+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-26588 | |||||||||
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Title | Human NKCC1 K289NA492E Bound with Furosemide | |||||||||
Map data | ||||||||||
Sample |
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Keywords | SLC12A2 / Outward-open / Furosemide / MEMBRANE PROTEIN | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Zhao Y / Cao E | |||||||||
Funding support | 1 items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structural basis for inhibition of the Cation-chloride cotransporter NKCC1 by the diuretic drug bumetanide Authors: Zhao Y / Roy K / Vidossich P / Cancedda L / De Vivo M / Forbush B / Cao E | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_26588.map.gz | 59.6 MB | EMDB map data format | |
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Header (meta data) | emd-26588-v30.xml emd-26588.xml | 11.1 KB 11.1 KB | Display Display | EMDB header |
Images | emd_26588.png | 56.5 KB | ||
Filedesc metadata | emd-26588.cif.gz | 3.6 KB | ||
Others | emd_26588_half_map_1.map.gz emd_26588_half_map_2.map.gz | 59.3 MB 59.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-26588 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26588 | HTTPS FTP |
-Validation report
Summary document | emd_26588_validation.pdf.gz | 834.3 KB | Display | EMDB validaton report |
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Full document | emd_26588_full_validation.pdf.gz | 833.9 KB | Display | |
Data in XML | emd_26588_validation.xml.gz | 12.2 KB | Display | |
Data in CIF | emd_26588_validation.cif.gz | 14.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26588 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26588 | HTTPS FTP |
-Related structure data
Related structure data | 7s1xC 7s1yC 7s1zC C: citing same article (ref.) |
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EM raw data | EMPIAR-11050 (Title: Cryo-EM structure of human NKCC1 K289NA492E bound with Furosemide Data size: 1.6 TB Data #1: Cryo-EM structure of human NKCC1 K289NA492E bound with Furosemide [micrographs - multiframe]) |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_26588.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: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_26588_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_26588_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : hNKCC1-Furosemide complex
Entire | Name: hNKCC1-Furosemide complex |
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Components |
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-Supramolecule #1: hNKCC1-Furosemide complex
Supramolecule | Name: hNKCC1-Furosemide complex / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 2 mg/mL |
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Buffer | pH: 7.4 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 47.0 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: 5.0 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1521495 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |