<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-1045" 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>2003-04-15</deposition>
         <header_release>2003-05-12</header_release>
         <map_release>2004-01-06</map_release>
         <update>2012-10-24</update>
      </key_dates>
      <title>Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process.</title>
      <authors_list>
         <author>Valle M</author>
         <author>Sengupta J</author>
         <author>Swami NK</author>
         <author>Grassucci RA</author>
         <author>Burkhardt N</author>
         <author>Nierhaus KH</author>
         <author>Agrawal RK</author>
         <author>Frank J</author>
      </authors_list>
      <keywords>
         </keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Valle M</author>
               <author order="2">Sengupta J</author>
               <author order="3">Swami NK</author>
               <author order="4">Grassucci RA</author>
               <author order="5">Burkhardt N</author>
               <author order="6">Nierhaus KH</author>
               <author order="7">Agrawal RK</author>
               <author order="8">Frank J</author>
               <title>Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process.</title>
               <journal>EMBO J.</journal>
               <volume>21</volume>
               <first_page>3557</first_page>
               <last_page>3567</last_page>
               <year>2002</year>
               <external_references type="PUBMED">12093756</external_references>
               <external_references type="DOI">doi:10.1093/emboj/cdf326</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
      <pdb_list>
         <pdb_reference>
            <pdb_id>1ls2</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
         <pdb_reference>
            <pdb_id>1lu3</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
      </pdb_list>
   </crossreferences>
   <sample>
      <name>70S aa-tRNA-EF-Tu.GDP.kirromycin complex from E.coli</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>70S aa-tRNA-EF-Tu.GDP.kirromycin complex from E.coli</name>
            <number_unique_components>6</number_unique_components>
            <molecular_weight>
               <experimental units="MDa">2.5</experimental>
               <theoretical units="MDa">2.5</theoretical>
            </molecular_weight>
         </sample_supramolecule>
         <complex_supramolecule supramolecule_id="1">
            <name>E.coli 70S ribosome</name>
            <details>10 pmol</details>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
            <ribosome-details>ribosome-prokaryote: ALL</ribosome-details>
         </complex_supramolecule>
      </supramolecule_list>
      <macromolecule_list>
         <rna macromolecule_id="1">
            <name>aa-tRNA</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <details>14 pmol; fMet-tRNA(fMet) at the P site and Phe-tRNA(phe)
 at the A site</details>
            <classification>TRANSFER</classification>
            <structure>DOUBLE HELIX</structure>
            <synthetic_flag>false</synthetic_flag>
         </rna>
         <ligand macromolecule_id="2">
            <name>EF-Tu</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <details>20 pmol</details>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
         </ligand>
         <ligand macromolecule_id="3">
            <name>GDP</name>
            <natural_source database="NCBI">
               <organism ncbi="32630">synthetic construct</organism>
            </natural_source>
            <details>8 ul of 2.5mM; [Alpha-(32)P]GTP The radioactivity contributed by
 the Alpha-(32)P moiety of the GDP served to
 calculate a ~50% occupancy for the elongation factor.</details>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
         </ligand>
         <ligand macromolecule_id="4">
            <name>kirromycin</name>
            <natural_source database="NCBI">
               <organism ncbi="32630">synthetic construct</organism>
            </natural_source>
            <details>3 ul of 100 mM; antibiotic</details>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
         </ligand>
         <ligand macromolecule_id="5">
            <name>MF-mRNA</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <details>15 pmol; M(Met).F(Phe)-mRNA</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">
               <buffer>
                  <ph>7.5</ph>
                  <details>20 mM HEPES-KOH, 6mM MgCl2, 150mM NH4Cl, 4mM
          2-metcaptoethanol, 0.05 mM spermine and 2 mM spermidine</details>
               </buffer>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <chamber_humidity units="percentage">30</chamber_humidity>
                  <chamber_temperature units="K">93</chamber_temperature>
                  <instrument>HOMEMADE PLUNGER</instrument>
                  <details>Vitrification instrument: two side blotting plunger</details>
                  <method>Blot for 2 seconds before plunging</method>
               </vitrification>
            </single_particle_preparation>
         </specimen_preparation_list>
         <microscopy_list>
            <single_particle_microscopy microscopy_id="1">
               <microscope>FEI/PHILIPS EM420</microscope>
               <illumination_mode>FLOOD BEAM</illumination_mode>
               <imaging_mode>BRIGHT FIELD</imaging_mode>
               <electron_source>LAB6</electron_source>
               <acceleration_voltage units="kV">100</acceleration_voltage>
               <nominal_cs units="mm">2.0</nominal_cs>
               <nominal_defocus_min units="&#181;m">1.041</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">3.844</nominal_defocus_max>
               <nominal_magnification>49000.0</nominal_magnification>
               <calibrated_magnification>52000.0</calibrated_magnification>
               <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
               <temperature>
                  <temperature_average units="K">93</temperature_average>
               </temperature>
               <details>Microscope: Philips EM420  Imaging date: 1997</details>
               <date>1998-06-01</date>
               <image_recording_list>
                  <image_recording>
                     <film_or_detector_model category="FILM">KODAK SO-163 FILM</film_or_detector_model>
                     <digitization_details>
                        <scanner>ZEISS SCAI</scanner>
                        <sampling_interval units="&#181;m">14</sampling_interval>
                     </digitization_details>
                     <number_real_images>45</number_real_images>
                     <average_electron_dose_per_image units="e/&#8491;^2">10</average_electron_dose_per_image>
                     <od_range>1.2</od_range>
                     <bits_per_pixel>12.</bits_per_pixel>
                  </image_recording>
               </image_recording_list>
               <specimen_holder>Cryo transfer</specimen_holder>
            </single_particle_microscopy>
         </microscopy_list>
         <singleparticle_processing image_processing_id="1">
            <ctf_correction>
               <details>defocus groups</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>C1</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">16.8</resolution>
               <resolution_method>FSC 0.5 CUT-OFF</resolution_method>
               <software_list>
                  <software>
                     <name>SPIDER</name>
                  </software>
               </software_list>
               <details>Final map was calculated from 8 CTF corrected
        defocus groups</details>
               <number_images_used>7985</number_images_used>
            </final_reconstruction>
            <final_angle_assignment>
               <details>SPIDER definition</details>
            </final_angle_assignment>
            <final_two_d_classification>
               <number_classes>2</number_classes>
            </final_two_d_classification>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="9827">
      <file>emd_1045.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
      <dimensions>
         <col>136</col>
         <row>136</row>
         <sec>136</sec>
      </dimensions>
      <origin>
         <col>-68</col>
         <row>-68</row>
         <sec>-68</sec>
      </origin>
      <spacing>
         <x>136</x>
         <y>136</y>
         <z>136</z>
      </spacing>
      <cell>
         <a units="&#8491;">365.84</a>
         <b units="&#8491;">365.84</b>
         <c units="&#8491;">365.84</c>
         <alpha units="deg">90</alpha>
         <beta units="deg">90</beta>
         <gamma units="deg">90</gamma>
      </cell>
      <axis_order>
         <fast>X</fast>
         <medium>Y</medium>
         <slow>Z</slow>
      </axis_order>
      <statistics>
         <minimum>-82.174800000000005</minimum>
         <maximum>184.76400000000001</maximum>
         <average>4.36412</average>
         <std>20.063500000000001</std>
      </statistics>
      <pixel_spacing>
         <x units="&#8491;">2.69</x>
         <y units="&#8491;">2.69</y>
         <z units="&#8491;">2.69</z>
      </pixel_spacing>
      <contour_list>
         <contour primary="true">
            <level>48.299999999999997</level>
         </contour>
      </contour_list>
      <annotation_details>70S aa-tRNA-EF-Tu.GDP.kirromycin complex</annotation_details>
      <details>::::EMDATABANK.org::::EMD-1045::::</details>
   </map>
   <interpretation>
      <modelling_list>
         <modelling>
            <initial_model>
               <access_code>1EFC</access_code>
            </initial_model>
            <refinement_protocol>RIGID BODY FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>manual</name>
               </software>
            </software_list>
            <details>Protocol: Rigid Body. The EF-Tu domains were separately fitted by manual docking using program O (pdb codes for fitted coordinates: 1LS2, 1LU3)</details>
            <target_criteria>cross correlation coefficient</target_criteria>
         </modelling>
      </modelling_list>
   </interpretation>
</emd>