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    <admin>
        <current_status>
            <date>2026-02-18</date>
            <code>REL</code>
            <processing_site>PDBe</processing_site>
        </current_status>
        <revision_history>
            <revision version="1.0" date="2026-02-11">
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                    <model>
                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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                        <revision_type>INITIAL_RELEASE</revision_type>
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                        <provider>REPOSITORY</provider>
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                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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                    <half_map part="2">
                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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                        <revision_type>INITIAL_RELEASE</revision_type>
                        <provider>REPOSITORY</provider>
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            <revision version="1.1" date="2026-02-18">
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                    <model>
                        <revision_group>DATABASE_REFERENCES</revision_group>
                        <categories>
                            <category>citation</category>
                            <category>em_admin</category>
                        </categories>
                        <items>
                            <item>_citation.pdbx_database_id_PubMed</item>
                            <item>_citation.title</item>
                            <item>_em_admin.last_update</item>
                        </items>
                    </model>
                    <metadata>
                        <revision_group>EXPERIMENTAL_SUMMARY</revision_group>
                        <categories>
                            <category>citation</category>
                            <category>em_admin</category>
                        </categories>
                        <items>
                            <item>_citation.pdbx_database_id_PubMed</item>
                            <item>_citation.title</item>
                            <item>_em_admin.last_update</item>
                        </items>
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                </change_list>
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        </revision_history>
        <sites>
            <deposition>PDBe</deposition>
            <last_processing>PDBe</last_processing>
        </sites>
        <key_dates>
            <deposition>2026-01-19</deposition>
            <header_release>2026-02-11</header_release>
            <map_release>2026-02-11</map_release>
            <update>2026-02-18</update>
        </key_dates>
        <grant_support>
            <grant_reference>
                <funding_body>Not funded</funding_body>
            </grant_reference>
        </grant_support>
        <title>Structure of the MAP2K MEK1 in an inactive conformation in complex with its substrate MAPK ERK2</title>
        <authors_list>
            <author>von Velsen J</author>
            <author>Juyoux P</author>
            <author>Bowler MW</author>
        </authors_list>
        <keywords>protein kinases, phosphoryl transfer, MAPK, MAP2K, cancer signaling, SIGNALING PROTEIN</keywords>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author order="1">von Velsen J</author>
                    <author order="2">Juyoux P</author>
                    <author order="3">Piasentin N</author>
                    <author order="4">Fisher H</author>
                    <author order="5">Lapouge K</author>
                    <author order="6">Vadas O</author>
                    <author order="7">Gervasio FL</author>
                    <author order="8">Bowler MW</author>
                    <title>Molecular basis of mitogen-activated protein kinase ERK2 activation by its upstream kinase MEK1.</title>
                    <journal_abbreviation>Biorxiv</journal_abbreviation>
                    <country>US</country>
                    <year>2026</year>
                    <external_references type="PUBMED">41648251</external_references>
                    <external_references type="DOI">doi:10.64898/2026.01.19.700303</external_references>
                    <external_references type="ISSN">2692-8205</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
        <emdb_list>
            <emdb_reference>
                <emdb_id>EMD-56419</emdb_id>
                <relationship>
                    <other>other EM volume</other>
                </relationship>
                <details>other reconstruction originate from the same data collection</details>
            </emdb_reference>
            <emdb_reference>
                <emdb_id>EMD-56420</emdb_id>
                <relationship>
                    <other>other EM volume</other>
                </relationship>
                <details>other reconstruction originate from the same data collection</details>
            </emdb_reference>
        </emdb_list>
        <pdb_list>
            <pdb_reference>
                <pdb_id>9tyg</pdb_id>
                <relationship>
                    <in_frame>FULLOVERLAP</in_frame>
                </relationship>
            </pdb_reference>
        </pdb_list>
        <other_db_list>
            <db_reference>
                <db_name>EMDB</db_name>
                <accession_id>EMD-56419</accession_id>
                <content_type>other EM volume</content_type>
                <details>other reconstruction originate from the same data collection</details>
            </db_reference>
            <db_reference>
                <db_name>EMDB</db_name>
                <accession_id>EMD-56420</accession_id>
                <content_type>other EM volume</content_type>
                <details>other reconstruction originate from the same data collection</details>
            </db_reference>
            <db_reference>
                <db_name>EMDB</db_name>
                <accession_id>EMD-56418</accession_id>
                <content_type>associated EM volume</content_type>
                <details>Structure of the MAP2K MEK1 in an inactive conformation in complex with its substrate MAPK ERK2</details>
            </db_reference>
        </other_db_list>
    </crossreferences>
    <sample>
        <name>Complex between the MAP2K MEK1 and its substrate MAPK ERK2</name>
        <supramolecule_list>
            <complex_supramolecule supramolecule_id="1">
                <name>Complex between the MAP2K MEK1 and its substrate MAPK ERK2</name>
                <parent>0</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>1</macromolecule_id>
                    </macromolecule>
                    <macromolecule>
                        <macromolecule_id>2</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="kDa/nm">41.7</theoretical>
                </molecular_weight>
            </complex_supramolecule>
            <organelle_or_cellular_component_supramolecule supramolecule_id="2">
                <name>MEK1DDGRA</name>
                <parent>1</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>1</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <details>human MEK1 with KIM motif exchanged to GRA24 KIM (15 residues).</details>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
            </organelle_or_cellular_component_supramolecule>
            <organelle_or_cellular_component_supramolecule supramolecule_id="3">
                <name>ERK2</name>
                <parent>1</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>2</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <details>human ERK2 with point mutation on T185V.</details>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
            </organelle_or_cellular_component_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name>Dual specificity mitogen-activated protein kinase kinase 1,Uncharacterized protein,Dual specificity mitogen-activated protein kinase kinase 1</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.044981561999999996</theoretical>
                </molecular_weight>
                <details>protein chimera of human MEK1, exchanging native KIM (r3-11) by GRA24 KIM (15 residues). Addition of activating mutations on serines in activation-loop: Ser218Asp, Ser222Asp.,protein chimera of human MEK1, exchanging native KIM (r3-11) by GRA24 KIM (15 residues). Addition of activating mutations on serines in activation-loop: Ser218Asp, Ser222Asp.,protein chimera of human MEK1, exchanging native KIM (r3-11) by GRA24 KIM (15 residues). Addition of activating mutations on serines in activation-loop: Ser218Asp, Ser222Asp.,protein chimera of human MEK1, exchanging native KIM (r3-11) by GRA24 KIM (15 residues). Addition of activating mutations on serines in activation-loop: Ser218Asp, Ser222Asp.,protein chimera of human MEK1, exchanging native KIM (r3-11) by GRA24 KIM (15 residues). Addition of activating mutations on serines in activation-loop: Ser218Asp, Ser222Asp.,protein chimera of human MEK1, exchanging native KIM (r3-11) by GRA24 KIM (15 residues). Addition of activating mutations on serines in activation-loop: Ser218Asp, Ser222Asp.</details>
                <number_of_copies>1</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="7111">Trichoplusia ni</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>MPLLERRGVSELPPLYINPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISEL
GAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQV
LKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDDMANDFVGTRSYMSPER
LQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELL
DYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGVL
EVLFQ</string>
                    <external_references type="UNIPROTKB">Q02750</external_references>
                    <external_references type="UNIPROTKB">A0A125YG37</external_references>
                    <external_references type="UNIPROTKB">Q02750</external_references>
                </sequence>
                <ec_number>2.7.12.2</ec_number>
            </protein_or_peptide>
            <protein_or_peptide macromolecule_id="2">
                <name>Mitogen-activated protein kinase 1</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.041724976999999996</theoretical>
                </molecular_weight>
                <details>ERK2 with point mutation on residue 185 to a valine</details>
                <number_of_copies>1</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="562">Escherichia coli</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>QGPMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLR
FRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLL
NTTCDLKICDFGLARVADPDHDHTGFLVEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQL
NHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYY
DPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS</string>
                    <external_references type="UNIPROTKB">P28482</external_references>
                </sequence>
                <ec_number>2.7.11.24</ec_number>
            </protein_or_peptide>
            <ligand macromolecule_id="3">
                <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="4">
                <name>MAGNESIUM ION</name>
                <molecular_weight>
                    <theoretical units="MDa">2.4305e-05</theoretical>
                </molecular_weight>
                <number_of_copies>1</number_of_copies>
                <formula>MG</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">
                    <concentration units="mg/mL">0.516</concentration>
                    <buffer>
                        <ph>7.5</ph>
                        <component>
                            <concentration units="mM">50.0</concentration>
                            <name>HEPES pH 7.5</name>
                        </component>
                        <component>
                            <concentration units="mM">200.0</concentration>
                            <formula>NaCl</formula>
                            <name>sodium chloride</name>
                        </component>
                        <component>
                            <concentration units="mM">10.0</concentration>
                            <formula>MgCl2</formula>
                            <name>magnesium chloride</name>
                        </component>
                        <component>
                            <concentration units="%">5.0</concentration>
                            <name>Glycerol</name>
                        </component>
                        <component>
                            <concentration units="mM">0.5</concentration>
                            <name>TCEP</name>
                        </component>
                    </buffer>
                    <grid>
                        <model>HexAuFoil</model>
                        <material>GOLD</material>
                        <support_film film_type_id="1">
                            <film_material>GOLD</film_material>
                            <film_topology>HOLEY</film_topology>
                        </support_film>
                        <pretreatment>
                            <type>PLASMA CLEANING</type>
                            <time units="s">180</time>
                            <atmosphere>OTHER</atmosphere>
                        </pretreatment>
                    </grid>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                        <chamber_humidity units="percentage">100</chamber_humidity>
                        <chamber_temperature units="K">279.15</chamber_temperature>
                        <instrument>FEI VITROBOT MARK IV</instrument>
                    </vitrification>
                    <details>250 uM ADP.AlF4- was added to the sample</details>
                </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">1.0</nominal_defocus_min>
                    <nominal_defocus_max units="µm">2.2</nominal_defocus_max>
                    <nominal_magnification>270000.0</nominal_magnification>
                    <specimen_holder_model>FEI TITAN KRIOS AUTOGRID HOLDER</specimen_holder_model>
                    <cooling_holder_cryogen>NITROGEN</cooling_holder_cryogen>
                    <specialist_optics>
                        <energy_filter>
                            <name>TFS Selectris X</name>
                            <slit_width units="eV">10</slit_width>
                        </energy_filter>
                    </specialist_optics>
                    <image_recording_list>
                        <image_recording image_recording_id="1">
                            <film_or_detector_model>TFS FALCON 4i (4k x 4k)</film_or_detector_model>
                            <number_grids_imaged>1</number_grids_imaged>
                            <number_real_images>88517</number_real_images>
                            <average_exposure_time units="s">1.7</average_exposure_time>
                            <average_electron_dose_per_image units="e/Å^2">50.0</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>v4.7.0</version>
                            <processing_details>Patch CTF</processing_details>
                        </software>
                    </software_list>
                    <type>PHASE FLIPPING AND AMPLITUDE CORRECTION</type>
                </ctf_correction>
                <startup_model type_of_model="INSILICO MODEL">
                    <insilico_model>AlphaFold</insilico_model>
                </startup_model>
                <final_reconstruction>
                    <resolution units="Å" res_type="BY AUTHOR">2.9</resolution>
                    <resolution_method>FSC 0.143 CUT-OFF</resolution_method>
                    <software_list>
                        <software>
                            <name>cryoSPARC</name>
                            <version>v4.7.0</version>
                        </software>
                    </software_list>
                    <number_images_used>142124</number_images_used>
                </final_reconstruction>
                <initial_angle_assignment>
                    <type>MAXIMUM LIKELIHOOD</type>
                </initial_angle_assignment>
                <final_angle_assignment>
                    <type>MAXIMUM LIKELIHOOD</type>
                </final_angle_assignment>
            </singleparticle_processing>
        </structure_determination>
    </structure_determination_list>
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        <file>emd_56418.map.gz</file>
        <symmetry>
            <space_group>1</space_group>
        </symmetry>
        <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
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            <col>220</col>
            <row>220</row>
            <sec>220</sec>
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            <sec>0</sec>
        </origin>
        <spacing>
            <x>220</x>
            <y>220</y>
            <z>220</z>
        </spacing>
        <cell>
            <a units="Å">202.40001</a>
            <b units="Å">202.40001</b>
            <c units="Å">202.40001</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>-0.20678288</minimum>
            <maximum>0.5856031</maximum>
            <average>0.0006000431</average>
            <std>0.0128877675</std>
        </statistics>
        <pixel_spacing>
            <x units="Å">0.92</x>
            <y units="Å">0.92</y>
            <z units="Å">0.92</z>
        </pixel_spacing>
        <contour_list>
            <contour primary="true">
