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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Pseudomonas aeruginosa ATPase State2b Fo focused | |||||||||
Map data | Pseudomonas aeruginosa ATPase State2b Fo focused | |||||||||
Sample |
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Keywords | ATPase / energy / ELECTRON TRANSPORT | |||||||||
| Function / homology | Function and homology informationproton motive force-driven plasma membrane ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / lipid binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.66 Å | |||||||||
Authors | Stewart AG / Sobti M | |||||||||
| Funding support | Australia, 1 items
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Citation | Journal: To Be PublishedTitle: Distinct Structural Features of Pseudomonas aeruginosa ATP Synthase Revealed by Cryo Electron Microscopy Authors: Sobti M / Stewart AG | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_70006.map.gz | 230.2 MB | EMDB map data format | |
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| Header (meta data) | emd-70006-v30.xml emd-70006.xml | 17 KB 17 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_70006_fsc.xml | 13.1 KB | Display | FSC data file |
| Images | emd_70006.png | 56.3 KB | ||
| Filedesc metadata | emd-70006.cif.gz | 5.7 KB | ||
| Others | emd_70006_half_map_1.map.gz emd_70006_half_map_2.map.gz | 226.7 MB 226.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70006 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70006 | HTTPS FTP |
-Validation report
| Summary document | emd_70006_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_70006_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_70006_validation.xml.gz | 21.6 KB | Display | |
| Data in CIF | emd_70006_validation.cif.gz | 27.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70006 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-70006 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9o1gMC ![]() 9o19C ![]() 9o1aC ![]() 9o1bC ![]() 9o1cC ![]() 9o1dC ![]() 9o1eC ![]() 9o1fC ![]() 9o1hC ![]() 9o1jC ![]() 9o1kC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_70006.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Pseudomonas aeruginosa ATPase State2b Fo focused | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Half Map B
| File | emd_70006_half_map_1.map | ||||||||||||
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| Annotation | Half Map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half Map A
| File | emd_70006_half_map_2.map | ||||||||||||
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| Annotation | Half Map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Pseudomonas aeruginosa ATPase
| Entire | Name: Pseudomonas aeruginosa ATPase |
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| Components |
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-Supramolecule #1: Pseudomonas aeruginosa ATPase
| Supramolecule | Name: Pseudomonas aeruginosa ATPase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: ATP synthase subunit c
| Macromolecule | Name: ATP synthase subunit c / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 8.61138 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: METVVGLTAI AVALLIGLGA LGTAIGFGLL GGKFLEGAAR QPEMVPMLQV KMFIVAGLLD AVTMIGVGIA LFFTFANPFV GQIAG UniProtKB: ATP synthase subunit c |
-Macromolecule #2: ATP synthase subunit b
| Macromolecule | Name: ATP synthase subunit b / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 16.978346 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MNINATLIGQ SVAFFIFVLF CMKFVWPPVI AALQERQKKI ADGLDAANRA ARDLELAHEK AGQQLREAKA QAAEIVEQAK KRANQIVDE ARDQARTEGE RLKAQAQAEI EQELNSVKDA LRAQVGALAV TGAEKILGAS IDANAHEQLV SKLAAEI UniProtKB: ATP synthase subunit b |
-Macromolecule #3: ATP synthase subunit a
| Macromolecule | Name: ATP synthase subunit a / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 31.944635 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAAETASGYI QHHLQNLTFG RLPNGDWGFA HTAEQAKEMG FWAFHVDTLG WSVLLGVVFL FIFRLAAKKA TSGQPGGLQN FVEVMVEFV DTSVKDTFHG RNPLIAPLAL TVFVWIFLLN LIDLVPVDYL PMLAAKITGD EHLFFRAVAT TDPNATLGLS I SVFALIVF ...String: MAAETASGYI QHHLQNLTFG RLPNGDWGFA HTAEQAKEMG FWAFHVDTLG WSVLLGVVFL FIFRLAAKKA TSGQPGGLQN FVEVMVEFV DTSVKDTFHG RNPLIAPLAL TVFVWIFLLN LIDLVPVDYL PMLAAKITGD EHLFFRAVAT TDPNATLGLS I SVFALIVF YSIKVKGIGG FLGELTLHPF SSKNIVVQIL LIPVNFLLEF VTLIAKPVSL ALRLFGNMYA GELIFILIAV MF GSGMFLL SALGVALNWA WAVFHILIIT LQAFIFMMLT IVYLSMAHED NH UniProtKB: ATP synthase subunit a |
-Macromolecule #4: ZINC ION
| Macromolecule | Name: ZINC ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: ZN |
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| Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 65.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Australia, 1 items
Citation
























Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN

