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        <sites>
            <deposition>PDBe</deposition>
            <last_processing>PDBe</last_processing>
        </sites>
        <key_dates>
            <deposition>2018-06-14</deposition>
            <header_release>2018-08-22</header_release>
            <map_release>2019-01-16</map_release>
            <update>2025-07-09</update>
        </key_dates>
        <grant_support>
            <grant_reference>
                <funding_body>Medical Research Council (United Kingdom)</funding_body>
                <code>MC_UU_12014/7</code>
                <country>United Kingdom</country>
            </grant_reference>
            <grant_reference>
                <funding_body>Biotechnology and Biological Sciences Research Council</funding_body>
                <code>BB/J013854/1</code>
                <country>United Kingdom</country>
            </grant_reference>
        </grant_support>
        <title>Feline Calicivirus Strain F9 bound to a soluble ectodomain fragment of feline junctional adhesion molecule A - leading to assembly of a portal structure at a unique three-fold axis.</title>
        <authors_list>
            <author>Conley MJ</author>
            <author>Bhella D</author>
        </authors_list>
        <keywords>Capsid, Calicivirus, Vesivirus, Vp1, portal, Vp2, junctional-adhesion molecule A, VIRUS</keywords>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author order="1">Conley MJ</author>
                    <author order="2">McElwee M</author>
                    <author order="3">Azmi L</author>
                    <author order="4">Gabrielsen M</author>
                    <author order="5">Byron O</author>
                    <author order="6">Goodfellow IG</author>
                    <author order="7">Bhella D</author>
                    <title>Calicivirus VP2 forms a portal-like assembly following receptor engagement.</title>
                    <journal_abbreviation>Nature</journal_abbreviation>
                    <country>UK</country>
                    <volume>565</volume>
                    <first_page>377</first_page>
                    <last_page>381</last_page>
                    <year>2019</year>
                    <external_references type="PUBMED">30626974</external_references>
                    <external_references type="DOI">doi:10.1038/s41586-018-0852-1</external_references>
                    <external_references type="ISSN">1476-4687</external_references>
                    <external_references type="CSD">0006</external_references>
                    <external_references type="ASTM">NATUAS</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
        <emdb_list>
            <emdb_reference>
                <emdb_id>EMD-0054</emdb_id>
                <relationship>
                    <other>other EM volume</other>
                </relationship>
                <details>Icosahedral reconstruction of FCV strain F9</details>
            </emdb_reference>
        </emdb_list>
        <pdb_list>
            <pdb_reference>
                <pdb_id>6gsi</pdb_id>
                <relationship>
                    <in_frame>FULLOVERLAP</in_frame>
                </relationship>
            </pdb_reference>
        </pdb_list>
    </crossreferences>
    <sample>
        <name>Feline calicivirus strain F9</name>
        <supramolecule_list>
            <virus_supramolecule supramolecule_id="1">
                <name>Feline calicivirus strain F9</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_list>
                <details>Virus was propagated in Crandell Reese Feline Kidney cells</details>
                <natural_host database="NCBI">
                    <organism ncbi="9685">Felis catus</organism>
                </natural_host>
                <virus_shell shell_id="1">
                    <name>Capsid</name>
                    <diameter units="Å">400.0</diameter>
                    <triangulation>3</triangulation>
                </virus_shell>
                <virus_type>VIRION</virus_type>
                <virus_isolate>STRAIN</virus_isolate>
                <virus_enveloped>false</virus_enveloped>
                <virus_empty>false</virus_empty>
            </virus_supramolecule>
            <virus_supramolecule supramolecule_id="2">
                <name>Feline calicivirus strain F9</name>
                <parent>1</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>1</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <details>Icosahedral Capsid</details>
                <sci_species_name ncbi="11981">Feline calicivirus strain F9</sci_species_name>
                <natural_host database="NCBI">
                    <organism ncbi="9685">Felis catus</organism>
                </natural_host>
                <virus_shell shell_id="2">
                    <name>Capsid</name>
                    <diameter units="Å">400.0</diameter>
                    <triangulation>3</triangulation>
                </virus_shell>
                <virus_type>VIRION</virus_type>
                <virus_isolate>STRAIN</virus_isolate>
                <virus_enveloped>false</virus_enveloped>
                <virus_empty>false</virus_empty>
            </virus_supramolecule>
            <complex_supramolecule supramolecule_id="3">
                <name>feline junctional adhesion molecule A</name>
                <parent>1</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>2</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <details>Soluble ectodomain fragment comprising Ig-like domains D1 and D2</details>
                <natural_source database="NCBI">
                    <organism ncbi="9685">Felis catus</organism>
                </natural_source>
            </complex_supramolecule>
            <complex_supramolecule supramolecule_id="4">
                <name>VP2 - portal.</name>
