+        <infon key="score">0.99844825</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:00:14Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="1226" length="18"/>
+        <text>Solution structure</text>
+      </annotation>
+      <annotation id="40">
+        <infon key="score">0.99984014</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="1248" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="41">
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+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="1253" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="42">
+        <infon key="score">0.9996598</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:59:32Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="1277" length="3"/>
+        <text>NMR</text>
+      </annotation>
+      <annotation id="238">
+        <infon key="type">evidence</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:00:28Z</infon>
+        <location offset="1281" length="14"/>
+        <text>chemical shift</text>
+      </annotation>
+      <annotation id="193">
+        <infon key="type">protein</infon>
+        <infon key="identifier">PR:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <location offset="1422" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="212">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <location offset="1427" length="3"/>
+        <text>GAT</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">title_1</infon>
+      <offset>1563</offset>
+      <text>Value of the data</text>
+    </passage>
+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">paragraph</infon>
+      <offset>1581</offset>
+      <text>The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.</text>
+      <annotation id="45">
+        <infon key="score">0.99983656</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="1585" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="213">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <location offset="1590" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="47">
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+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:00:14Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="1601" length="18"/>
+        <text>solution structure</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">paragraph</infon>
+      <offset>1690</offset>
+      <text>Tom1 GAT can adopt distinct conformations upon ligand binding.</text>
+      <annotation id="48">
+        <infon key="score">0.999843</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="1690" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="49">
+        <infon key="score">0.9992766</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="1695" length="3"/>
+        <text>GAT</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">paragraph</infon>
+      <offset>1753</offset>
+      <text>A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.</text>
+      <annotation id="50">
+        <infon key="score">0.99981683</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="1786" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="214">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <location offset="1791" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="52">
+        <infon key="score">0.9990669</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:16Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="1807" length="6"/>
+        <text>Tollip</text>
+      </annotation>
+      <annotation id="53">
+        <infon key="score">0.99973947</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:36Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="1814" length="3"/>
+        <text>TBD</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">title_1</infon>
+      <offset>1903</offset>
+      <text>Data</text>
+    </passage>
+    <passage>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">paragraph</infon>
+      <offset>1908</offset>
+      <text>Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions. The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3). Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).</text>
+      <annotation id="54">
+        <infon key="score">0.99765813</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:25Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="1924" length="25"/>
+        <text>far-UV circular dichroism</text>
+      </annotation>
+      <annotation id="55">
+        <infon key="score">0.97389156</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:22Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="1951" length="2"/>
+        <text>CD</text>
+      </annotation>
+      <annotation id="56">
+        <infon key="score">0.9930906</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:19Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="1955" length="8"/>
+        <text>spectrum</text>
+      </annotation>
+      <annotation id="57">
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+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:06:22Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="1971" length="5"/>
+        <text>Tom 1</text>
+      </annotation>
+      <annotation id="215">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <location offset="1977" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="59">
+        <infon key="score">0.999609</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:58Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2012" length="7"/>
+        <text>α-helix</text>
+      </annotation>
+      <annotation id="60">
+        <infon key="score">0.9994879</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:59Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2024" length="8"/>
+        <text>β-strand</text>
+      </annotation>
+      <annotation id="61">
+        <infon key="score">0.99985206</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="2080" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="62">
+        <infon key="score">0.7947963</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2085" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="63">
+        <infon key="score">0.9988989</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:06:41Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2089" length="21"/>
+        <text>structural restraints</text>
+      </annotation>
+      <annotation id="64">
+        <infon key="score">0.9295965</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:06:45Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2131" length="10"/>
+        <text>structures</text>
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+      <annotation id="65">
+        <infon key="score">0.9993277</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:33Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2161" length="26"/>
+        <text>root mean square deviation</text>
+      </annotation>
+      <annotation id="66">
+        <infon key="score">0.9996222</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:36Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2189" length="4"/>
+        <text>RMSD</text>
+      </annotation>
+      <annotation id="67">
+        <infon key="score">0.9990892</infon>
+        <infon key="type">residue_range</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:42Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2319" length="9"/>
+        <text>Q216-E240</text>
+      </annotation>
+      <annotation id="68">
+        <infon key="score">0.9997021</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:49Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2330" length="9"/>
+        <text>α-helix 1</text>
+      </annotation>
+      <annotation id="69">
+        <infon key="score">0.9991074</infon>
+        <infon key="type">residue_range</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:44Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2342" length="9"/>
+        <text>P248-Q274</text>
+      </annotation>
+      <annotation id="70">
+        <infon key="score">0.9997027</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:51Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2353" length="9"/>
+        <text>α-helix 2</text>
+      </annotation>
+      <annotation id="71">
+        <infon key="score">0.99909496</infon>
+        <infon key="type">residue_range</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:46Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="2369" length="9"/>
+        <text>E278-T306</text>
+      </annotation>
+      <annotation id="72">
+        <infon key="score">0.99970627</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:53Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2380" length="9"/>
+        <text>α-helix 3</text>
+      </annotation>
+      <annotation id="73">
+        <infon key="score">0.99831545</infon>
+        <infon key="type">chemical</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:07:05Z</infon>
+        <infon key="identifier">CHEBI:</infon>
+        <location offset="2399" length="9"/>
+        <text>ubiquitin</text>
+      </annotation>
+      <annotation id="74">
+        <infon key="score">0.99984026</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="2466" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="75">
+        <infon key="score">0.99932325</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:58Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2471" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="76">
+        <infon key="score">0.9996645</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:01:56Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2475" length="17"/>
+        <text>α-helices 1 and 2</text>
+      </annotation>
+      <annotation id="77">
+        <infon key="score">0.9998336</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:16Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="2504" length="6"/>
+        <text>Tollip</text>
+      </annotation>
+      <annotation id="78">
+        <infon key="score">0.9960354</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:36Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="2511" length="3"/>
+        <text>TBD</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">title_1</infon>
+      <offset>2559</offset>
+      <text>Experimental design, materials, and methods</text>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">title_2</infon>
+      <offset>2603</offset>
+      <text>Protein expression and purification</text>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">paragraph</infon>
+      <offset>2639</offset>
+      <text>Human Tom1 GAT (residues 215–309) cDNA was cloned into both pGEX6P1 and pET28a vectors, and expressed as GST-tagged and His-tagged fusion proteins, respectively, using Escherichia coli [Rosetta (DE3) strain]. The 13C, 15N-labeled Tom1 GAT domain was expressed and purified as described previously.</text>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">title_2</infon>
+      <offset>2939</offset>
+      <text>Circular dichroism</text>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">paragraph</infon>
+      <offset>2958</offset>
+      <text>Far-UV CD spectra of the His-Tom1 GAT domain were collected on a Jasco J-815 spectropolarimeter using a 1 mm path length quartz cell at room temperature. The protein (10 μM) was solubilized in 5 mM Tris–HCl (pH 7) and 100 mM KF. Spectra were obtained from five accumulated scans from 190 to 260 nm using a bandwidth of 1 nm and a response time of 1 s at a scan speed of 20 nm/min. Buffer backgrounds were employed to subtract the protein spectra. Data was processed using the Dichroweb server and the CONTIN algorithm (http://dichroweb.cryst.bbk.ac.uk/html/home.shtml).</text>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">title_2</infon>
+      <offset>3539</offset>
+      <text>NMR structure determination</text>
+    </passage>
+    <passage>
+      <infon key="section_type">METHODS</infon>
+      <infon key="type">paragraph</infon>
+      <offset>3567</offset>
