<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-2000" 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>2011-12-01</deposition>
         <header_release>2011-12-16</header_release>
         <map_release>2012-04-17</map_release>
         <update>2012-10-24</update>
      </key_dates>
      <title>ATP-triggered molecular mechanics of the chaperonin GroEL</title>
      <authors_list>
         <author>Clare DK</author>
         <author>Vasishtan D</author>
         <author>Stagg S</author>
         <author>Quispe J</author>
         <author>Farr GW</author>
         <author>Topf M</author>
         <author>Horwich AL</author>
         <author>Saibil HR</author>
      </authors_list>
      <keywords>Tetradecamer of GroEL with ATP bound in one ring</keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Clare DK</author>
               <author order="2">Vasishtan D</author>
               <author order="3">Stagg S</author>
               <author order="4">Quispe J</author>
               <author order="5">Farr GW</author>
               <author order="6">Topf M</author>
               <author order="7">Horwich AL</author>
               <author order="8">Saibil HR</author>
               <title>ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin.</title>
               <journal>CELL(CAMBRIDGE,MASS.)</journal>
               <volume>149</volume>
               <first_page>113</first_page>
               <last_page>123</last_page>
               <year>2012</year>
               <external_references type="PUBMED">22445172</external_references>
               <external_references type="DOI">doi:10.1016/j.cell.2012.02.047</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
      <pdb_list>
         <pdb_reference>
            <pdb_id>4aas</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
      </pdb_list>
   </crossreferences>
   <sample>
      <name>GroEL-ATP7 Rs_open</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>GroEL-ATP7 Rs_open</name>
            <oligomeric_state>Tetradecamer of GroEL with 7 ATP molecules bound</oligomeric_state>
            <number_unique_components>2</number_unique_components>
            <molecular_weight>
               <experimental units="MDa">0.8</experimental>
               <theoretical units="MDa">0.8</theoretical>
            </molecular_weight>
         </sample_supramolecule>
      </supramolecule_list>
      <macromolecule_list>
         <protein_or_peptide macromolecule_id="1">
            <name synonym="GroEL">hsp60</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
               <cellular_location>cytoplasm</cellular_location>
            </natural_source>
            <molecular_weight>
               <experimental units="MDa">0.056</experimental>
               <theoretical units="MDa">0.056</theoretical>
            </molecular_weight>
            <details>ATPase mutant, D398A</details>
            <number_of_copies>14</number_of_copies>
            <oligomeric_state>tetradecamer</oligomeric_state>
            <recombinant_exp_flag>true</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               <recombinant_organism ncbi="562">Escherichia coli</recombinant_organism>
            </recombinant_expression>
            <sequence>
               <external_references type="GO">GO:0042026</external_references>
               <external_references type="INTERPRO">IPR002423</external_references>
            </sequence>
         </protein_or_peptide>
         <ligand macromolecule_id="2">
            <name synonym="ATP">ATP</name>
            <natural_source database="NCBI">
               <organism ncbi="32630">synthetic construct</organism>
            </natural_source>
            <molecular_weight>
               <experimental units="MDa">0.00055</experimental>
               <theoretical units="MDa">0.00055</theoretical>
            </molecular_weight>
            <details>ATP is bound to seven subunits of one ring</details>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
         </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">4</concentration>
               <buffer>
                  <ph>7.4</ph>
                  <details>50 mM Tris-HCl pH 7.4, 50 mM KCl, 10 mM MgCl2 and 200uM ATP</details>
               </buffer>
               <grid>
                  <details>cflat grids r2/2</details>
               </grid>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <chamber_humidity units="percentage">100</chamber_humidity>
                  <chamber_temperature units="K">95</chamber_temperature>
                  <instrument>OTHER</instrument>
                  <details>Vitrification instrument: Vitrobot</details>