                <level>0.0669</level>
                <source>AUTHOR</source>
            </contour>
        </contour_list>
        <label>::::EMDATABANK.org::::EMD-56418::::</label>
        <annotation_details>refined map of MEK1DDGRA-ERK2T185V</annotation_details>
    </map>
    <interpretation>
        <modelling_list>
            <modelling>
                <initial_model>
                    <chain>
                        <source_name>AlphaFold</source_name>
                        <initial_model_type>in silico model</initial_model_type>
                    </chain>
                </initial_model>
                <refinement_protocol>RIGID BODY FIT</refinement_protocol>
                <refinement_space>REAL</refinement_space>
            </modelling>
        </modelling_list>
        <segmentation_list>
            <segmentation>
                <file>emd_56418_msk_1.map</file>
            </segmentation>
        </segmentation_list>
        <additional_map_list>
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                <file>emd_56418_additional_1.map.gz</file>
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                    <space_group>1</space_group>
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                    <row>220</row>
                    <sec>220</sec>
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                <spacing>
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                    <z>220</z>
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                <cell>
                    <a units="Å">202.40001</a>
                    <b units="Å">202.40001</b>
                    <c units="Å">202.40001</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>-0.2759306</minimum>
                    <maximum>0.7205638</maximum>
                    <average>0.00077336375</average>
                    <std>0.014220664</std>
                </statistics>
                <pixel_spacing>
                    <x units="Å">0.92</x>
                    <y units="Å">0.92</y>
                    <z units="Å">0.92</z>
                </pixel_spacing>
                <contour_list>
                    <contour primary="true">
                        <source>AUTHOR</source>
                    </contour>
                </contour_list>
                <label>::::EMDATABANK.org::::EMD-56418::::</label>
                <annotation_details>B-factor sharpened map of MEK1DDGRA-T185V</annotation_details>
            </additional_map>
        </additional_map_list>
        <half_map_list>
            <half_map format="CCP4" size_kbytes="42593">
                <file>emd_56418_half_map_2.map.gz</file>
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                    <space_group>1</space_group>
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                    <col>220</col>
                    <row>220</row>
                    <sec>220</sec>
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                    <col>0</col>
                    <row>0</row>
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                </origin>
                <spacing>
                    <x>220</x>
                    <y>220</y>
                    <z>220</z>
                </spacing>
                <cell>
                    <a units="Å">202.40001</a>
                    <b units="Å">202.40001</b>
                    <c units="Å">202.40001</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>-0.3910495</minimum>
                    <maximum>0.7068123</maximum>
                    <average>0.000504464</average>
                    <std>0.052621096</std>
                </statistics>
                <pixel_spacing>
                    <x units="Å">0.92</x>
                    <y units="Å">0.92</y>
                    <z units="Å">0.92</z>
                </pixel_spacing>
                <contour_list>
                    <contour primary="true">
                        <source>AUTHOR</source>
                    </contour>
                </contour_list>
                <label>::::EMDATABANK.org::::EMD-56418::::</label>
                <annotation_details>half map B</annotation_details>
            </half_map>
            <half_map format="CCP4" size_kbytes="42593">
                <file>emd_56418_half_map_1.map.gz</file>
                <symmetry>
                    <space_group>1</space_group>
                </symmetry>
                <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
                <dimensions>
                    <col>220</col>
                    <row>220</row>
                    <sec>220</sec>
                </dimensions>
                <origin>
                    <col>0</col>
                    <row>0</row>
                    <sec>0</sec>
                </origin>
                <spacing>
                    <x>220</x>
                    <y>220</y>
                    <z>220</z>
                </spacing>
                <cell>
                    <a units="Å">202.40001</a>
                    <b units="Å">202.40001</b>
                    <c units="Å">202.40001</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>-0.41755557</minimum>
                    <maximum>0.757493</maximum>
                    <average>0.0005045392</average>
                    <std>0.053354505</std>
                </statistics>
                <pixel_spacing>
                    <x units="Å">0.92</x>
                    <y units="Å">0.92</y>
                    <z units="Å">0.92</z>
                </pixel_spacing>
                <contour_list>
                    <contour primary="true">
                        <source>AUTHOR</source>
                    </contour>
                </contour_list>
                <label>::::EMDATABANK.org::::EMD-56418::::</label>
                <annotation_details>half map A</annotation_details>
            </half_map>
        </half_map_list>
    </interpretation>
</emd>
