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    <admin>
        <current_status>
            <date>2025-10-01</date>
            <code>REL</code>
            <processing_site>PDBe</processing_site>
        </current_status>
        <revision_history>
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                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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        </revision_history>
        <sites>
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            <last_processing>PDBe</last_processing>
        </sites>
        <key_dates>
            <deposition>2025-02-26</deposition>
            <header_release>2025-10-01</header_release>
            <map_release>2025-10-01</map_release>
            <update>2025-10-01</update>
        </key_dates>
        <grant_support>
            <grant_reference>
                <funding_body>German Research Foundation (DFG)</funding_body>
                <country>Germany</country>
            </grant_reference>
        </grant_support>
        <title>Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor TRF2 fragment (438-542)</title>
        <authors_list>
            <author>Cui HJ</author>
            <author>Lammens K</author>
            <author>Hopfner KP</author>
            <author>Fan YL</author>
            <author>Kuybu F</author>
        </authors_list>
        <keywords>Mre11-Rad50-TRF2 complex, double-strand DNA break repair protein, nuclease, HYDROLASE</keywords>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author ORCID="0009-0003-1954-9343" order="1">Fan Y</author>
                    <author ORCID="0000-0002-8404-2536" order="2">Kuybu F</author>
                    <author ORCID="0000-0002-5445-0424" order="3">Cui H</author>
                    <author ORCID="0000-0002-4438-1381" order="4">Lammens K</author>
                    <author order="5">Chen JX</author>
                    <author ORCID="0000-0002-0752-9682" order="6">Kugler M</author>
                    <author ORCID="0000-0002-9774-1125" order="7">Jung C</author>
                    <author ORCID="0000-0002-4528-8357" order="8">Hopfner KP</author>
                    <title>Structural basis for DNA break sensing by human MRE11-RAD50-NBS1 and its regulation by telomeric factor TRF2.</title>
                    <journal_abbreviation>Nat Commun</journal_abbreviation>
                    <country>UK</country>
                    <volume>16</volume>
                    <first_page>8320</first_page>
                    <last_page>8320</last_page>
                    <year>2025</year>
                    <external_references type="PUBMED">40968163</external_references>
                    <external_references type="DOI">doi:10.1038/s41467-025-64082-x</external_references>
                    <external_references type="ISSN">2041-1723</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
        <pdb_list>
            <pdb_reference>
                <pdb_id>9q9k</pdb_id>
                <relationship>
                    <in_frame>FULLOVERLAP</in_frame>
                </relationship>
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                <db_name>EMDB</db_name>
                <accession_id>EMD-52962</accession_id>
                <content_type>associated EM volume</content_type>
                <details>Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor TRF2 fragment (438-542)</details>
            </db_reference>
        </other_db_list>
    </crossreferences>
    <sample>
        <name>MR-TRF2(438-542)-DNA complex</name>
        <supramolecule_list>
            <complex_supramolecule supramolecule_id="1">
                <name>MR-TRF2(438-542)-DNA complex</name>
                <parent>0</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>1</macromolecule_id>
                    </macromolecule>
                    <macromolecule>
                        <macromolecule_id>2</macromolecule_id>
                    </macromolecule>
                    <macromolecule>
                        <macromolecule_id>3</macromolecule_id>
                    </macromolecule>
                    <macromolecule>
                        <macromolecule_id>4</macromolecule_id>
                    </macromolecule>
                    <macromolecule>
                        <macromolecule_id>5</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.52</theoretical>
                </molecular_weight>
            </complex_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name>Telomeric repeat-binding factor 2</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.012931349</theoretical>
                </molecular_weight>
                <details>GP is the leftover sequence from PreScission cleavage site, and GGSSGGSSG is a linker sequence between the cleavage site and TRF2(438-542) fragment.</details>
                <number_of_copies>2</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="7111">Trichoplusia ni</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>GPGGSSGGSSGQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDEDSTTNITKKQKWTVEESEWVKAGVQK
YGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLGMN</string>
                    <external_references type="UNIPROTKB">Q15554</external_references>
                </sequence>
            </protein_or_peptide>
            <dna macromolecule_id="2">
                <name>DNA (64-MER)</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.019423369</theoretical>
                </molecular_weight>
                <number_of_copies>1</number_of_copies>
                <sequence>
                    <string>(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)
(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)
(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)
(DT)(DT)(DT)(DT)</string>
                </sequence>
                <classification>DNA</classification>
            </dna>
            <dna macromolecule_id="3">
                <name>DNA (64-MER)</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.020000280999999998</theoretical>
                </molecular_weight>
                <number_of_copies>1</number_of_copies>
                <sequence>
                    <string>(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)
(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)
(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)
(DA)(DA)(DA)(DA)</string>
                </sequence>
                <classification>DNA</classification>
            </dna>
            <protein_or_peptide macromolecule_id="4">
                <name>DNA repair protein RAD50</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.154150016</theoretical>
                </molecular_weight>
                <number_of_copies>2</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="7111">Trichoplusia ni</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>MSRIEKMSILGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRA
QIRLQFRDVNGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQE
DSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEI
VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKER
KLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLV
RERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQE
LIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHS
DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFES
DLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELK
KKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQM
ELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTN
LQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKD
IENYIQDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQ
HLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKD
LDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGR
CSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRS
EYVEKFYRIKKNIDQCSEIVKCSVSSLGFNVH</string>
                    <external_references type="UNIPROTKB">Q92878</external_references>
                </sequence>
            </protein_or_peptide>
            <protein_or_peptide macromolecule_id="5">
                <name>Double-strand break repair protein MRE11</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.08403267999999998</theoretical>
                </molecular_weight>
                <details>Following residue R708 is a short GS linker, a PreScission cleavage site, and two FLAG tags.</details>
                <number_of_copies>2</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="7111">Trichoplusia ni</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLR
KYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVE
KIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDL
VIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDI
FNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFR
HREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEK
TQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDD
SISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNY
SEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRRSGGSLEVLFQGP
DYKDDDDKGTDYKDDDDK</string>
                    <external_references type="UNIPROTKB">P49959</external_references>
                </sequence>
                <ec_number>3.1.-.-</ec_number>
            </protein_or_peptide>
            <ligand macromolecule_id="6">
                <name>ADENOSINE-5'-DIPHOSPHATE</name>
                <molecular_weight>
                    <theoretical units="MDa">0.000427201</theoretical>
                </molecular_weight>
                <number_of_copies>2</number_of_copies>
                <formula>ADP</formula>
            </ligand>
            <ligand macromolecule_id="7">
                <name>MAGNESIUM ION</name>
                <molecular_weight>
                    <theoretical units="MDa">2.4305e-05</theoretical>
                </molecular_weight>
                <number_of_copies>2</number_of_copies>
                <formula>MG</formula>
            </ligand>
            <ligand macromolecule_id="8">
                <name>BERYLLIUM TRIFLUORIDE ION</name>
                <molecular_weight>
                    <theoretical units="MDa">6.600700000000001e-05</theoretical>
                </molecular_weight>
                <number_of_copies>2</number_of_copies>
                <formula>BEF</formula>
            </ligand>
            <ligand macromolecule_id="9">
                <name>MANGANESE (II) ION</name>
                <molecular_weight>
                    <theoretical units="MDa">5.4938e-05</theoretical>
                </molecular_weight>
                <number_of_copies>4</number_of_copies>
                <formula>MN</formula>
            </ligand>
            <ligand macromolecule_id="10">
                <name>water</name>
                <molecular_weight>
                    <theoretical units="MDa">1.8015e-05</theoretical>
                </molecular_weight>
                <number_of_copies>6</number_of_copies>
                <formula>HOH</formula>
            </ligand>
        </macromolecule_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>
                        <details>25mM Hepes-NaOH, pH 7.5, 150 mM NaCl, 1 mM DTT, 1 mM ATP, 1mM BeF3, 5 mM MgCl2, 1 mM MnCl2</details>
                    </buffer>
                    <grid>
                        <model>Quantifoil R2/1</model>
                        <material>COPPER</material>
                        <mesh>200</mesh>
                        <support_film film_type_id="1">
                            <film_material>CARBON</film_material>
                            <film_topology>HOLEY</film_topology>
                        </support_film>
                        <pretreatment>
                            <type>GLOW DISCHARGE</type>
                            <time units="s">7</time>
                        </pretreatment>
                        <details>20 mA, 7 s</details>
                    </grid>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                        <chamber_humidity units="percentage">95</chamber_humidity>
                        <chamber_temperature units="K">283</chamber_temperature>
                        <instrument>LEICA PLUNGER</instrument>
                    </vitrification>
                </single_particle_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <single_particle_microscopy microscopy_id="1">
                    <microscope>TFS KRIOS</microscope>
                    <illumination_mode>FLOOD BEAM</illumination_mode>
                    <imaging_mode>BRIGHT FIELD</imaging_mode>
                    <electron_source>FIELD EMISSION GUN</electron_source>
                    <acceleration_voltage units="kV">300</acceleration_voltage>
                    <nominal_cs units="mm">2.7</nominal_cs>
                    <nominal_defocus_min units="µm">0.5</nominal_defocus_min>
                    <nominal_defocus_max units="µm">2.6</nominal_defocus_max>
                    <cooling_holder_cryogen>NITROGEN</cooling_holder_cryogen>
                    <specialist_optics>
                        <energy_filter>
                            <name>GIF Bioquantum</name>
                            <slit_width units="eV">20</slit_width>
                        </energy_filter>
                    </specialist_optics>
                    <image_recording_list>
                        <image_recording image_recording_id="1">
                            <film_or_detector_model>FEI FALCON IV (4k x 4k)</film_or_detector_model>
                            <detector_mode>COUNTING</detector_mode>
                            <digitization_details/>
                            <average_electron_dose_per_image units="e/Å^2">40.0</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>
                <ctf_correction>
                    <software_list>
                        <software>
                            <name>cryoSPARC</name>
                            <version>4.6.2</version>
                        </software>
                    </software_list>
                    <type>PHASE FLIPPING AND AMPLITUDE CORRECTION</type>
                </ctf_correction>
                <startup_model type_of_model="INSILICO MODEL"/>
                <final_reconstruction>
                    <resolution units="Å" res_type="BY AUTHOR">2.59</resolution>
                    <resolution_method>FSC 0.143 CUT-OFF</resolution_method>
                    <software_list>
                        <software>
                            <name>cryoSPARC</name>
                            <version>4.6.2</version>
                        </software>
                    </software_list>
                    <number_images_used>274928</number_images_used>
                </final_reconstruction>
                <initial_angle_assignment>
                    <type>MAXIMUM LIKELIHOOD</type>
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                        <software>
                            <name>cryoSPARC</name>
                            <version>4.6.2</version>
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                <final_angle_assignment>
                    <type>MAXIMUM LIKELIHOOD</type>
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                    <b units="Å">261.72</b>
                    <c units="Å">261.72</c>
                    <alpha units="deg">90.0</alpha>
                    <beta units="deg">90.0</beta>
                    <gamma units="deg">90.0</gamma>
                </cell>
                <axis_order>
                    <fast>X</fast>
                    <medium>Y</medium>
                    <slow>Z</slow>
                </axis_order>
                <statistics>
                    <minimum>-0.50943017</minimum>
                    <maximum>1.4444592</maximum>
                    <average>0.0011108797</average>
                    <std>0.043588415</std>
                </statistics>
                <pixel_spacing>
                    <x units="Å">0.727</x>
                    <y units="Å">0.727</y>
                    <z units="Å">0.727</z>
                </pixel_spacing>
                <contour_list>
                    <contour primary="true">
                        <source>AUTHOR</source>
                    </contour>
                </contour_list>
                <label>::::EMDATABANK.org::::EMD-52962::::</label>
            </half_map>
        </half_map_list>
    </interpretation>
</emd>