                  <timed_resolved_state>Vitrified within 30 seconds</timed_resolved_state>
                  <method>Grids were blotted for 2-3 seconds</method>
               </vitrification>
            </single_particle_preparation>
         </specimen_preparation_list>
         <microscopy_list>
            <single_particle_microscopy microscopy_id="1">
               <microscope>FEI TECNAI F20</microscope>
               <illumination_mode>FLOOD BEAM</illumination_mode>
               <imaging_mode>BRIGHT FIELD</imaging_mode>
               <electron_source>FIELD EMISSION GUN</electron_source>
               <acceleration_voltage units="kV">120</acceleration_voltage>
               <nominal_cs units="mm">2</nominal_cs>
               <nominal_defocus_min units="&#181;m">0.7</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">3.5</nominal_defocus_max>
               <calibrated_magnification>148500.0</calibrated_magnification>
               <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
               <temperature>
                  <temperature_min units="K">95</temperature_min>
                  <temperature_max units="K">95</temperature_max>
                  <temperature_average units="K">95</temperature_average>
               </temperature>
               <details>The data were collected with Leginon at SCRIPPS</details>
               <image_recording_list>
                  <image_recording>
                     <film_or_detector_model category="CCD">GATAN ULTRASCAN 4000 (4k x 4k)</film_or_detector_model>
                     <average_electron_dose_per_image units="e/&#8491;^2">15</average_electron_dose_per_image>
                  </image_recording>
               </image_recording_list>
               <specimen_holder>Eucentric</specimen_holder>
            </single_particle_microscopy>
         </microscopy_list>
         <singleparticle_processing image_processing_id="1">
            <details>The particles were automatically picked using FindEM</details>
            <ctf_correction>
               <details>Each particle was phase flipped</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>C7</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">8.5</resolution>
               <resolution_method>FSC 0.5 CUT-OFF</resolution_method>
               <software_list>
                  <software>
                     <name>SPIDER, IMAGIC</name>
                  </software>
               </software_list>
               <details>SIRT was used to reconstruct the final map</details>
               <number_images_used>5500</number_images_used>
            </final_reconstruction>
            <final_angle_assignment>
               <details>theta 80-100, phi 0-51.42</details>
            </final_angle_assignment>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="27649">
      <file>emd_2000.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
      <dimensions>
         <col>192</col>
         <row>192</row>
         <sec>192</sec>
      </dimensions>
      <origin>
         <col>-96</col>
         <row>-96</row>
         <sec>-96</sec>
      </origin>
      <spacing>
         <x>192</x>
         <y>192</y>
         <z>192</z>
      </spacing>
      <cell>
         <a units="&#8491;">387.84</a>
         <b units="&#8491;">387.84</b>
         <c units="&#8491;">387.84</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>-1.717103</minimum>
         <maximum>2.61815715</maximum>
         <average>0.00811408</average>
         <std>0.1052276</std>
      </statistics>
      <pixel_spacing>
         <x units="&#8491;">2.02</x>
         <y units="&#8491;">2.02</y>
         <z units="&#8491;">2.02</z>
      </pixel_spacing>
      <contour_list>
         <contour primary="true">
            <level>0.2</level>
            <source>AUTHOR</source>
         </contour>
      </contour_list>
      <annotation_details>The GroEL-ATP7 Rs_open map is one of seven maps calculated from a heterogenous sample</annotation_details>
      <details>::::EMDATABANK.org::::EMD-2000::::</details>
   </map>
   <interpretation>
      <modelling_list>
         <modelling>
            <initial_model>
               <access_code>1OEL</access_code>
            </initial_model>
            <refinement_protocol>FLEXIBLE FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>Chimera, Flex-EM, NAMD2.6</name>
               </software>
            </software_list>
            <details>Protocol: Flexible fitting</details>
            <target_criteria>Cross-correlation coefficient</target_criteria>
            <refinement_space>REAL</refinement_space>
         </modelling>
      </modelling_list>
   </interpretation>
</emd>