+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-36041 | |||||||||
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Title | ion channel | |||||||||
Map data | ||||||||||
Sample |
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Keywords | ion channel / TRANSPORT PROTEIN | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Chen HW / Jiang DH | |||||||||
Funding support | China, 1 items
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Citation | Journal: To Be Published Title: ion channel Authors: Chen HW / Jiang DH | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_36041.map.gz | 59.6 MB | EMDB map data format | |
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Header (meta data) | emd-36041-v30.xml emd-36041.xml | 13.8 KB 13.8 KB | Display Display | EMDB header |
Images | emd_36041.png | 46 KB | ||
Filedesc metadata | emd-36041.cif.gz | 5.4 KB | ||
Others | emd_36041_half_map_1.map.gz emd_36041_half_map_2.map.gz | 59.2 MB 59.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-36041 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36041 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_36041.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_36041_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_36041_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : ion channel complex
Entire | Name: ion channel complex |
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Components |
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-Supramolecule #1: ion channel complex
Supramolecule | Name: ion channel complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: ion channel
Macromolecule | Name: ion channel / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 91.684469 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MIAAIHNARR KKREAAAAHK AQHRTAENSM DSLEDSTHET DAGERAQAGS TKLAWTDVVA PPPRKVVFWL PHQRKVFDFY ASQGVQYFT AFLIVSNFIF NCAEKEWDPY TDQLYQGLWR WGEFAFNTMF LIELLINFYG IAFCFWRYNW AWNTFDLVVV A IGTLTMAE ...String: MIAAIHNARR KKREAAAAHK AQHRTAENSM DSLEDSTHET DAGERAQAGS TKLAWTDVVA PPPRKVVFWL PHQRKVFDFY ASQGVQYFT AFLIVSNFIF NCAEKEWDPY TDQLYQGLWR WGEFAFNTMF LIELLINFYG IAFCFWRYNW AWNTFDLVVV A IGTLTMAE AIGGNFMPPS MALIRNLRAF RIFRLFKRIK SLNKIIVSLG KAIPGVANAF VIMVIIMCIY AILGVEFYHM TG SDGTYVT YNDNVKRGLC TGDEVELGQC SLNQTVSSET ARGYTYGEEY YGTFFRALYT LFQVLTGESW SEAVARPAVF ESH YDSFGP VLFYVSFIII CQIVLINVVV AVLLDKMVEE DDSEDPEKQT VAEKLSEMLS QEHAQLREIF RTWDEDNSGT ISIK EWRKA VKSMGYRGPI DVLDQIFASM DKDHSGELDY AEIDRMLSPT AARERRSSTH ANPKRSVKEE VVAMRAEFTD HVARL ETQI AALVLELQLQ RKPCGAEAPA PAHSRLAHDS DGAPTEPPPP AAPDHHHLED DEDTTQRVAA ALEVLFQGPS KGEELF TGV VPILVELDGD VNGHKFSVRG EGEGDATNGK LTLKFICTTG KLPVPWPTLV TTLTYGVQCF SRYPDHMKRH DFFKSAM PE GYVQERTISF KDDGTYKTRA EVKFEGDTLV NRIELKGIDF KEDGNILGHK LEYNFNSHNV YITADKQKNG IKANFKIR H NVEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSVLSK DPNEKRDHMV LLEFVTAAGI THGMDEWSHP QFEKGGGSG GGSGGSAWSH PQFEK |
-Macromolecule #2: ILE-ALA-ALA-ILE-HIS-ASN-ALA-ARG-ARG-LYS-LYS-ARG-GLU-ALA-ALA-ALA-A...
Macromolecule | Name: ILE-ALA-ALA-ILE-HIS-ASN-ALA-ARG-ARG-LYS-LYS-ARG-GLU-ALA-ALA-ALA-ALA-HIS-LYS-ALA type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 2.191584 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: IAAIHNARRK KREAAAAHKA |
-Macromolecule #3: water
Macromolecule | Name: water / type: ligand / ID: 3 / Number of copies: 1 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 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: 1.2 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 59377 |
Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |