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    <admin>
        <current_status>
            <date>2019-06-19</date>
            <code>REL</code>
            <processing_site>RCSB</processing_site>
        </current_status>
        <sites>
            <deposition>RCSB</deposition>
            <last_processing>RCSB</last_processing>
        </sites>
        <key_dates>
            <deposition>2019-03-09</deposition>
            <header_release>2019-04-10</header_release>
            <map_release>2019-04-24</map_release>
            <update>2019-06-19</update>
        </key_dates>
        <grant_support>
            <grant_reference>
                <funding_body>National Institutes of Health/National Human Genome Research Institute</funding_body>
                <code>5R01GM115882-03</code>
                <country>United States</country>
            </grant_reference>
            <grant_reference>
                <funding_body>Other private</funding_body>
                <code>David and Lucille Packard Foundation</code>
                <country>United States</country>
            </grant_reference>
        </grant_support>
        <title>Structural basis of Dot1L stimulation by histone H2B lysine 120 ubiquitination. 5.2A reconstruction of Dot1L on H2BK120Ub nucleosome</title>
        <authors_list>
            <author>Valencia-Sanchez MI</author>
            <author>De Ioannes P</author>
            <author>Wang M</author>
            <author>Vasilyev N</author>
            <author>Chen R</author>
            <author>Nudler E</author>
            <author>Armache J-P</author>
            <author>Armache K-J</author>
        </authors_list>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author order="1">Valencia-Sanchez MI</author>
                    <author order="2">De Ioannes P</author>
                    <author order="3">Wang M</author>
                    <author order="4">Vasilyev N</author>
                    <author order="5">Chen R</author>
                    <author order="6">Nudler E</author>
                    <author order="7">Armache JP</author>
                    <author order="8">Armache KJ</author>
                    <title>Structural Basis of Dot1L Stimulation by Histone H2B Lysine 120 Ubiquitination.</title>
                    <journal_abbreviation>Mol.Cell</journal_abbreviation>
                    <country>US</country>
                    <volume>74</volume>
                    <first_page>1010</first_page>
                    <last_page>1019.e6</last_page>
                    <year>2019</year>
                    <external_references type="PUBMED">30981630</external_references>
                    <external_references type="DOI">doi:10.1016/j.molcel.2019.03.029</external_references>
                    <external_references type="ISSN">1097-2765</external_references>
                    <external_references type="CSD">2168</external_references>
                    <external_references type="ASTM">MOCEFL</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
        <emdb_list>
            <emdb_reference>
                <emdb_id>EMD-0654</emdb_id>
                <relationship>
                    <other>associated EM volume</other>
                </relationship>
            </emdb_reference>
        </emdb_list>
    </crossreferences>
    <sample>
        <name>Cryo-EM structure of human Dot1L bound to H2BK120Ub  nucleosome at 5.2A resolution</name>
        <supramolecule_list>
            <complex_supramolecule supramolecule_id="1">
                <name>Cryo-EM structure of human Dot1L bound to H2BK120Ub  nucleosome at 5.2A resolution</name>
                <parent>0</parent>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="469008">Escherichia coli</recombinant_organism>
                    <recombinant_strain>BL21(DE3)</recombinant_strain>
                </recombinant_expression>
            </complex_supramolecule>
        </supramolecule_list>
    </sample>
    <structure_determination_list>
        <structure_determination structure_determination_id="1">
            <method>singleParticle</method>
            <aggregation_state>particle</aggregation_state>
            <specimen_preparation_list>
                <single_particle_preparation preparation_id="1">
                    <buffer>
                        <ph>7.5</ph>
                    </buffer>
                    <grid>
                        <support_film film_type_id="1">
                            <film_material>CARBON</film_material>
                            <film_topology>HOLEY</film_topology>
                        </support_film>
                        <details>unspecified</details>
                    </grid>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                        <chamber_humidity units="percentage">100</chamber_humidity>
                        <chamber_temperature units="K">295.15</chamber_temperature>
                        <instrument>FEI VITROBOT MARK I</instrument>
                        <details>3  ul  of  Dot1L-nucleosome complexes were applied to a glow discharged Quantifoil  holey  carbon  grid  (1.2  um  hole  size,  200  mesh),  blotted  in  a Vitrobot  Mark  III  (FEI Company)  using  1.5  seconds  blotting  at  100%  humidity,  and  then  plunge-frozen  in  liquid  ethane cooled  by  liquid  nitrogen.. </details>
                    </vitrification>
                    <details>This sample was monodisperse</details>
                </single_particle_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <single_particle_microscopy microscopy_id="1">
                    <microscope>FEI TALOS ARCTICA</microscope>
                    <illumination_mode>FLOOD BEAM</illumination_mode>
                    <imaging_mode>BRIGHT FIELD</imaging_mode>
                    <electron_source>FIELD EMISSION GUN</electron_source>
                    <acceleration_voltage units="kV">200</acceleration_voltage>
                    <image_recording_list>
                        <image_recording image_recording_id="1">
                            <film_or_detector_model>GATAN K2 SUMMIT (4k x 4k)</film_or_detector_model>
                            <detector_mode>SUPER-RESOLUTION</detector_mode>
                            <digitization_details>
                                <sampling_interval units="µm">5.0</sampling_interval>
                            </digitization_details>
                            <average_electron_dose_per_image units="e/Å^2">41.0</average_electron_dose_per_image>
                        </image_recording>
                    </image_recording_list>
                </single_particle_microscopy>
            </microscopy_list>
            <singleparticle_processing image_processing_id="1">
                <image_recording_id>1</image_recording_id>
                <details>Frames were motion corrected using MotionCor2 with dose-weighting</details>
                <particle_selection>
                    <number_selected>1607487</number_selected>
                </particle_selection>
                <ctf_correction>
                    <software_list>
                        <software>
                            <name>Gctf</name>
                        </software>
                    </software_list>
                </ctf_correction>
                <startup_model type_of_model="INSILICO MODEL">
                    <insilico_model>Generated using cryosparc ab initio run</insilico_model>
                </startup_model>
                <final_reconstruction>
                    <resolution units="Å" res_type="BY AUTHOR">5.2</resolution>
                    <resolution_method>FSC 0.143 CUT-OFF</resolution_method>
                    <number_images_used>85029</number_images_used>
                </final_reconstruction>
                <initial_angle_assignment>
                    <type>PROJECTION MATCHING</type>
                    <projection_matching_processing/>
                </initial_angle_assignment>
                <final_angle_assignment>
                    <type>PROJECTION MATCHING</type>
                    <projection_matching_processing/>
                </final_angle_assignment>
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            <alpha units="deg">90.0</alpha>
            <beta units="deg">90.0</beta>
            <gamma units="deg">90.0</gamma>
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            <medium>Y</medium>
            <slow>Z</slow>
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            <minimum>-7.5235167</minimum>
            <maximum>13.706490499999999</maximum>
            <average>-0.0060144644</average>
            <std>0.40734196</std>
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        <pixel_spacing>
            <x units="Å">1.45</x>
            <y units="Å">1.45</y>
            <z units="Å">1.45</z>
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                <level>2.0</level>
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        <label>::::EMDATABANK.org::::EMD-0654::::</label>
        <annotation_details>Result of cisTEM refinement, filtered to 5.2A, not sharpened. This map is in the same environment as the model constructed. It is shifted and resampled to fit with the environment of the paper</annotation_details>
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        <modelling_list>
            <modelling>
                <refinement_protocol>FLEXIBLE FIT</refinement_protocol>
                <refinement_space>REAL</refinement_space>
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                    <minimum>-8.098045000000001</minimum>
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                    <average>-0.006739371</average>
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                <label>::::EMDATABANK.org::::EMD-0654::::</label>
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                    <beta units="deg">90.0</beta>
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                    <average>-0.10943525</average>
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                    <y units="Å">1.45</y>
                    <z units="Å">1.45</z>
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                        <source>AUTHOR</source>
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                <label>::::EMDATABANK.org::::EMD-0654::::</label>
                <annotation_details>Half-map 2</annotation_details>
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                    <a units="Å">371.2</a>
                    <b units="Å">371.2</b>
                    <c units="Å">371.2</c>
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                    <beta units="deg">90.0</beta>
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                    <medium>Y</medium>
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                    <average>-0.10947102</average>
                    <std>0.335982</std>
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                <pixel_spacing>
                    <x units="Å">1.45</x>
                    <y units="Å">1.45</y>
                    <z units="Å">1.45</z>
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                    <contour primary="true">
                        <source>AUTHOR</source>
                    </contour>
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                <label>::::EMDATABANK.org::::EMD-0654::::</label>
                <annotation_details>Half-map 1</annotation_details>
            </half_map>
        </half_map_list>
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