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Yorodumi- EMDB-65300: Structure of the phosphomimetic mutant CAX1 in Arabidopsis thalia... -
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Open data
- Basic information
Basic information
| Entry |  | |||||||||
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| Title | Structure of the phosphomimetic mutant CAX1 in Arabidopsis thaliana in the Calcium-bound state | |||||||||
|  Map data | ||||||||||
|  Sample | 
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|  Keywords | Calcium / Transporter / Proton / CAX1 / TRANSPORT PROTEIN | |||||||||
| Function / homology |  Function and homology information calcium:proton antiporter complex / calcium:proton antiporter activity / lithium ion transport / plant-type vacuole membrane / cold acclimation / intracellular manganese ion homeostasis / regulation of stomatal movement / phosphate ion homeostasis / plant-type vacuole / vacuole ...calcium:proton antiporter complex / calcium:proton antiporter activity / lithium ion transport / plant-type vacuole membrane / cold acclimation / intracellular manganese ion homeostasis / regulation of stomatal movement / phosphate ion homeostasis / plant-type vacuole / vacuole / intracellular zinc ion homeostasis / monoatomic cation transport / response to salt stress / intracellular calcium ion homeostasis / calcium ion transport Similarity search - Function | |||||||||
| Biological species |   Arabidopsis thaliana (thale cress) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
|  Authors | Sun L / Wang K | |||||||||
| Funding support |  China, 1 items 
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|  Citation |  Journal: To Be Published Title: Structure of the phosphomimetic mutant CAX1 in Arabidopsis thaliana in the Calcium-bound state Authors: Sun L / Wang K | |||||||||
| History | 
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- Structure visualization
Structure visualization
| Supplemental images | 
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- Downloads & links
Downloads & links
-EMDB archive
| Map data |  emd_65300.map.gz | 59.7 MB |  EMDB map data format | |
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| Header (meta data) |  emd-65300-v30.xml  emd-65300.xml | 15 KB 15 KB | Display Display |  EMDB header | 
| Images |  emd_65300.png | 142.4 KB | ||
| Masks |  emd_65300_msk_1.map | 64 MB |  Mask map | |
| Filedesc metadata |  emd-65300.cif.gz | 5.5 KB | ||
| Others |  emd_65300_half_map_1.map.gz  emd_65300_half_map_2.map.gz | 59.3 MB 59.3 MB | ||
| Archive directory |  http://ftp.pdbj.org/pub/emdb/structures/EMD-65300  ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65300 | HTTPS FTP | 
-Validation report
| Summary document |  emd_65300_validation.pdf.gz | 805.2 KB | Display |  EMDB validaton report | 
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| Full document |  emd_65300_full_validation.pdf.gz | 804.7 KB | Display | |
| Data in XML |  emd_65300_validation.xml.gz | 12.4 KB | Display | |
| Data in CIF |  emd_65300_validation.cif.gz | 14.7 KB | Display | |
| Arichive directory |  https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-65300  ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-65300 | HTTPS FTP | 
-Related structure data
| Related structure data |  9vscMC 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 | 
- Links
Links
| EMDB pages |  EMDB (EBI/PDBe) /  EMDataResource | 
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- Map
Map
| File |  Download / File: emd_65300.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
 
 Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||
| Density | 
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML: 
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-Supplemental data
-Mask #1
| File |  emd_65300_msk_1.map | ||||||||||||
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| Projections & Slices | 
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| Density Histograms | 
-Half map: #1
| File | emd_65300_half_map_1.map | ||||||||||||
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| Projections & Slices | 
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| Density Histograms | 
-Half map: #2
| File | emd_65300_half_map_2.map | ||||||||||||
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| Projections & Slices | 
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| Density Histograms | 
- Sample components
Sample components
-Entire : CAX1 trimer
| Entire | Name: CAX1 trimer | 
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| Components | 
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-Supramolecule #1: CAX1 trimer
| Supramolecule | Name: CAX1 trimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 | 
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| Source (natural) | Organism:   Arabidopsis thaliana (thale cress) | 
-Macromolecule #1: Vacuolar cation/proton exchanger 1
| Macromolecule | Name: Vacuolar cation/proton exchanger 1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO | 
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| Source (natural) | Organism:   Arabidopsis thaliana (thale cress) | 
| Molecular weight | Theoretical: 51.32141 KDa | 
| Recombinant expression | Organism:  Homo sapiens (human) | 
| Sequence | String: MAGIVTEPWS VAENGNPSIT AKGSSRELRL GRTAHNMDDD DLRKKSDLRV IQKVPYKGLK DFLSNLQEVI LGTKLAILFP  AIPAAIICT YCGVSQPWIF GLSLLGLTPL AERVSFLTEQ LAFYTGPTLG GLLNATCGNA TELIIAILAL TNNKVAVVKY S LLGSILSN  ...String: MAGIVTEPWS VAENGNPSIT AKGSSRELRL GRTAHNMDDD DLRKKSDLRV IQKVPYKGLK DFLSNLQEVI LGTKLAILFP  AIPAAIICT YCGVSQPWIF GLSLLGLTPL AERVSFLTEQ LAFYTGPTLG GLLNATCGNA TELIIAILAL TNNKVAVVKY S LLGSILSN LLLVLGTSLF CGGIANIRRE QRFDRKQADV NFFLLLLGFL CHLLPLLVGY LKNGEASAAV LSDMQLSISR GF SIVMLIS YIAYLVFQLW THRQLFDAQE QEDEYDDDVE QETAVISFWS GFAWLVGMTL VIALLSEYVV ATIEEASDKW NLS VSFISI ILLPIVGNAA EHAGAVIFAF KNKLDISLGV ALGSATQIGL FVVPLTIIVA WILGINMDLN FGPLETGCLA VSII ITAFT LQDGSSHYMK GLVLLLCYFI IAICFFVDKL PQKQNAIHLG HQAMNNVVTA TGGGVFSSDY KDDDDK UniProtKB: Vacuolar cation/proton exchanger 1 | 
-Macromolecule #2: CALCIUM ION
| Macromolecule | Name: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 3 / Formula: CA | 
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| Molecular weight | Theoretical: 40.078 Da | 
-Experimental details
-Structure determination
| Method | cryo EM | 
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|  Processing | single particle reconstruction | 
| Aggregation state | particle | 
- Sample preparation
Sample preparation
| Buffer | pH: 7.4 | 
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| Vitrification | Cryogen name: ETHANE | 
- Electron microscopy
Electron microscopy
| Microscope | TFS KRIOS | 
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 | 
| Electron beam | Acceleration voltage: 300 kV / Electron source:  FIELD EMISSION GUN | 
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm | 
| Experimental equipment |  Model: Titan Krios / Image courtesy: FEI Company | 
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