<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-1049" version="3.0.1.1" xsi:schemaLocation="https://github.com/emdb-empiar/emdb-schemas/blob/master/v3/v3_0_1_1/emdb_relaxed.xsd">
   <admin>
      <current_status>
         <code>REL</code>
         <processing_site>PDBe</processing_site>
      </current_status>
      <sites>
         <deposition>PDBe</deposition>
         <last_processing>PDBe</last_processing>
      </sites>
      <key_dates>
         <deposition>2003-05-29</deposition>
         <header_release>2003-05-19</header_release>
         <map_release>2003-06-03</map_release>
         <update>2012-10-24</update>
      </key_dates>
      <title>A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid.</title>
      <authors_list>
         <author>Neumann E</author>
         <author>Moser R</author>
         <author>Snyers L</author>
         <author>Blaas D</author>
         <author>Hewat EA</author>
      </authors_list>
      <keywords>
         </keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Neumann E</author>
               <author order="2">Moser R</author>
               <author order="3">Snyers L</author>
               <author order="4">Blaas D</author>
               <author order="5">Hewat EA</author>
               <title>A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid.</title>
               <journal>J.VIROL.</journal>
               <volume>77</volume>
               <first_page>8504</first_page>
               <last_page>8511</last_page>
               <year>2003</year>
               <external_references type="PUBMED">12857919</external_references>
               <external_references type="DOI">doi:10.1128/JVI.77.15.8504-8511.2003</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
   </crossreferences>
   <sample>
      <name>Human Rhinovirus 2 in complex with its cellular receptor, VLDL-R</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>Human Rhinovirus 2 in complex with its cellular receptor, VLDL-R</name>
            <number_unique_components>2</number_unique_components>
         </sample_supramolecule>
         <virus_supramolecule supramolecule_id="1">
            <name>Human rhinovirus 2</name>
            <sci_species_name ncbi="12130">Human rhinovirus 2</sci_species_name>
            <natural_host database="NCBI">
               <organism ncbi="9606">Homo sapiens</organism>
               <synonym_organism>VERTEBRATES</synonym_organism>
            </natural_host>
            <host_system database="NCBI">
               </host_system>
            <virus_shell shell_id="1">
               <diameter units="&#8491;">300</diameter>
            </virus_shell>
            <virus_type>VIRION</virus_type>
            <virus_isolate>SEROTYPE</virus_isolate>
            <virus_enveloped>false</virus_enveloped>
            <virus_empty>false</virus_empty>
         </virus_supramolecule>
         <organelle_or_cellular_component_supramolecule supramolecule_id="2">
            <name synonym="Very Low Density Lipoprotein - Receptor">Cellular Receptor</name>
            <details>The VLDL-R consists of eight imperfect
 ligand-binding repeats of approximately 40 amino
 acids at its N-terminus. Recombinant
 VLDL-minireceptors encompassing different
 ligand-binding repeats are here expressed with the first
 three repeats + a Maltose Binding
 Protein fused to the N-terminus + a
 Hexa-his-tag fused to the C-terminus.</details>
            <recombinant_exp_flag>true</recombinant_exp_flag>
            <natural_source database="NCBI">
               <organism ncbi="9606">Homo sapiens</organism>
               <synonym_organism>Human</synonym_organism>
               <tissue>muscle</tissue>
            </natural_source>
            <recombinant_expression database="NCBI">
               <recombinant_organism ncbi="562">Escherichia coli</recombinant_organism>
               <recombinant_plasmid>pMALTM-c2x</recombinant_plasmid>
            </recombinant_expression>
         </organelle_or_cellular_component_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">
               <concentration units="mg/mL">0.82</concentration>
               <buffer>
                  <ph>7.4</ph>
                  <details>50 mM Tris-HCl for the virus  2 mM CaCl2, 20 mM
          Tris-HCL for       the receptor fragment</details>
               </buffer>
               <grid>
                  <details>300 mesh copper grid</details>
               </grid>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <method>Blot with filter paper for 1-2 seconds</method>
               </vitrification>
            </single_particle_preparation>