                <parent>1</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>3</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <details>Postulated to mediate endosome escape, this virion component is only present on the outer surface of the capsid following receptor engagement.</details>
                <natural_source database="NCBI">
                    <organism ncbi="11981">Feline calicivirus strain F9</organism>
                </natural_source>
            </complex_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name>Capsid protein</name>
                <natural_source database="NCBI">
                    <organism ncbi="11981">Feline calicivirus strain F9</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.073346664</theoretical>
                </molecular_weight>
                <number_of_copies>4</number_of_copies>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>MCSTCANVLKYYNWDPHFRLVIDPNKFLSVGFCDNPLMCCYPELLPEFGTVWDCDQSPLQIYLESILGDDEWASTYEAID
PAVPPMHWDAAGKIFQPHPGVLMHHLIGEVAKAWDPNLPMFRLEADGDGSITAPEQGTPVGGVIAEPSAQMSAAADMATG
KSVDSEWEAFFSFHTSVNWSTSETQGKILFKQSLGPLLNPYLEHLAKLYVAWSGSIDVRFSISGSGVFGGKLAAIVVPPG
VDPVQSTSMLQYPHVLFDARQVEPVIFSIPDLRSTLYHLMSDTDTTSLVIMVYNDLINPYANDSNSSGCIVTVETKPGAD
FKFHLLKPPGSMLTHGSVPSDLIPKSSSLWIGNRHWTDITDFVIRPFVFQANRHFDFNQETAGWSTPRYRPITITISEKN
GAKLGIGVATDYIVPGIPDGWPDTTIPEKLTPAGDYAITNKSGNDITTAAGYDGADVIVNNTNFKGMYICGSLQRAWGDK
KISNTAFITTATKVDNAIEPSNVIDMTKIAVYQDTHVGKEVQTSDDTLSLLGYTGIGEQAIGSDRDRVVRISVLPETGAR
GGNHPIFYKNSIKLGYVIRSIDVFNSQILHTSRQLSLNHYLLPPDSFAVYRIIDSNGSWFDIGIDSDGFSFVGVSSIGKL
EFPLTASYMGIQLAKIRLASNIRSSMTKL</string>
                    <external_references type="UNIPROTKB">P27406</external_references>
                </sequence>
            </protein_or_peptide>
            <protein_or_peptide macromolecule_id="2">
                <name>Junctional adhesion molecule A</name>
                <natural_source database="NCBI">
                    <organism ncbi="9685">Felis catus</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.02218065</theoretical>
                </molecular_weight>
                <number_of_copies>4</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="10029">Cricetulus griseus</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>AVYTSEPDVRVPEDKPAKLSCSYSGFSNPRVEWKFAHGDITSLVCYKNKITASYADRVTFSHSGITFHSVTRKDTGTYTC
MVSDDGGNTYGEVSVQLTVLVPPSKPTVHIPSSATIGSRAVLTCSEKDGSPPSEYYWFKDGVRMPLEPKGNRAFSNSSYS
LNEKTGELVFDPVSAWDTGEYTCEAQNGYGMPMRSEAVRMEA</string>
                    <external_references type="UNIPROTKB">Q2WGK2</external_references>
                </sequence>
            </protein_or_peptide>
            <protein_or_peptide macromolecule_id="3">
                <name>VP2</name>
                <natural_source database="NCBI">
                    <organism ncbi="11981">Feline calicivirus strain F9</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.012209837999999999</theoretical>
                </molecular_weight>
                <number_of_copies>4</number_of_copies>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>MNSILGLIDTVTNTIGKAQQIELDKAALGQQRELALKRMKLDHQALNNQVEQFNKILEQRVQGPIQSVRLARAAGFRVDP
YSYTDQNFYDDQLNAIRLSYRNLFKN</string>
                    <external_references type="UNIPROTKB">P28711</external_references>
                </sequence>
            </protein_or_peptide>
            <ligand macromolecule_id="4">
                <name>POTASSIUM ION</name>
                <molecular_weight>
                    <theoretical units="MDa">3.9098e-05</theoretical>
                </molecular_weight>
                <number_of_copies>4</number_of_copies>
                <formula>K</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">1</concentration>
                    <buffer>
                        <ph>7.2</ph>
                        <details>Phosphate buffered saline</details>
                    </buffer>
                    <grid>
                        <model>C-flat-2/2</model>
                        <material>COPPER</material>
                        <mesh>400</mesh>
                        <support_film film_type_id="1">
                            <film_material>CARBON</film_material>
                            <film_topology>HOLEY ARRAY</film_topology>
                        </support_film>
                        <pretreatment>
                            <type>GLOW DISCHARGE</type>
                            <time units="s">4</time>
                            <atmosphere>AIR</atmosphere>
                        </pretreatment>
                    </grid>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                        <chamber_humidity units="percentage">100</chamber_humidity>
                        <chamber_temperature units="K">277</chamber_temperature>
                        <instrument>FEI VITROBOT MARK IV</instrument>
                    </vitrification>
                    <details>Purified virions were incubated in the presence of purified ectodomain fragments.</details>
                </single_particle_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <single_particle_microscopy microscopy_id="1">
                    <microscope>FEI TITAN 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_magnification>75000.0</nominal_magnification>
                    <specimen_holder_model>FEI TITAN KRIOS AUTOGRID HOLDER</specimen_holder_model>
                    <cooling_holder_cryogen>NITROGEN</cooling_holder_cryogen>
                    <image_recording_list>
                        <image_recording image_recording_id="1">
                            <film_or_detector_model>FEI FALCON III (4k x 4k)</film_or_detector_model>
                            <detector_mode>INTEGRATING</detector_mode>
                            <number_grids_imaged>1</number_grids_imaged>
                            <number_real_images>13865</number_real_images>
                            <average_electron_dose_per_image units="e/Å^2">63.0</average_electron_dose_per_image>