+      <text>NMR experiments were performed using 1 mM 13C, 15N-labeled Tom1 GAT domain in a buffer containing 20 mM d11-TrisHCl (pH 7), 50 mM KCl, 1 mM d18-DTT, and 1 mM NaN3. NMR spectra were recorded at 25 °C on a Bruker 800-MHz spectrometer (University of Virginia). The individual structure of Tom1 GAT was generated using CS-Rosetta (https://csrosetta.bmrb.wisc.edu/csrosetta). Chemical shift information (BMRB #26574) was used to obtain the structure calculation. The Rosetta calculations yielded 3000 structures of Tom1 GAT. From these, ten structures were selected based on their score and RMSDs, and converted to Protein Data Bank (PDB) format. NMR structural statistics for the ten lowest energy conformers of Tom1 GAT was generated using the Protein Structure Validation Suite. By using MolProbity, the Ramachandran analysis of the ten superimposed Tom1 GAT structures identified that 100% of the residues were in the most favored regions and there were no Ramachandran outliers in the allowed and disallowed regions. Protein structure images were obtained using PyMol (http://www.pymol.org). The structures of the ubiquitin- and Tollip TBD-bound states of the Tom1 GAT domain were obtained from data reported in Refs. and.</text>
+    </passage>
+    <passage>
+      <infon key="section_type">REF</infon>
+      <infon key="type">title</infon>
+      <offset>4797</offset>
+      <text>References</text>
+    </passage>
+    <passage>
+      <infon key="fpage">1910</infon>
+      <infon key="lpage">1920</infon>
+      <infon key="name_0">surname:Xiao;given-names:S.</infon>
+      <infon key="name_1">surname:Brannon;given-names:M.K.</infon>
+      <infon key="name_2">surname:Zhao;given-names:X.</infon>
+      <infon key="name_3">surname:Fread;given-names:K.I.</infon>
+      <infon key="name_4">surname:Ellena;given-names:J.F.</infon>
+      <infon key="name_5">surname:Bushweller;given-names:J.H.</infon>
+      <infon key="name_6">surname:Finkielstein;given-names:C.V.</infon>
+      <infon key="name_7">surname:Armstrong;given-names:G.S.</infon>
+      <infon key="name_8">surname:Capelluto;given-names:D.G.</infon>
+      <infon key="section_type">REF</infon>
+      <infon key="source">Structure</infon>
+      <infon key="type">ref</infon>
+      <infon key="volume">23</infon>
+      <infon key="year">2015</infon>
+      <offset>4808</offset>
+      <text>Tom1 modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism</text>
+    </passage>
+    <passage>
+      <infon key="fpage">5385</infon>
+      <infon key="lpage">5391</infon>
+      <infon key="name_0">surname:Akutsu;given-names:M.</infon>
+      <infon key="name_1">surname:Kawasaki;given-names:M.</infon>
+      <infon key="name_2">surname:Katoh;given-names:Y.</infon>
+      <infon key="name_3">surname:Shiba;given-names:T.</infon>
+      <infon key="name_4">surname:Yamaguchi;given-names:Y.</infon>
+      <infon key="name_5">surname:Kato;given-names:R.</infon>
+      <infon key="name_6">surname:Kato;given-names:K.</infon>
+      <infon key="name_7">surname:Nakayama;given-names:K.</infon>
+      <infon key="name_8">surname:Wakatsuki;given-names:S.</infon>
+      <infon key="pub-id_pmid">16199040</infon>
+      <infon key="section_type">REF</infon>
+      <infon key="source">FEBS Lett.</infon>
+      <infon key="type">ref</infon>
+      <infon key="volume">579</infon>
+      <infon key="year">2005</infon>
+      <offset>4921</offset>
+      <text>Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain</text>
+    </passage>
+    <passage>
+      <infon key="section_type">SUPPL</infon>
+      <infon key="type">title_1</infon>
+      <offset>4996</offset>
+      <text>Supplementary material</text>
+    </passage>
+    <passage>
+      <infon key="section_type">SUPPL</infon>
+      <infon key="type">footnote</infon>
+      <offset>5019</offset>
+      <text>Supplementary data associated with this article can be found in the online version at doi:10.1016/j.dib.2016.02.042.</text>
+    </passage>
+    <passage>
+      <infon key="file">gr1.jpg</infon>
+      <infon key="id">f0005</infon>
+      <infon key="section_type">FIG</infon>
+      <infon key="type">fig_caption</infon>
+      <offset>5136</offset>
+      <text>Representative far-UV CD spectrum of the His-Tom1 GAT domain.</text>
+      <annotation id="151">
+        <infon key="score">0.99858</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:03:56Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5151" length="9"/>
+        <text>far-UV CD</text>
+      </annotation>
+      <annotation id="152">
+        <infon key="score">0.71714723</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:06:50Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5161" length="8"/>
+        <text>spectrum</text>
+      </annotation>
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+        <infon key="score">0.8865229</infon>
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+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:04:25Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5177" length="4"/>
+        <text>His-</text>
+      </annotation>
+      <annotation id="154">
+        <infon key="score">0.9922563</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5181" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="225">
+        <infon key="type">structure_element</infon>
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+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="5186" length="3"/>
+        <text>GAT</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="file">gr1.jpg</infon>
+      <infon key="id">f0005</infon>
+      <infon key="section_type">FIG</infon>
+      <infon key="type">fig</infon>
+      <offset>5198</offset>
+      <text>Fig. 1.</text>
+    </passage>
+    <passage>
+      <infon key="file">gr2.jpg</infon>
+      <infon key="id">f0010</infon>
+      <infon key="section_type">FIG</infon>
+      <infon key="type">fig_caption</infon>
+      <offset>5206</offset>
+      <text>(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain. Helices are shown in orange, whereas loops are colored in green. (B) Ribbon illustration of the Tom1 GAT domain.</text>
+      <annotation id="156">
+        <infon key="score">0.9992467</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:04:41Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5246" length="22"/>
+        <text>backbone superposition</text>
+      </annotation>
+      <annotation id="157">
+        <infon key="score">0.9941738</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:06:54Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5284" length="10"/>
+        <text>structures</text>
+      </annotation>
+      <annotation id="158">
+        <infon key="score">0.9998486</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5303" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="226">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="5308" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="160">
+        <infon key="score">0.99984694</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5416" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="227">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="5421" length="3"/>
+        <text>GAT</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="file">gr2.jpg</infon>
+      <infon key="id">f0010</infon>
+      <infon key="section_type">FIG</infon>
+      <infon key="type">fig</infon>
+      <offset>5433</offset>
+      <text>Fig. 2.</text>
+    </passage>
+    <passage>
+      <infon key="file">gr3.jpg</infon>
+      <infon key="id">f0015</infon>
+      <infon key="section_type">FIG</infon>
+      <infon key="type">fig_caption</infon>
+      <offset>5441</offset>
+      <text>(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).</text>
+      <annotation id="162">
+        <infon key="score">0.9534955</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:10Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5462" length="23"/>
+        <text>superimposed structures</text>
+      </annotation>
+      <annotation id="163">
+        <infon key="score">0.99984646</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5493" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="228">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="5498" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="165">
+        <infon key="score">0.99965954</infon>
+        <infon key="type">protein_state</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:18Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5516" length="4"/>
+        <text>free</text>
+      </annotation>
+      <annotation id="166">
+        <infon key="score">0.9996728</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:16Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5551" length="6"/>
+        <text>Tollip</text>
+      </annotation>
+      <annotation id="167">
+        <infon key="score">0.99953216</infon>
+        <infon key="type">protein_state</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:15Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5558" length="9"/>
+        <text>TBD-bound</text>
+      </annotation>
+      <annotation id="168">
+        <infon key="score">0.9632287</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:12Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5602" length="23"/>
+        <text>superimposed structures</text>
+      </annotation>
+      <annotation id="169">
+        <infon key="score">0.9998419</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5633" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="229">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="5638" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="171">
+        <infon key="score">0.9995443</infon>
+        <infon key="type">protein_state</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:16Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5673" length="8"/>
+        <text>Ub-bound</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="file">gr3.jpg</infon>
+      <infon key="id">f0015</infon>
+      <infon key="section_type">FIG</infon>
+      <infon key="type">fig</infon>
+      <offset>5697</offset>
+      <text>Fig. 3.</text>
+    </passage>
+    <passage>
+      <infon key="file">t0005.xml</infon>
+      <infon key="id">t0005</infon>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">table_caption</infon>
+      <offset>5705</offset>
+      <text>NMR and refinement statistics for the Tom1 GAT domain. NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.</text>
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+        <infon key="score">0.99963295</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:59:32Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5705" length="3"/>
+        <text>NMR</text>
+      </annotation>
+      <annotation id="173">
+        <infon key="score">0.9961254</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:29Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5713" length="21"/>
+        <text>refinement statistics</text>
+      </annotation>
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+        <infon key="score">0.9998447</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5743" length="4"/>
+        <text>Tom1</text>
+      </annotation>
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+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="5748" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="176">
+        <infon key="score">0.999608</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:59:32Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5760" length="3"/>
+        <text>NMR</text>
+      </annotation>
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+        <infon key="score">0.9994303</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:33Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="5764" length="21"/>
+        <text>structural statistics</text>
+      </annotation>
+      <annotation id="178">
+        <infon key="score">0.99985063</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="5818" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="179">
+        <infon key="score">0.9986708</infon>
+        <infon key="type">structure_element</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <infon key="identifier">SO:</infon>
+        <location offset="5823" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="180">
+        <infon key="score">0.9996277</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:31Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="5833" length="4"/>
+        <text>PSVS</text>
+      </annotation>
+    </passage>
+    <passage>
+      <infon key="file">t0005.xml</infon>
+      <infon key="id">t0005</infon>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">table</infon>
+      <infon key="xml">&lt;?xml version="1.0" encoding="UTF-8"?&gt;
+&lt;table frame="hsides" rules="groups"&gt;&lt;thead&gt;&lt;tr&gt;&lt;th/&gt;&lt;th&gt;&lt;bold&gt;Tom1 GAT&lt;/bold&gt;&lt;/th&gt;&lt;/tr&gt;&lt;/thead&gt;&lt;tbody&gt;&lt;tr&gt;&lt;td&gt;&lt;bold&gt;NMR distance and dihedral constraints&lt;/bold&gt;&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Dihedral angle restraints total&lt;/td&gt;&lt;td&gt;178&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;&lt;italic&gt; ϕ&lt;/italic&gt;&lt;/td&gt;&lt;td&gt;89&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;&lt;italic&gt; ψ&lt;/italic&gt;&lt;/td&gt;&lt;td&gt;89&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;&lt;bold&gt;Structure statistics&lt;/bold&gt;&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Dihedral angle constraints (deg)&lt;/td&gt;&lt;td&gt;8.8±0.2&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Max. dihedral angle violation (deg)&lt;/td&gt;&lt;td&gt;111±3&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Deviations from idealized geometry&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Bond lengths (Å)&lt;/td&gt;&lt;td&gt;0.011&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Bond angles (deg)&lt;/td&gt;&lt;td&gt;0.7&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Average pairwise r.m.s. deviation (Å)&lt;xref rid="tbl1fna" ref-type="table-fn"&gt;a&lt;/xref&gt;&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Protein&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Heavy&lt;/td&gt;&lt;td&gt;1.3&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Backbone&lt;/td&gt;&lt;td&gt;0.9&lt;/td&gt;&lt;/tr&gt;&lt;/tbody&gt;&lt;/table&gt;
+</infon>
+      <offset>5839</offset>
+      <text>Table 1.	 	</text>
+    </passage>
+    <passage>
+      <infon key="file">t0005.xml</infon>
+      <infon key="id">t0005</infon>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">table</infon>
+      <infon key="xml">&lt;?xml version="1.0" encoding="UTF-8"?&gt;
+&lt;table frame="hsides" rules="groups"&gt;&lt;thead&gt;&lt;tr&gt;&lt;th/&gt;&lt;th&gt;&lt;bold&gt;Tom1 GAT&lt;/bold&gt;&lt;/th&gt;&lt;/tr&gt;&lt;/thead&gt;&lt;tbody&gt;&lt;tr&gt;&lt;td&gt;&lt;bold&gt;NMR distance and dihedral constraints&lt;/bold&gt;&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Dihedral angle restraints total&lt;/td&gt;&lt;td&gt;178&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;&lt;italic&gt; ϕ&lt;/italic&gt;&lt;/td&gt;&lt;td&gt;89&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;&lt;italic&gt; ψ&lt;/italic&gt;&lt;/td&gt;&lt;td&gt;89&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;&lt;bold&gt;Structure statistics&lt;/bold&gt;&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Dihedral angle constraints (deg)&lt;/td&gt;&lt;td&gt;8.8±0.2&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Max. dihedral angle violation (deg)&lt;/td&gt;&lt;td&gt;111±3&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Deviations from idealized geometry&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Bond lengths (Å)&lt;/td&gt;&lt;td&gt;0.011&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Bond angles (deg)&lt;/td&gt;&lt;td&gt;0.7&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt;Average pairwise r.m.s. deviation (Å)&lt;xref rid="tbl1fna" ref-type="table-fn"&gt;a&lt;/xref&gt;&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Protein&lt;/td&gt;&lt;td/&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Heavy&lt;/td&gt;&lt;td&gt;1.3&lt;/td&gt;&lt;/tr&gt;&lt;tr&gt;&lt;td&gt; Backbone&lt;/td&gt;&lt;td&gt;0.9&lt;/td&gt;&lt;/tr&gt;&lt;/tbody&gt;&lt;/table&gt;
+</infon>
+      <offset>5851</offset>
+      <text>	Tom1 GAT	 	NMR distance and dihedral constraints		 	 Dihedral angle restraints total	178	 	 ϕ	89	 	 ψ	89	 	Structure statistics		 	 Dihedral angle constraints (deg)	8.8±0.2	 	 Max. dihedral angle violation (deg)	111±3	 	Deviations from idealized geometry		 	 Bond lengths (Å)	0.011	 	 Bond angles (deg)	0.7	 	Average pairwise r.m.s. deviation (Å)a		 	 Protein		 	 Heavy	1.3	 	 Backbone	0.9	 	</text>
+    </passage>
+    <passage>
+      <infon key="file">t0005.xml</infon>
+      <infon key="id">t0005</infon>
+      <infon key="section_type">TABLE</infon>
+      <infon key="type">table_footnote</infon>
+      <offset>6261</offset>
+      <text>Pairwise backbone and heavy-atom r.m.s. deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.</text>
+      <annotation id="187">
+        <infon key="score">0.9994108</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:50Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="6294" length="17"/>
+        <text>r.m.s. deviations</text>
+      </annotation>
+      <annotation id="188">
+        <infon key="score">0.99964523</infon>
+        <infon key="type">experimental_method</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:52Z</infon>
+        <infon key="identifier">MESH:</infon>
+        <location offset="6329" length="13"/>
+        <text>superimposing</text>
+      </annotation>
+      <annotation id="189">
+        <infon key="score">0.9990513</infon>
+        <infon key="type">residue_range</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:05:56Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="6352" length="7"/>
+        <text>215–309</text>
+      </annotation>
+      <annotation id="190">
+        <infon key="score">0.99986255</infon>
+        <infon key="type">protein</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:12Z</infon>
+        <infon key="identifier">PR:</infon>
+        <location offset="6363" length="4"/>
+        <text>Tom1</text>
+      </annotation>
+      <annotation id="232">
+        <infon key="type">structure_element</infon>
+        <infon key="identifier">SO:</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T14:57:59Z</infon>
+        <location offset="6368" length="3"/>
+        <text>GAT</text>
+      </annotation>
+      <annotation id="191">
+        <infon key="score">0.9991259</infon>
+        <infon key="type">evidence</infon>
+        <infon key="annotator">cleaner0</infon>
+        <infon key="updated_at">2023-07-20T15:06:59Z</infon>
+        <infon key="identifier">DUMMY:</infon>
+        <location offset="6403" length="10"/>
+        <text>structures</text>
+      </annotation>
+    </passage>
+  </document>
+</collection>

annotation_CSV/PMC4781976.csv

@@ -0,0 +1,114 @@
+anno_start	anno_end	anno_text	entity_type	sentence	section
+0	9	Structure	evidence	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
+17	20	GAT	structure_element	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
+45	60	adapter protein	protein_type	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
+61	65	Tom1	protein	Structure of the GAT domain of the endosomal adapter protein Tom1	TITLE
+50	71	cell-surface receptor	protein_type	Cellular homeostasis requires correct delivery of cell-surface receptor proteins (cargo) to their target subcellular compartments.	ABSTRACT
+4	20	adapter proteins	protein_type	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
+21	25	Tom1	protein	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
+30	36	Tollip	protein	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
+64	77	ubiquitinated	ptm	The adapter proteins Tom1 and Tollip are involved in sorting of ubiquitinated cargo in endosomal compartments.	ABSTRACT
+15	19	Tom1	protein	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
+69	72	GAT	structure_element	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
+97	103	Tollip	protein	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
+106	125	Tom1-binding domain	structure_element	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
+127	130	TBD	structure_element	Recruitment of Tom1 to the endosomal compartments is mediated by its GAT domain’s association to Tollip’s Tom1-binding domain (TBD).	ABSTRACT
+36	48	solution NMR	experimental_method	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
+57	66	structure	evidence	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
+74	78	Tom1	protein	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
+79	82	GAT	structure_element	In this data article, we report the solution NMR-derived structure of the Tom1 GAT domain.	ABSTRACT
+22	31	structure	evidence	The estimated protein structure exhibits a bundle of three helical elements.	ABSTRACT
+3	10	compare	experimental_method	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+15	19	Tom1	protein	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+20	23	GAT	structure_element	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+24	33	structure	evidence	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+45	55	structures	evidence	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+77	83	Tollip	protein	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+84	88	TBD-	protein_state	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+93	108	ubiquitin-bound	protein_state	We compare the Tom1 GAT structure with those structures corresponding to the Tollip TBD- and ubiquitin-bound states.	ABSTRACT
+141	159	Circular dichroism	experimental_method	"Subject area	Biology	 	More specific subject area	Structural biology	 	Type of data	Table, text file, graph, figures	 	How data was acquired	Circular dichroism and NMR."	TABLE
+164	167	NMR	experimental_method	"Subject area	Biology	 	More specific subject area	Structural biology	 	Type of data	Table, text file, graph, figures	 	How data was acquired	Circular dichroism and NMR."	TABLE
+0	3	NMR	experimental_method	"NMR data was recorded using a Bruker 800 MHz	 	Data format	PDB format text file."	TABLE
+12	22	CS-Rosetta	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+24	59	Protein Structure Validation Server	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+61	65	PSVS	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+68	75	NMRPipe	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+77	84	NMRDraw	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+131	136	human	species	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+137	141	Tom1	protein	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+142	145	GAT	structure_element	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+216	234	Solution structure	evidence	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+238	242	Tom1	protein	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+243	246	GAT	structure_element	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+267	270	NMR	experimental_method	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+271	285	chemical shift	evidence	"Analyzed by CS-Rosetta, Protein Structure Validation Server (PSVS), NMRPipe, NMRDraw, and PyMol	 	Experimental factors	Recombinant human Tom1 GAT domain was purified to homogeneity before use	 	Experimental features	Solution structure of Tom1 GAT was determined from NMR chemical shift data	 	Data source location	Virginia and Colorado, United States."	TABLE
+5	8	GAT	structure_element	"Tom1 GAT structural data is publicly available in the RCSB Protein Data Bank (http://www.rscb.org/) under the accession number PDB: 2n9d	 	"	TABLE
+4	8	Tom1	protein	The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.	TABLE
+9	12	GAT	structure_element	The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.	TABLE
+20	38	solution structure	evidence	The Tom1 GAT domain solution structure will provide additional tools for modulating its biological function.	TABLE
+0	4	Tom1	protein	Tom1 GAT can adopt distinct conformations upon ligand binding.	TABLE
+5	8	GAT	structure_element	Tom1 GAT can adopt distinct conformations upon ligand binding.	TABLE
+33	37	Tom1	protein	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
+38	41	GAT	structure_element	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
+54	60	Tollip	protein	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
+61	64	TBD	structure_element	A conformational response of the Tom1 GAT domain upon Tollip TBD binding can serve as an example to explain mutually exclusive ligand binding events.	TABLE
+16	41	far-UV circular dichroism	experimental_method	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+43	45	CD	experimental_method	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+47	55	spectrum	evidence	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+63	68	Tom 1	protein	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+69	72	GAT	structure_element	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+104	111	α-helix	structure_element	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+116	124	β-strand	structure_element	Analysis of the far-UV circular dichroism (CD) spectrum of the Tom 1 GAT domain (Fig. 1) predicts 58.7% α-helix, 3% β-strand, 15.5% turn, and 22.8% disordered regions.	TABLE
+4	8	Tom1	protein	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+9	12	GAT	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+13	34	structural restraints	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+55	65	structures	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+85	111	root mean square deviation	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+113	117	RMSD	evidence	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+243	252	Q216-E240	residue_range	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+254	263	α-helix 1	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+266	275	P248-Q274	residue_range	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+277	286	α-helix 2	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+293	302	E278-T306	residue_range	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+304	313	α-helix 3	structure_element	The Tom1 GAT structural restraints yielded ten helical structures (Fig. 2A,B) with a root mean square deviation (RMSD) of 0.9 Å for backbone and 1.3 Å for all heavy atoms (Table 1) and estimated the presence of three helices spanning residues Q216-E240 (α-helix 1), P248-Q274 (α-helix 2), and E278-T306 (α-helix 3).	TABLE
+7	16	ubiquitin	chemical	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
+74	78	Tom1	protein	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
+79	82	GAT	structure_element	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
+83	100	α-helices 1 and 2	structure_element	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
+112	118	Tollip	protein	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
+119	122	TBD	structure_element	Unlike ubiquitin binding, data suggest that conformational changes of the Tom1 GAT α-helices 1 and 2 occur upon Tollip TBD binding (Fig. 3A,B).	TABLE
+15	24	far-UV CD	experimental_method	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
+25	33	spectrum	evidence	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
+41	45	His-	experimental_method	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
+45	49	Tom1	protein	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
+50	53	GAT	structure_element	Representative far-UV CD spectrum of the His-Tom1 GAT domain.	FIG
+40	62	backbone superposition	experimental_method	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
+78	88	structures	evidence	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
+97	101	Tom1	protein	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
+102	105	GAT	structure_element	(A) Stereo view displaying the best-fit backbone superposition of the refined structures for the Tom1 GAT domain.	FIG
+96	100	Tom1	protein	Helices are shown in orange, whereas loops are colored in green. (B) Ribbon illustration of the Tom1 GAT domain.	FIG
+101	104	GAT	structure_element	Helices are shown in orange, whereas loops are colored in green. (B) Ribbon illustration of the Tom1 GAT domain.	FIG
+21	44	superimposed structures	experimental_method	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+52	56	Tom1	protein	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+57	60	GAT	structure_element	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+75	79	free	protein_state	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+110	116	Tollip	protein	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+117	126	TBD-bound	protein_state	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+161	184	superimposed structures	experimental_method	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+192	196	Tom1	protein	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+197	200	GAT	structure_element	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+232	240	Ub-bound	protein_state	(A) Two views of the superimposed structures of the Tom1 GAT domain in the free state (gray) with that in the Tollip TBD-bound state (red). (B) Two views of the superimposed structures of the Tom1 GAT domain (gray) with that in the Ub-bound state (green).	FIG
+0	3	NMR	experimental_method	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
+8	29	refinement statistics	evidence	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
+38	42	Tom1	protein	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
+43	46	GAT	structure_element	NMR and refinement statistics for the Tom1 GAT domain.	TABLE
+0	3	NMR	experimental_method	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
+4	25	structural statistics	evidence	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
+58	62	Tom1	protein	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
+63	66	GAT	structure_element	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
+73	77	PSVS	experimental_method	NMR structural statistics for lowest energy conformers of Tom1 GAT using PSVS.	TABLE
+28	41	superimposing	experimental_method	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
+51	58	215–309	residue_range	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
+62	66	Tom1	protein	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
+67	70	GAT	structure_element	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE
+102	112	structures	evidence	deviations were obtained by superimposing residues 215–309 of Tom1 GAT among 10 lowest energy refined structures.	TABLE

annotation_CSV/PMC4871749.csv

@@ -0,0 +1,412 @@
+anno_start	anno_end	anno_text	entity_type	sentence	section
+4	9	Taf14	protein	The Taf14 YEATS domain is a reader of histone crotonylation	TITLE
+10	22	YEATS domain	structure_element	The Taf14 YEATS domain is a reader of histone crotonylation	TITLE
+38	45	histone	protein_type	The Taf14 YEATS domain is a reader of histone crotonylation	TITLE
+46	59	crotonylation	ptm	The Taf14 YEATS domain is a reader of histone crotonylation	TITLE
+21	28	histone	protein_type	The discovery of new histone modifications is unfolding at startling rates, however, the identification of effectors capable of interpreting these modifications has lagged behind.	ABSTRACT
+19	31	YEATS domain	structure_element	Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription.	ABSTRACT
+58	65	histone	protein_type	Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription.	ABSTRACT
+66	72	lysine	residue_name	Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription.	ABSTRACT
+73	86	crotonylation	ptm	Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription.	ABSTRACT
+17	22	Taf14	protein	We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.	ABSTRACT
+23	35	YEATS domain	structure_element	We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.	ABSTRACT
+44	58	crotonyllysine	residue_name	We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.	ABSTRACT
+72	86	π-π-π-stacking	bond_interaction	We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.	ABSTRACT
+112	125	YEATS domains	structure_element	We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.	ABSTRACT
+131	145	crotonyllysine	residue_name	We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.	ABSTRACT
+0	13	Crotonylation	ptm	Crotonylation of lysine residues (crotonyllysine, Kcr) has emerged as one of the fundamental histone post-translational modifications (PTMs) found in mammalian chromatin.	INTRO
+17	23	lysine	residue_name	Crotonylation of lysine residues (crotonyllysine, Kcr) has emerged as one of the fundamental histone post-translational modifications (PTMs) found in mammalian chromatin.	INTRO
+34	48	crotonyllysine	residue_name	Crotonylation of lysine residues (crotonyllysine, Kcr) has emerged as one of the fundamental histone post-translational modifications (PTMs) found in mammalian chromatin.	INTRO
+50	53	Kcr	residue_name	Crotonylation of lysine residues (crotonyllysine, Kcr) has emerged as one of the fundamental histone post-translational modifications (PTMs) found in mammalian chromatin.	INTRO
+93	100	histone	protein_type	Crotonylation of lysine residues (crotonyllysine, Kcr) has emerged as one of the fundamental histone post-translational modifications (PTMs) found in mammalian chromatin.	INTRO
+150	159	mammalian	taxonomy_domain	Crotonylation of lysine residues (crotonyllysine, Kcr) has emerged as one of the fundamental histone post-translational modifications (PTMs) found in mammalian chromatin.	INTRO
+4	18	crotonyllysine	residue_name	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+27	34	histone	protein_type	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+35	37	H3	protein_type	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+37	40	K18	residue_name_number	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+56	60	p300	protein	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+64	89	histone acetyltransferase	protein_type	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+111	122	acetylation	ptm	The crotonyllysine mark on histone H3K18 is produced by p300, a histone acetyltransferase also responsible for acetylation of histones.	INTRO
+61	75	crotonyllysine	residue_name	Owing to some differences in their genomic distribution, the crotonyllysine and acetyllysine (Kac) modifications have been linked to distinct functional outcomes.	INTRO
+80	92	acetyllysine	residue_name	Owing to some differences in their genomic distribution, the crotonyllysine and acetyllysine (Kac) modifications have been linked to distinct functional outcomes.	INTRO
+94	97	Kac	residue_name	Owing to some differences in their genomic distribution, the crotonyllysine and acetyllysine (Kac) modifications have been linked to distinct functional outcomes.	INTRO
+0	4	p300	protein	p300-catalyzed histone crotonylation, which is likely metabolically regulated, stimulates transcription to a greater degree than p300-catalyzed acetylation.	INTRO
+15	22	histone	protein_type	p300-catalyzed histone crotonylation, which is likely metabolically regulated, stimulates transcription to a greater degree than p300-catalyzed acetylation.	INTRO
+23	36	crotonylation	ptm	p300-catalyzed histone crotonylation, which is likely metabolically regulated, stimulates transcription to a greater degree than p300-catalyzed acetylation.	INTRO
+129	133	p300	protein	p300-catalyzed histone crotonylation, which is likely metabolically regulated, stimulates transcription to a greater degree than p300-catalyzed acetylation.	INTRO
+144	155	acetylation	ptm	p300-catalyzed histone crotonylation, which is likely metabolically regulated, stimulates transcription to a greater degree than p300-catalyzed acetylation.	INTRO
+53	67	crotonyllysine	residue_name	The discovery of individual biological roles for the crotonyllysine and acetyllysine marks suggests that these PTMs can be read by distinct readers.	INTRO
+72	84	acetyllysine	residue_name	The discovery of individual biological roles for the crotonyllysine and acetyllysine marks suggests that these PTMs can be read by distinct readers.	INTRO
+18	30	acetyllysine	residue_name	While a number of acetyllysine readers have been identified and characterized, a specific reader of the crotonyllysine mark remains unknown (reviewed in).	INTRO
+104	118	crotonyllysine	residue_name	While a number of acetyllysine readers have been identified and characterized, a specific reader of the crotonyllysine mark remains unknown (reviewed in).	INTRO
+19	31	bromodomains	structure_element	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+33	36	BDs	structure_element	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+65	67	BD	structure_element	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+98	110	crotonylated	protein_state	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+153	163	acetylated	protein_state	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+189	201	bromodomains	structure_element	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+242	256	crotonyllysine	residue_name	A recent survey of bromodomains (BDs) demonstrates that only one BD associates very weakly with a crotonylated peptide, however it binds more tightly to acetylated peptides, inferring that bromodomains do not possess physiologically relevant crotonyllysine binding activity.	INTRO
+14	26	acetyllysine	residue_name	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+81	86	YEATS	structure_element	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+88	92	Yaf9	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+94	97	ENL	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+99	102	AF9	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+104	109	Taf14	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+111	115	Sas5	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+128	133	human	species	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+134	137	AF9	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+142	147	yeast	taxonomy_domain	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+148	153	Taf14	protein	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+185	192	histone	protein_type	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+198	200	H3	protein_type	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+200	204	K9ac	ptm	The family of acetyllysine readers has been expanded with the discovery that the YEATS (Yaf9, ENL, AF9, Taf14, Sas5) domains of human AF9 and yeast Taf14 are capable of recognizing the histone mark H3K9ac.	INTRO
+4	16	acetyllysine	residue_name	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+41	44	AF9	protein	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+45	57	YEATS domain	structure_element	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+98	123	histone methyltransferase	protein_type	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+124	129	DOT1L	protein	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+133	135	H3	protein_type	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+135	139	K9ac	ptm	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+169	174	DOT1L	protein	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+184	186	H3	protein_type	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+186	189	K79	residue_name_number	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+190	201	methylation	ptm	The acetyllysine binding function of the AF9 YEATS domain is essential for the recruitment of the histone methyltransferase DOT1L to H3K9ac-containing chromatin and for DOT1L-mediated H3K79 methylation and transcription.	INTRO
+68	73	yeast	taxonomy_domain	Similarly, activation of a subset of genes and DNA damage repair in yeast require the acetyllysine binding activity of the Taf14 YEATS domain.	INTRO
+86	98	acetyllysine	residue_name	Similarly, activation of a subset of genes and DNA damage repair in yeast require the acetyllysine binding activity of the Taf14 YEATS domain.	INTRO
+123	128	Taf14	protein	Similarly, activation of a subset of genes and DNA damage repair in yeast require the acetyllysine binding activity of the Taf14 YEATS domain.	INTRO
+129	141	YEATS domain	structure_element	Similarly, activation of a subset of genes and DNA damage repair in yeast require the acetyllysine binding activity of the Taf14 YEATS domain.	INTRO
+45	50	Taf14	protein	Consistent with its role in gene regulation, Taf14 was identified as a core component of the transcription factor complexes TFIID and TFIIF.	INTRO
+124	129	TFIID	complex_assembly	Consistent with its role in gene regulation, Taf14 was identified as a core component of the transcription factor complexes TFIID and TFIIF.	INTRO
+134	139	TFIIF	complex_assembly	Consistent with its role in gene regulation, Taf14 was identified as a core component of the transcription factor complexes TFIID and TFIIF.	INTRO
+9	14	Taf14	protein	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+82	87	INO80	complex_assembly	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+89	96	SWI/SNF	complex_assembly	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+101	104	RSC	complex_assembly	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+114	139	histone acetyltransferase	protein_type	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+148	152	NuA3	complex_assembly	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+188	193	Taf14	protein	However, Taf14 is also found in a number of chromatin-remodeling complexes (i.e., INO80, SWI/SNF and RSC) and the histone acetyltransferase complex NuA3, indicating a multifaceted role of Taf14 in transcriptional regulation and chromatin biology.	INTRO
+33	38	Taf14	protein	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+39	51	YEATS domain	structure_element	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+67	81	crotonyllysine	residue_name	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+96	103	histone	protein_type	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+104	106	H3	protein_type	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+107	119	crotonylated	protein_state	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+123	131	lysine 9	residue_name_number	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+133	135	H3	protein_type	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+135	139	K9cr	ptm	In this study, we identified the Taf14 YEATS domain as a reader of crotonyllysine that binds to histone H3 crotonylated at lysine 9 (H3K9cr) via a distinctive binding mechanism.	INTRO
+14	16	H3	protein_type	We found that H3K9cr is present in yeast and is dynamically regulated.	INTRO
+16	20	K9cr	ptm	We found that H3K9cr is present in yeast and is dynamically regulated.	INTRO
+35	40	yeast	taxonomy_domain	We found that H3K9cr is present in yeast and is dynamically regulated.	INTRO
+56	58	H3	protein_type	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+58	62	K9cr	ptm	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+83	100	crystal structure	evidence	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+108	113	Taf14	protein	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+114	126	YEATS domain	structure_element	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+127	142	in complex with	protein_state	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+143	153	H3K9cr5-13	chemical	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+164	168	5–13	residue_range	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+172	174	H3	protein_type	To elucidate the molecular basis for recognition of the H3K9cr mark, we obtained a crystal structure of the Taf14 YEATS domain in complex with H3K9cr5-13 (residues 5–13 of H3) peptide (Fig. 1, Supplementary Results, Supplementary Fig. 1 and Supplementary Table 1).	INTRO
+4	9	Taf14	protein	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+10	22	YEATS domain	structure_element	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+33	66	immunoglobin-like β sandwich fold	structure_element	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+84	107	anti-parallel β strands	structure_element	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+124	129	loops	structure_element	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+142	154	binding site	site	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+159	161	H3	protein_type	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+161	165	K9cr	ptm	The Taf14 YEATS domain adopts an immunoglobin-like β sandwich fold containing eight anti-parallel β strands linked by short loops that form a binding site for H3K9cr (Fig. 1b).	INTRO
+4	6	H3	protein_type	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+6	10	K9cr	ptm	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+30	51	extended conformation	protein_state	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+88	97	β strands	structure_element	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+159	164	water	chemical	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+174	188	hydrogen bonds	bond_interaction	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+195	206	salt bridge	bond_interaction	The H3K9cr peptide lays in an extended conformation in an orientation orthogonal to the β strands and is stabilized through an extensive network of direct and water-mediated hydrogen bonds and a salt bridge (Fig. 1c).	INTRO
+33	47	crotonyllysine	residue_name	The most striking feature of the crotonyllysine recognition mechanism is the unique coordination of crotonylated lysine residue.	INTRO
+100	112	crotonylated	protein_state	The most striking feature of the crotonyllysine recognition mechanism is the unique coordination of crotonylated lysine residue.	INTRO
+113	119	lysine	residue_name	The most striking feature of the crotonyllysine recognition mechanism is the unique coordination of crotonylated lysine residue.	INTRO
+33	37	K9cr	ptm	The fully extended side chain of K9cr transverses the narrow tunnel, crossing the β sandwich at right angle in a corkscrew-like manner (Fig. 1b and Supplementary Figure 1b).	INTRO
+82	92	β sandwich	structure_element	The fully extended side chain of K9cr transverses the narrow tunnel, crossing the β sandwich at right angle in a corkscrew-like manner (Fig. 1b and Supplementary Figure 1b).	INTRO
+11	19	crotonyl	chemical	The planar crotonyl group is inserted between Trp81 and Phe62 of the protein, the aromatic rings of which are positioned strictly parallel to each other and at equal distance from the crotonyl group, yielding a novel aromatic-amide/aliphatic-aromatic π-π-π-stacking system that, to our knowledge, has not been reported previously for any protein-protein interaction (Fig. 1d and Supplementary Fig. 1c).	INTRO
+46	51	Trp81	residue_name_number	The planar crotonyl group is inserted between Trp81 and Phe62 of the protein, the aromatic rings of which are positioned strictly parallel to each other and at equal distance from the crotonyl group, yielding a novel aromatic-amide/aliphatic-aromatic π-π-π-stacking system that, to our knowledge, has not been reported previously for any protein-protein interaction (Fig. 1d and Supplementary Fig. 1c).	INTRO
+56	61	Phe62	residue_name_number	The planar crotonyl group is inserted between Trp81 and Phe62 of the protein, the aromatic rings of which are positioned strictly parallel to each other and at equal distance from the crotonyl group, yielding a novel aromatic-amide/aliphatic-aromatic π-π-π-stacking system that, to our knowledge, has not been reported previously for any protein-protein interaction (Fig. 1d and Supplementary Fig. 1c).	INTRO
+184	192	crotonyl	chemical	The planar crotonyl group is inserted between Trp81 and Phe62 of the protein, the aromatic rings of which are positioned strictly parallel to each other and at equal distance from the crotonyl group, yielding a novel aromatic-amide/aliphatic-aromatic π-π-π-stacking system that, to our knowledge, has not been reported previously for any protein-protein interaction (Fig. 1d and Supplementary Fig. 1c).	INTRO
+251	265	π-π-π-stacking	bond_interaction	The planar crotonyl group is inserted between Trp81 and Phe62 of the protein, the aromatic rings of which are positioned strictly parallel to each other and at equal distance from the crotonyl group, yielding a novel aromatic-amide/aliphatic-aromatic π-π-π-stacking system that, to our knowledge, has not been reported previously for any protein-protein interaction (Fig. 1d and Supplementary Fig. 1c).	INTRO
+18	23	Trp81	residue_name_number	The side chain of Trp81 appears to adopt two conformations, one of which provides maximum π-stacking with the alkene functional group while the other rotamer affords maximum π-stacking with the amide π electrons (Supplementary Fig. 1c).	INTRO
+90	100	π-stacking	bond_interaction	The side chain of Trp81 appears to adopt two conformations, one of which provides maximum π-stacking with the alkene functional group while the other rotamer affords maximum π-stacking with the amide π electrons (Supplementary Fig. 1c).	INTRO
+174	184	π-stacking	bond_interaction	The side chain of Trp81 appears to adopt two conformations, one of which provides maximum π-stacking with the alkene functional group while the other rotamer affords maximum π-stacking with the amide π electrons (Supplementary Fig. 1c).	INTRO
+25	30	Trp81	residue_name_number	The dual conformation of Trp81 is likely due to the conjugated nature of the C=C and C=O π-orbitals within the crotonyl functional group.	INTRO
+111	119	crotonyl	chemical	The dual conformation of Trp81 is likely due to the conjugated nature of the C=C and C=O π-orbitals within the crotonyl functional group.	INTRO
+15	29	π-π-π stacking	bond_interaction	In addition to π-π-π stacking, the crotonyl group is stabilized by a set of hydrogen bonds and electrostatic interactions.	INTRO
+35	43	crotonyl	chemical	In addition to π-π-π stacking, the crotonyl group is stabilized by a set of hydrogen bonds and electrostatic interactions.	INTRO
+76	90	hydrogen bonds	bond_interaction	In addition to π-π-π stacking, the crotonyl group is stabilized by a set of hydrogen bonds and electrostatic interactions.	INTRO
+95	121	electrostatic interactions	bond_interaction	In addition to π-π-π stacking, the crotonyl group is stabilized by a set of hydrogen bonds and electrostatic interactions.	INTRO
+4	10	π bond	bond_interaction	The π bond conjugation of the crotonyl group gives rise to a dipole moment of the alkene moiety, resulting in a partial positive charge on the β-carbon (Cβ) and a partial negative charge on the α-carbon (Cα).	INTRO
+30	38	crotonyl	chemical	The π bond conjugation of the crotonyl group gives rise to a dipole moment of the alkene moiety, resulting in a partial positive charge on the β-carbon (Cβ) and a partial negative charge on the α-carbon (Cα).	INTRO
+59	81	electrostatic contacts	bond_interaction	This provides the capability for the alkene moiety to form electrostatic contacts, as Cα and Cβ lay within electrostatic interaction distances of the carbonyl oxygen of Gln79 and of the hydroxyl group of Thr61, respectively.	INTRO
+107	132	electrostatic interaction	bond_interaction	This provides the capability for the alkene moiety to form electrostatic contacts, as Cα and Cβ lay within electrostatic interaction distances of the carbonyl oxygen of Gln79 and of the hydroxyl group of Thr61, respectively.	INTRO
+169	174	Gln79	residue_name_number	This provides the capability for the alkene moiety to form electrostatic contacts, as Cα and Cβ lay within electrostatic interaction distances of the carbonyl oxygen of Gln79 and of the hydroxyl group of Thr61, respectively.	INTRO
+204	209	Thr61	residue_name_number	This provides the capability for the alkene moiety to form electrostatic contacts, as Cα and Cβ lay within electrostatic interaction distances of the carbonyl oxygen of Gln79 and of the hydroxyl group of Thr61, respectively.	INTRO
+22	27	Thr61	residue_name_number	The hydroxyl group of Thr61 also participates in a hydrogen bond with the amide nitrogen of the K9cr side chain (Fig. 1d).	INTRO
+51	64	hydrogen bond	bond_interaction	The hydroxyl group of Thr61 also participates in a hydrogen bond with the amide nitrogen of the K9cr side chain (Fig. 1d).	INTRO
+96	100	K9cr	ptm	The hydroxyl group of Thr61 also participates in a hydrogen bond with the amide nitrogen of the K9cr side chain (Fig. 1d).	INTRO
+26	31	Thr61	residue_name_number	The fixed position of the Thr61 hydroxyl group, which facilitates interactions with both the amide and Cα of K9cr, is achieved through a hydrogen bond with imidazole ring of His59.	INTRO
+109	113	K9cr	ptm	The fixed position of the Thr61 hydroxyl group, which facilitates interactions with both the amide and Cα of K9cr, is achieved through a hydrogen bond with imidazole ring of His59.	INTRO
+137	150	hydrogen bond	bond_interaction	The fixed position of the Thr61 hydroxyl group, which facilitates interactions with both the amide and Cα of K9cr, is achieved through a hydrogen bond with imidazole ring of His59.	INTRO
+174	179	His59	residue_name_number	The fixed position of the Thr61 hydroxyl group, which facilitates interactions with both the amide and Cα of K9cr, is achieved through a hydrogen bond with imidazole ring of His59.	INTRO
+23	27	K9cr	ptm	Extra stabilization of K9cr is attained by a hydrogen bond formed between its carbonyl oxygen and the backbone nitrogen of Trp81, as well as a water-mediated hydrogen bond with the backbone carbonyl group of Gly82 (Fig 1d).	INTRO
+45	58	hydrogen bond	bond_interaction	Extra stabilization of K9cr is attained by a hydrogen bond formed between its carbonyl oxygen and the backbone nitrogen of Trp81, as well as a water-mediated hydrogen bond with the backbone carbonyl group of Gly82 (Fig 1d).	INTRO
+123	128	Trp81	residue_name_number	Extra stabilization of K9cr is attained by a hydrogen bond formed between its carbonyl oxygen and the backbone nitrogen of Trp81, as well as a water-mediated hydrogen bond with the backbone carbonyl group of Gly82 (Fig 1d).	INTRO
+143	148	water	chemical	Extra stabilization of K9cr is attained by a hydrogen bond formed between its carbonyl oxygen and the backbone nitrogen of Trp81, as well as a water-mediated hydrogen bond with the backbone carbonyl group of Gly82 (Fig 1d).	INTRO
+158	171	hydrogen bond	bond_interaction	Extra stabilization of K9cr is attained by a hydrogen bond formed between its carbonyl oxygen and the backbone nitrogen of Trp81, as well as a water-mediated hydrogen bond with the backbone carbonyl group of Gly82 (Fig 1d).	INTRO
+208	213	Gly82	residue_name_number	Extra stabilization of K9cr is attained by a hydrogen bond formed between its carbonyl oxygen and the backbone nitrogen of Trp81, as well as a water-mediated hydrogen bond with the backbone carbonyl group of Gly82 (Fig 1d).	INTRO
+64	69	Taf14	protein	This distinctive mechanism was corroborated through mapping the Taf14 YEATS-H3K9cr binding interface in solution using NMR chemical shift perturbation analysis (Supplementary Fig. 2a, b).	INTRO
+70	100	YEATS-H3K9cr binding interface	site	This distinctive mechanism was corroborated through mapping the Taf14 YEATS-H3K9cr binding interface in solution using NMR chemical shift perturbation analysis (Supplementary Fig. 2a, b).	INTRO
+119	159	NMR chemical shift perturbation analysis	experimental_method	This distinctive mechanism was corroborated through mapping the Taf14 YEATS-H3K9cr binding interface in solution using NMR chemical shift perturbation analysis (Supplementary Fig. 2a, b).	INTRO
+15	20	Taf14	protein	Binding of the Taf14 YEATS domain to H3K9cr is robust.	INTRO
+21	33	YEATS domain	structure_element	Binding of the Taf14 YEATS domain to H3K9cr is robust.	INTRO
+37	39	H3	protein_type	Binding of the Taf14 YEATS domain to H3K9cr is robust.	INTRO
+39	43	K9cr	ptm	Binding of the Taf14 YEATS domain to H3K9cr is robust.	INTRO
+4	25	dissociation constant	evidence	The dissociation constant (Kd) for the Taf14 YEATS-H3K9cr5-13 complex was found to be 9.5 μM, as measured by fluorescence spectroscopy (Supplementary Fig. 2c).	INTRO
+27	29	Kd	evidence	The dissociation constant (Kd) for the Taf14 YEATS-H3K9cr5-13 complex was found to be 9.5 μM, as measured by fluorescence spectroscopy (Supplementary Fig. 2c).	INTRO
+39	61	Taf14 YEATS-H3K9cr5-13	complex_assembly	The dissociation constant (Kd) for the Taf14 YEATS-H3K9cr5-13 complex was found to be 9.5 μM, as measured by fluorescence spectroscopy (Supplementary Fig. 2c).	INTRO
+109	134	fluorescence spectroscopy	experimental_method	The dissociation constant (Kd) for the Taf14 YEATS-H3K9cr5-13 complex was found to be 9.5 μM, as measured by fluorescence spectroscopy (Supplementary Fig. 2c).	INTRO
+30	48	binding affinities	evidence	This value is in the range of binding affinities exhibited by the majority of histone readers, thus attesting to the physiological relevance of the H3K9cr recognition by Taf14.	INTRO
+148	150	H3	protein_type	This value is in the range of binding affinities exhibited by the majority of histone readers, thus attesting to the physiological relevance of the H3K9cr recognition by Taf14.	INTRO
+150	154	K9cr	ptm	This value is in the range of binding affinities exhibited by the majority of histone readers, thus attesting to the physiological relevance of the H3K9cr recognition by Taf14.	INTRO
+170	175	Taf14	protein	This value is in the range of binding affinities exhibited by the majority of histone readers, thus attesting to the physiological relevance of the H3K9cr recognition by Taf14.	INTRO
+21	23	H3	protein_type	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+23	27	K9cr	ptm	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+42	47	yeast	taxonomy_domain	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+62	81	whole cell extracts	experimental_method	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+111	116	yeast	taxonomy_domain	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+145	166	Western blot analysis	experimental_method	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+201	203	H3	protein_type	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+203	207	K9cr	ptm	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+209	211	H3	protein_type	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+211	215	K9ac	ptm	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+220	222	H3	protein_type	To determine whether H3K9cr is present in yeast, we generated whole cell extracts from logarithmically growing yeast cells and subjected them to Western blot analysis using antibodies directed towards H3K9cr, H3K9ac and H3 (Fig. 2a, b, Supplementary Fig. 3 and Supplementary Table 2).	INTRO
+5	7	H3	protein_type	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+7	11	K9cr	ptm	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+16	18	H3	protein_type	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+18	22	K9ac	ptm	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+40	45	yeast	taxonomy_domain	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+46	54	histones	protein_type	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+102	104	H3	protein_type	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+104	108	K9cr	ptm	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+122	127	yeast	taxonomy_domain	Both H3K9cr and H3K9ac were detected in yeast histones; to our knowledge, this is the first report of H3K9cr occurring in yeast.	INTRO
+17	19	H3	protein_type	We next asked if H3K9cr is regulated by the actions of histone acetyltransferases (HATs) and histone deacetylases (HDACs).	INTRO
+19	23	K9cr	ptm	We next asked if H3K9cr is regulated by the actions of histone acetyltransferases (HATs) and histone deacetylases (HDACs).	INTRO
+55	81	histone acetyltransferases	protein_type	We next asked if H3K9cr is regulated by the actions of histone acetyltransferases (HATs) and histone deacetylases (HDACs).	INTRO
+83	87	HATs	protein_type	We next asked if H3K9cr is regulated by the actions of histone acetyltransferases (HATs) and histone deacetylases (HDACs).	INTRO
+93	113	histone deacetylases	protein_type	We next asked if H3K9cr is regulated by the actions of histone acetyltransferases (HATs) and histone deacetylases (HDACs).	INTRO
+115	120	HDACs	protein_type	We next asked if H3K9cr is regulated by the actions of histone acetyltransferases (HATs) and histone deacetylases (HDACs).	INTRO
+50	55	yeast	taxonomy_domain	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+77	82	yeast	taxonomy_domain	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+83	87	HATs	protein_type	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+89	93	HAT1	protein	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+95	99	Gcn5	protein	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+105	111	Rtt109	protein	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+116	121	HDACs	protein_type	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+123	127	Rpd3	protein	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+129	133	Hos1	protein	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+139	143	Hos2	protein	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+150	157	deleted	experimental_method	Towards this end, we probed extracts derived from yeast cells in which major yeast HATs (HAT1, Gcn5, and Rtt109) or HDACs (Rpd3, Hos1, and Hos2) were deleted.	INTRO
+52	54	H3	protein_type	As shown in Figure 2a, b and Supplementary Fig. 3e, H3K9cr levels were abolished or reduced considerably in the HAT deletion strains, whereas they were dramatically increased in the HDAC deletion strains.	INTRO
+54	58	K9cr	ptm	As shown in Figure 2a, b and Supplementary Fig. 3e, H3K9cr levels were abolished or reduced considerably in the HAT deletion strains, whereas they were dramatically increased in the HDAC deletion strains.	INTRO
+112	115	HAT	protein_type	As shown in Figure 2a, b and Supplementary Fig. 3e, H3K9cr levels were abolished or reduced considerably in the HAT deletion strains, whereas they were dramatically increased in the HDAC deletion strains.	INTRO
+116	124	deletion	experimental_method	As shown in Figure 2a, b and Supplementary Fig. 3e, H3K9cr levels were abolished or reduced considerably in the HAT deletion strains, whereas they were dramatically increased in the HDAC deletion strains.	INTRO
+182	186	HDAC	protein_type	As shown in Figure 2a, b and Supplementary Fig. 3e, H3K9cr levels were abolished or reduced considerably in the HAT deletion strains, whereas they were dramatically increased in the HDAC deletion strains.	INTRO
+187	195	deletion	experimental_method	As shown in Figure 2a, b and Supplementary Fig. 3e, H3K9cr levels were abolished or reduced considerably in the HAT deletion strains, whereas they were dramatically increased in the HDAC deletion strains.	INTRO
+33	35	H3	protein_type	Furthermore, fluctuations in the H3K9cr levels were more substantial than fluctuations in the corresponding H3K9ac levels.	INTRO
+35	39	K9cr	ptm	Furthermore, fluctuations in the H3K9cr levels were more substantial than fluctuations in the corresponding H3K9ac levels.	INTRO
+108	110	H3	protein_type	Furthermore, fluctuations in the H3K9cr levels were more substantial than fluctuations in the corresponding H3K9ac levels.	INTRO
+110	114	K9ac	ptm	Furthermore, fluctuations in the H3K9cr levels were more substantial than fluctuations in the corresponding H3K9ac levels.	INTRO
+36	38	H3	protein_type	Together, these results reveal that H3K9cr is a dynamic mark of chromatin in yeast and suggest an important role for this modification in transcription as it is regulated by HATs and HDACs.	INTRO
+38	42	K9cr	ptm	Together, these results reveal that H3K9cr is a dynamic mark of chromatin in yeast and suggest an important role for this modification in transcription as it is regulated by HATs and HDACs.	INTRO
+77	82	yeast	taxonomy_domain	Together, these results reveal that H3K9cr is a dynamic mark of chromatin in yeast and suggest an important role for this modification in transcription as it is regulated by HATs and HDACs.	INTRO
+174	178	HATs	protein_type	Together, these results reveal that H3K9cr is a dynamic mark of chromatin in yeast and suggest an important role for this modification in transcription as it is regulated by HATs and HDACs.	INTRO
+183	188	HDACs	protein_type	Together, these results reveal that H3K9cr is a dynamic mark of chromatin in yeast and suggest an important role for this modification in transcription as it is regulated by HATs and HDACs.	INTRO
+36	46	acetylated	protein_state	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+47	54	histone	protein_type	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+66	71	Taf14	protein	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+72	84	YEATS domain	structure_element	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+93	103	acetylated	protein_state	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+104	106	H3	protein_type	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+106	108	K9	residue_name_number	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+163	165	H3	protein_type	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+165	169	K9cr	ptm	We have previously shown that among acetylated histone marks, the Taf14 YEATS domain prefers acetylated H3K9 (also see Supplementary Fig. 3b), however it binds to H3K9cr tighter.	INTRO
+19	24	Taf14	protein	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+33	47	crotonyllysine	residue_name	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+69	80	1H,15N HSQC	experimental_method	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+110	120	H3K9cr5-13	chemical	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+124	134	H3K9ac5-13	chemical	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+147	155	titrated	experimental_method	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+165	176	15N-labeled	protein_state	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+177	182	Taf14	protein	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+183	195	YEATS domain	structure_element	The selectivity of Taf14 towards crotonyllysine was substantiated by 1H,15N HSQC experiments, in which either H3K9cr5-13 or H3K9ac5-13 peptide was titrated into the 15N-labeled Taf14 YEATS domain (Fig. 2c and Supplementary Fig. 4a, b).	INTRO
+11	13	H3	protein_type	Binding of H3K9cr induced resonance changes in slow exchange regime on the NMR time scale, indicative of strong interaction.	INTRO
+13	17	K9cr	ptm	Binding of H3K9cr induced resonance changes in slow exchange regime on the NMR time scale, indicative of strong interaction.	INTRO
+26	43	resonance changes	evidence	Binding of H3K9cr induced resonance changes in slow exchange regime on the NMR time scale, indicative of strong interaction.	INTRO
+75	78	NMR	experimental_method	Binding of H3K9cr induced resonance changes in slow exchange regime on the NMR time scale, indicative of strong interaction.	INTRO
+24	26	H3	protein_type	In contrast, binding of H3K9ac resulted in an intermediate exchange, which is characteristic of a weaker association.	INTRO
+26	30	K9ac	ptm	In contrast, binding of H3K9ac resulted in an intermediate exchange, which is characteristic of a weaker association.	INTRO
+13	23	crosspeaks	evidence	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+27	32	Gly80	residue_name_number	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+37	42	Trp81	residue_name_number	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+50	62	YEATS domain	structure_element	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+90	92	H3	protein_type	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+92	96	K9cr	ptm	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+101	103	H3	protein_type	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+103	107	K9ac	ptm	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+171	218	crotonyllysine and acetyllysine binding pockets	site	Furthermore, crosspeaks of Gly80 and Trp81 of the YEATS domain were uniquely perturbed by H3K9cr and H3K9ac, indicating a different chemical environment in the respective crotonyllysine and acetyllysine binding pockets (Supplementary Fig. 4a).	INTRO
+41	46	Trp81	residue_name_number	These differences support our model that Trp81 adopts two conformations upon complex formation with the H3K9cr mark as compared to H3K9ac (Supplementary Figs. 1c, d and 4c).	INTRO
+104	106	H3	protein_type	These differences support our model that Trp81 adopts two conformations upon complex formation with the H3K9cr mark as compared to H3K9ac (Supplementary Figs. 1c, d and 4c).	INTRO
+106	110	K9cr	ptm	These differences support our model that Trp81 adopts two conformations upon complex formation with the H3K9cr mark as compared to H3K9ac (Supplementary Figs. 1c, d and 4c).	INTRO
+131	133	H3	protein_type	These differences support our model that Trp81 adopts two conformations upon complex formation with the H3K9cr mark as compared to H3K9ac (Supplementary Figs. 1c, d and 4c).	INTRO
+133	137	K9ac	ptm	These differences support our model that Trp81 adopts two conformations upon complex formation with the H3K9cr mark as compared to H3K9ac (Supplementary Figs. 1c, d and 4c).	INTRO
+136	148	YEATS-H3K9cr	complex_assembly	One of the conformations, characterized by the π stacking involving two aromatic residues and the alkene group, is observed only in the YEATS-H3K9cr complex.	INTRO
+25	30	Taf14	protein	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+31	43	YEATS domain	structure_element	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+91	101	acyllysine	residue_name	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+122	147	solution pull-down assays	experimental_method	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+154	156	H3	protein_type	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+166	176	acetylated	protein_state	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+178	191	propionylated	protein_state	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+193	204	butyrylated	protein_state	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+210	222	crotonylated	protein_state	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+226	234	lysine 9	residue_name_number	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+245	249	1–20	residue_range	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+253	255	H3	protein_type	To establish whether the Taf14 YEATS domain is able to recognize other recently identified acyllysine marks, we performed solution pull-down assays using H3 peptides acetylated, propionylated, butyrylated, and crotonylated at lysine 9 (residues 1–20 of H3).	INTRO
+53	58	Taf14	protein	As shown in Figure 2d and Supplementary Fig. 5a, the Taf14 YEATS domain binds more strongly to H3K9cr1-20, as compared to other acylated histone peptides.	INTRO
+59	71	YEATS domain	structure_element	As shown in Figure 2d and Supplementary Fig. 5a, the Taf14 YEATS domain binds more strongly to H3K9cr1-20, as compared to other acylated histone peptides.	INTRO
+95	105	H3K9cr1-20	chemical	As shown in Figure 2d and Supplementary Fig. 5a, the Taf14 YEATS domain binds more strongly to H3K9cr1-20, as compared to other acylated histone peptides.	INTRO
+128	136	acylated	protein_state	As shown in Figure 2d and Supplementary Fig. 5a, the Taf14 YEATS domain binds more strongly to H3K9cr1-20, as compared to other acylated histone peptides.	INTRO
+19	21	H3	protein_type	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+21	25	K9cr	ptm	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+31	33	H3	protein_type	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+33	37	K9ac	ptm	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+39	41	H3	protein_type	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+41	45	K9pr	ptm	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+50	52	H3	protein_type	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+52	56	K9bu	ptm	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+74	107	1H,15N HSQC titration experiments	experimental_method	The preference for H3K9cr over H3K9ac, H3K9pr and H3K9bu was supported by 1H,15N HSQC titration experiments.	INTRO
+12	22	H3K9ac1-20	chemical	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+24	34	H3K9pr1-20	chemical	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+40	50	H3K9bu1-20	chemical	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+67	95	chemical shift perturbations	evidence	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+103	108	Taf14	protein	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+109	121	YEATS domain	structure_element	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+236	246	H3K9cr1-20	chemical	Addition of H3K9ac1-20, H3K9pr1-20, and H3K9bu1-20 peptides caused chemical shift perturbations in the Taf14 YEATS domain in intermediate exchange regime, implying that these interactions are weaker compared to the interaction with the H3K9cr1-20 peptide (Supplementary Fig. 5b).	INTRO
+18	20	H3	protein_type	We concluded that H3K9cr is the preferred target of this domain.	INTRO
+20	24	K9cr	ptm	We concluded that H3K9cr is the preferred target of this domain.	INTRO
+5	36	comparative structural analysis	experimental_method	From comparative structural analysis of the YEATS complexes, Gly80 emerged as candidate residue potentially responsible for the preference for crotonyllysine.	INTRO
+61	66	Gly80	residue_name_number	From comparative structural analysis of the YEATS complexes, Gly80 emerged as candidate residue potentially responsible for the preference for crotonyllysine.	INTRO
+143	157	crotonyllysine	residue_name	From comparative structural analysis of the YEATS complexes, Gly80 emerged as candidate residue potentially responsible for the preference for crotonyllysine.	INTRO
+123	131	crotonyl	chemical	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+143	150	mutated	protein_state	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+151	156	Gly80	residue_name_number	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+193	203	mutants of	protein_state	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+204	209	Gly80	residue_name_number	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+255	263	acylated	protein_state	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+289	294	Gly80	residue_name_number	In attempt to generate a mutant capable of accommodating a short acetyl moiety but discriminating against a longer, planar crotonyl moiety, we mutated Gly80 to more bulky residues, however all mutants of Gly80 lost their binding activities towards either acylated peptide, suggesting that Gly80 is absolutely required for the interaction.	INTRO
+13	21	mutation	experimental_method	In contrast, mutation of Val24, a residue located on another side of Trp81, had no effect on binding (Fig. 2d and Supplementary Fig. 5a, c).	INTRO
+25	30	Val24	residue_name_number	In contrast, mutation of Val24, a residue located on another side of Trp81, had no effect on binding (Fig. 2d and Supplementary Fig. 5a, c).	INTRO
+69	74	Trp81	residue_name_number	In contrast, mutation of Val24, a residue located on another side of Trp81, had no effect on binding (Fig. 2d and Supplementary Fig. 5a, c).	INTRO
+31	45	crotonyllysine	residue_name	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+49	58	conserved	protein_state	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+70	75	human	species	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+76	89	YEATS domains	structure_element	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+93	114	pull-down experiments	experimental_method	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+141	151	acetylated	protein_state	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+153	166	propionylated	protein_state	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+168	179	butyrylated	protein_state	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+185	197	crotonylated	protein_state	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+198	205	histone	protein_type	To determine if the binding to crotonyllysine is conserved, we tested human YEATS domains by pull-down experiments using singly and multiply acetylated, propionylated, butyrylated, and crotonylated histone peptides (Supplementary Fig. 6).	INTRO
+18	31	YEATS domains	structure_element	We found that all YEATS domains tested are capable of binding to crotonyllysine peptides, though they display variable preferences for the acyl moieties.	INTRO
+65	79	crotonyllysine	residue_name	We found that all YEATS domains tested are capable of binding to crotonyllysine peptides, though they display variable preferences for the acyl moieties.	INTRO
+6	12	YEATS2	protein	While YEATS2 and ENL showed selectivity for the crotonylated peptides, GAS41 and AF9 bound acylated peptides almost equally well.	INTRO
+17	20	ENL	protein	While YEATS2 and ENL showed selectivity for the crotonylated peptides, GAS41 and AF9 bound acylated peptides almost equally well.	INTRO
+48	60	crotonylated	protein_state	While YEATS2 and ENL showed selectivity for the crotonylated peptides, GAS41 and AF9 bound acylated peptides almost equally well.	INTRO
+71	76	GAS41	protein	While YEATS2 and ENL showed selectivity for the crotonylated peptides, GAS41 and AF9 bound acylated peptides almost equally well.	INTRO
+81	84	AF9	protein	While YEATS2 and ENL showed selectivity for the crotonylated peptides, GAS41 and AF9 bound acylated peptides almost equally well.	INTRO
+91	99	acylated	protein_state	While YEATS2 and ENL showed selectivity for the crotonylated peptides, GAS41 and AF9 bound acylated peptides almost equally well.	INTRO
+11	23	YEATS domain	structure_element	Unlike the YEATS domain, a known acetyllysine reader, bromodomain, does not recognize crotonyllysine.	INTRO
+33	52	acetyllysine reader	protein_type	Unlike the YEATS domain, a known acetyllysine reader, bromodomain, does not recognize crotonyllysine.	INTRO
+54	65	bromodomain	structure_element	Unlike the YEATS domain, a known acetyllysine reader, bromodomain, does not recognize crotonyllysine.	INTRO
+86	100	crotonyllysine	residue_name	Unlike the YEATS domain, a known acetyllysine reader, bromodomain, does not recognize crotonyllysine.	INTRO
+26	29	BDs	structure_element	We assayed a large set of BDs in pull-down experiments and found that this module is highly specific for acetyllysine and propionyllysine containing peptides (Supplementary Fig. 7).	INTRO
+33	54	pull-down experiments	experimental_method	We assayed a large set of BDs in pull-down experiments and found that this module is highly specific for acetyllysine and propionyllysine containing peptides (Supplementary Fig. 7).	INTRO
+105	117	acetyllysine	residue_name	We assayed a large set of BDs in pull-down experiments and found that this module is highly specific for acetyllysine and propionyllysine containing peptides (Supplementary Fig. 7).	INTRO
+122	137	propionyllysine	residue_name	We assayed a large set of BDs in pull-down experiments and found that this module is highly specific for acetyllysine and propionyllysine containing peptides (Supplementary Fig. 7).	INTRO
+9	21	bromodomains	structure_element	However, bromodomains did not interact (or associated very weakly) with longer acyl modifications, including crotonyllysine, as in the case of BDs of TAF1 and BRD2, supporting recent reports.	INTRO
+109	123	crotonyllysine	residue_name	However, bromodomains did not interact (or associated very weakly) with longer acyl modifications, including crotonyllysine, as in the case of BDs of TAF1 and BRD2, supporting recent reports.	INTRO
+143	146	BDs	structure_element	However, bromodomains did not interact (or associated very weakly) with longer acyl modifications, including crotonyllysine, as in the case of BDs of TAF1 and BRD2, supporting recent reports.	INTRO
+150	154	TAF1	protein	However, bromodomains did not interact (or associated very weakly) with longer acyl modifications, including crotonyllysine, as in the case of BDs of TAF1 and BRD2, supporting recent reports.	INTRO
+159	163	BRD2	protein	However, bromodomains did not interact (or associated very weakly) with longer acyl modifications, including crotonyllysine, as in the case of BDs of TAF1 and BRD2, supporting recent reports.	INTRO
+35	47	YEATS domain	structure_element	These results demonstrate that the YEATS domain is currently the sole reader of crotonyllysine.	INTRO
+80	94	crotonyllysine	residue_name	These results demonstrate that the YEATS domain is currently the sole reader of crotonyllysine.	INTRO
+38	50	YEATS domain	structure_element	In conclusion, we have identified the YEATS domain of Taf14 as the first reader of histone crotonylation.	INTRO
+54	59	Taf14	protein	In conclusion, we have identified the YEATS domain of Taf14 as the first reader of histone crotonylation.	INTRO
+83	90	histone	protein_type	In conclusion, we have identified the YEATS domain of Taf14 as the first reader of histone crotonylation.	INTRO
+91	104	crotonylation	ptm	In conclusion, we have identified the YEATS domain of Taf14 as the first reader of histone crotonylation.	INTRO
+71	85	π-π-π-stacking	bond_interaction	The unique and previously unobserved aromatic-amide/aliphatic-aromatic π-π-π-stacking mechanism facilitates the specific recognition of the crotonyl moiety.	INTRO
+140	148	crotonyl	chemical	The unique and previously unobserved aromatic-amide/aliphatic-aromatic π-π-π-stacking mechanism facilitates the specific recognition of the crotonyl moiety.	INTRO
+28	30	H3	protein_type	We further demonstrate that H3K9cr exists in yeast and is dynamically regulated by HATs and HDACs.	INTRO
+30	34	K9cr	ptm	We further demonstrate that H3K9cr exists in yeast and is dynamically regulated by HATs and HDACs.	INTRO
+45	50	yeast	taxonomy_domain	We further demonstrate that H3K9cr exists in yeast and is dynamically regulated by HATs and HDACs.	INTRO
+83	87	HATs	protein_type	We further demonstrate that H3K9cr exists in yeast and is dynamically regulated by HATs and HDACs.	INTRO
+92	97	HDACs	protein_type	We further demonstrate that H3K9cr exists in yeast and is dynamically regulated by HATs and HDACs.	INTRO
+42	52	acyllysine	residue_name	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+68	73	Taf14	protein	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+74	86	YEATS domain	structure_element	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+210	224	crotonyllysine	residue_name	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+276	281	Taf14	protein	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+309	323	crotonyllysine	residue_name	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+328	340	acetyllysine	residue_name	As we previously showed the importance of acyllysine binding by the Taf14 YEATS domain for the DNA damage response and gene transcription, it will be essential in the future to define the physiological role of crotonyllysine recognition and to differentiate the activities of Taf14 that are due to binding to crotonyllysine and acetyllysine modifications.	INTRO
+44	58	crotonyllysine	residue_name	Furthermore, the functional significance of crotonyllysine recognition by other YEATS proteins will be of great importance to elucidate and compare.	INTRO
+80	85	YEATS	protein_type	Furthermore, the functional significance of crotonyllysine recognition by other YEATS proteins will be of great importance to elucidate and compare.	INTRO
+48	50	H3	protein_type	The structural mechanism for the recognition of H3K9cr	FIG
+50	54	K9cr	ptm	The structural mechanism for the recognition of H3K9cr	FIG
+26	40	crotonyllysine	residue_name	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+50	67	crystal structure	evidence	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+75	80	Taf14	protein	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+81	93	YEATS domain	structure_element	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+102	117	in complex with	protein_state	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+122	132	H3K9cr5-13	chemical	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+154	156	H3	protein_type	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+156	160	K9cr	ptm	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+218	254	electrostatic and polar interactions	bond_interaction	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+264	269	Taf14	protein	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+270	282	YEATS domain	structure_element	(a) Chemical structure of crotonyllysine. (b) The crystal structure of the Taf14 YEATS domain (wheat) in complex with the H3K9cr5-13 peptide (green). (c) H3K9cr is stabilized via an extensive network of intermolecular electrostatic and polar interactions with the Taf14 YEATS domain.	FIG
+8	22	π-π-π stacking	bond_interaction	(d) The π-π-π stacking mechanism involving the alkene moiety of crotonyllysine.	FIG
+64	78	crotonyllysine	residue_name	(d) The π-π-π stacking mechanism involving the alkene moiety of crotonyllysine.	FIG
+0	2	H3	protein_type	H3K9cr is a selective target of the Taf14 YEATS domain	FIG
+2	6	K9cr	ptm	H3K9cr is a selective target of the Taf14 YEATS domain	FIG
+36	41	Taf14	protein	H3K9cr is a selective target of the Taf14 YEATS domain	FIG
+42	54	YEATS domain	structure_element	H3K9cr is a selective target of the Taf14 YEATS domain	FIG
+7	19	Western blot	experimental_method	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+53	55	H3	protein_type	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+55	59	K9cr	ptm	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+64	66	H3	protein_type	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+66	70	K9ac	ptm	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+74	83	wild type	protein_state	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+85	87	WT	protein_state	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+90	93	HAT	protein_type	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+107	111	HDAC	protein_type	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+112	120	deletion	experimental_method	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+121	126	yeast	taxonomy_domain	(a, b) Western blot analysis comparing the levels of H3K9cr and H3K9ac in wild type (WT), HAT deletion, or HDAC deletion yeast strains.	FIG
+6	8	H3	protein_type	Total H3 was used as a loading control.	FIG
+17	28	1H,15N HSQC	experimental_method	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+29	36	spectra	evidence	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+40	45	Taf14	protein	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+46	51	YEATS	structure_element	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+64	74	H3K9cr5-13	chemical	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+79	89	H3K9ac5-13	chemical	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+104	112	titrated	experimental_method	(c) Superimposed 1H,15N HSQC spectra of Taf14 YEATS recorded as H3K9cr5-13 and H3K9ac5-13 peptides were titrated in.	FIG
+0	7	Spectra	evidence	Spectra are color coded according to the protein:peptide molar ratio.	FIG
+4	16	Western blot	experimental_method	(d) Western blot analyses of peptide pull-down assays using wild-type and mutated Taf14 YEATS domains and indicated peptides.	FIG
+29	53	peptide pull-down assays	experimental_method	(d) Western blot analyses of peptide pull-down assays using wild-type and mutated Taf14 YEATS domains and indicated peptides.	FIG
+60	69	wild-type	protein_state	(d) Western blot analyses of peptide pull-down assays using wild-type and mutated Taf14 YEATS domains and indicated peptides.	FIG
+74	81	mutated	protein_state	(d) Western blot analyses of peptide pull-down assays using wild-type and mutated Taf14 YEATS domains and indicated peptides.	FIG
+82	87	Taf14	protein	(d) Western blot analyses of peptide pull-down assays using wild-type and mutated Taf14 YEATS domains and indicated peptides.	FIG
+88	101	YEATS domains	structure_element	(d) Western blot analyses of peptide pull-down assays using wild-type and mutated Taf14 YEATS domains and indicated peptides.	FIG