         </specimen_preparation_list>
         <microscopy_list>
            <single_particle_microscopy microscopy_id="1">
               <microscope>JEOL 2010F</microscope>
               <illumination_mode>SPOT SCAN</illumination_mode>
               <imaging_mode>BRIGHT FIELD</imaging_mode>
               <electron_source>FIELD EMISSION GUN</electron_source>
               <acceleration_voltage units="kV">200</acceleration_voltage>
               <nominal_cs units="mm">1.4</nominal_cs>
               <nominal_defocus_min units="&#181;m">1.18</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">2.9</nominal_defocus_max>
               <nominal_magnification>40000.0</nominal_magnification>
               <calibrated_magnification>39700.0</calibrated_magnification>
               <specimen_holder_model>OTHER</specimen_holder_model>
               <alignment_procedure>
                  <legacy>
                     <astigmatism>objective lens astigmatism was corrected at
        300,000       times magnification</astigmatism>
                  </legacy>
               </alignment_procedure>
               <image_recording_list>
                  <image_recording>
                     <film_or_detector_model category="FILM">KODAK SO-163 FILM</film_or_detector_model>
                     <digitization_details>
                        <scanner>OTHER</scanner>
                        <sampling_interval units="&#181;m">7</sampling_interval>
                     </digitization_details>
                     <number_real_images>33</number_real_images>
                     <average_electron_dose_per_image units="e/&#8491;^2">15</average_electron_dose_per_image>
                     <details>Zeiss PhotoScan TD scanner</details>
                  </image_recording>
               </image_recording_list>
               <specimen_holder>Oxford cryo-holder CT3200</specimen_holder>
            </single_particle_microscopy>
         </microscopy_list>
         <singleparticle_processing image_processing_id="1">
            <details>HRV2 and receptor fragment were incubated for 1
          hour       at 4       degree Celcius.</details>
            <ctf_correction>
               <details>CTFMIX</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>I</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">16.0</resolution>
               <resolution_method>FSC 0.5 CUT-OFF</resolution_method>
               <details>Methods for reconstructing density maps of
        "single" particles from cryoelectron micrographs to
        subnanometer resolution (Conway et al.,J Struct Biol. 1999 Dec            1;128(1):106-18.)</details>
               <number_images_used>912</number_images_used>
            </final_reconstruction>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="32387">
      <file>emd_1049.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS SIGNED INTEGER (2 BYTES)</data_type>
      <dimensions>
         <col>255</col>
         <row>255</row>
         <sec>255</sec>
      </dimensions>
      <origin>
         <col>-127</col>
         <row>-127</row>
         <sec>-127</sec>
      </origin>
      <spacing>
         <x>255</x>
         <y>255</y>
         <z>255</z>
      </spacing>
      <cell>
         <a units="&#8491;">448.8</a>
         <b units="&#8491;">448.8</b>
         <c units="&#8491;">448.8</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>-17360.0</minimum>
         <maximum>25708.0</maximum>
         <average>312.54598999000001</average>
         <std>3491.530029300000024</std>
      </statistics>
      <pixel_spacing>
         <x units="&#8491;">1.76</x>
         <y units="&#8491;">1.76</y>
         <z units="&#8491;">1.76</z>
      </pixel_spacing>
      <contour_list>
         <contour primary="true">
            <level>4380.0</level>
            <source>AUTHOR</source>
         </contour>
      </contour_list>
      <annotation_details>This is a 3D reconstruction of HRV2/MBP-VLDLR(-123)</annotation_details>
      <details>::::EMDATABANK.org::::EMD-1049::::</details>
   </map>
   <interpretation>
      <modelling_list>
         <modelling>
            <refinement_protocol>RIGID BODY FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>O</name>
               </software>
            </software_list>
            <details>Protocol: Manual docking. Fitting the X-RAY structures of HRV2 and the VLDL-R repeats to the cryo-electron microscope reconstructed density. Determination of the residues included in the footprints.</details>
            <refinement_space>REAL</refinement_space>
         </modelling>
      </modelling_list>
   </interpretation>
</emd>