                            <details>Each micrograph was recorded as a movie of 50 individual fractions with a total dose of 63 e/angstrom squared</details>
                        </image_recording>
                    </image_recording_list>
                </single_particle_microscopy>
            </microscopy_list>
            <singleparticle_processing image_processing_id="1">
                <image_recording_id>1</image_recording_id>
                <details>Images were motion-corrected using motioncor2
Defocus estimation was performed using GCTF</details>
                <particle_selection>
                    <number_selected>129884</number_selected>
                    <details>Autopicking in Relion</details>
                </particle_selection>
                <ctf_correction>
                    <software_list>
                        <software>
                            <name>Gctf</name>
                        </software>
                    </software_list>
                    <details>CTF correction was implemented through Relion</details>
                    <type>PHASE FLIPPING AND AMPLITUDE CORRECTION</type>
                </ctf_correction>
                <startup_model type_of_model="OTHER">
                    <details>Previously published models calculated at lower resolution.</details>
                </startup_model>
                <final_reconstruction>
                    <applied_symmetry>
                        <point_group>C1</point_group>
                    </applied_symmetry>
                    <resolution units="Å" res_type="BY AUTHOR">3.75</resolution>
                    <resolution_method>FSC 0.143 CUT-OFF</resolution_method>
                    <software_list>
                        <software>
                            <name>RELION</name>
                            <version>2.1</version>
                        </software>
                    </software_list>
                    <details>Origins and orientations were originally assigned by 3D auto refinement with full icosahedral symmetry. Random group assignment was carried through the focussed classification process and used to divide the data into two roughly even halves that had been initially refined independently.</details>
                    <number_images_used>58510</number_images_used>
                </final_reconstruction>
                <initial_angle_assignment>
                    <type>PROJECTION MATCHING</type>
                    <projection_matching_processing/>
                    <software_list>
                        <software>
                            <name>RELION</name>
                            <version>2.1</version>
                        </software>
                    </software_list>
                </initial_angle_assignment>
                <final_angle_assignment>
                    <type>MAXIMUM LIKELIHOOD</type>
                    <software_list>
                        <software>
                            <name>RELION</name>
                            <version>2.1</version>
                        </software>
                    </software_list>
                </final_angle_assignment>
                <final_three_d_classification>
                    <number_classes>10</number_classes>
                    <software_list>
                        <software>
                            <name>RELION</name>
                            <version>2.1</version>
                        </software>
                    </software_list>
                    <details>Origin and orientation values were initially determined by 3D auto refine in RELION, assuming full icosahedral symmetry (i.e. with full gold-standard methods). Once orientations were accurately determined relion_symmetry_expand was used to produce a STAR file with 60 orientations per particle. This was used for a focussed classification experiment in which a cylindrical mask was applied to a single three-fold axis for 3D classification without orientation refinement. One class showed the presence of the previously detected portal assembly. Particles contributed a median 3 views each. NOTE The reconstruction half-sets were calculated with C1 symmetry, however as three views per particle are present that are derived from icosahedral redundancy, C3 symmetry is imposed by the data.</details>
                </final_three_d_classification>
            </singleparticle_processing>
        </structure_determination>
    </structure_determination_list>
    <map format="CCP4" size_kbytes="864001">
        <file>emd_0056.map.gz</file>
        <symmetry>
            <space_group>1</space_group>
        </symmetry>
        <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
        <dimensions>
            <col>600</col>
            <row>600</row>
            <sec>600</sec>
        </dimensions>
        <origin>
            <col>-300</col>
            <row>-300</row>
            <sec>-300</sec>
        </origin>
        <spacing>
            <x>600</x>
            <y>600</y>
            <z>600</z>
        </spacing>
        <cell>
            <a units="Å">639.00006</a>
            <b units="Å">639.00006</b>
            <c units="Å">639.00006</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>-0.11780139</minimum>
            <maximum>0.21274377</maximum>
            <average>0.00095921505</average>
            <std>0.013303866</std>
        </statistics>
        <pixel_spacing>
            <x units="Å">1.065</x>
            <y units="Å">1.065</y>
            <z units="Å">1.065</z>
        </pixel_spacing>
        <contour_list>
            <contour primary="true">
                <level>0.05</level>
                <source>AUTHOR</source>
            </contour>
        </contour_list>
        <label>::::EMDATABANK.org::::EMD-0056::::</label>
        <annotation_details>C3 reconstruction of Feline Calicivirus decorated with a soluble ectodomain fragment of the cellular receptor feline junctional adhesion molecule A.</annotation_details>
    </map>
</emd>
