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- EMDB-7130: Cryo-EM structure of ENaC -

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Basic information

Entry
Database: EMDB / ID: EMD-7130
TitleCryo-EM structure of ENaC
Map dataUnsharpened map
Sample
  • Cell: Membrane protein complex
    • Protein or peptide: SCNN1A
    • Protein or peptide: SCNN1B
    • Protein or peptide: EGFP-SCNN1G chimera
    • Protein or peptide: 7B1 fab
    • Protein or peptide: 7B1 fab
    • Protein or peptide: 10D4 fab
    • Protein or peptide: 10D4 fab
Keywordssodium channel / MEMBRANE PROTEIN
Function / homology
Function and homology information


sensory perception of salty taste / Sensory perception of salty taste / sensory perception of sour taste / neutrophil-mediated killing of bacterium / leukocyte activation involved in inflammatory response / aldosterone metabolic process / cellular response to vasopressin / sperm principal piece / sodium channel complex / ligand-gated sodium channel activity ...sensory perception of salty taste / Sensory perception of salty taste / sensory perception of sour taste / neutrophil-mediated killing of bacterium / leukocyte activation involved in inflammatory response / aldosterone metabolic process / cellular response to vasopressin / sperm principal piece / sodium channel complex / ligand-gated sodium channel activity / epithelial fluid transport / sodium ion homeostasis / mucus secretion / artery smooth muscle contraction / renal system process / neutrophil activation involved in immune response / cellular response to aldosterone / multicellular organismal-level water homeostasis / cellular response to acidic pH / sodium ion import across plasma membrane / potassium ion homeostasis / intracellular sodium ion homeostasis / motile cilium / sodium channel activity / erythrocyte homeostasis / response to food / ciliary membrane / WW domain binding / sodium ion transport / monoatomic ion channel activity / sodium ion transmembrane transport / acrosomal vesicle / cytoplasmic vesicle membrane / multicellular organism growth / Stimuli-sensing channels / regulation of blood pressure / gene expression / response to xenobiotic stimulus / apical plasma membrane / external side of plasma membrane / extracellular exosome / nucleoplasm / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Epithelial sodium channel, chordates / Epithelial sodium channel, conserved site / Amiloride-sensitive sodium channels signature. / Epithelial sodium channel / Amiloride-sensitive sodium channel
Similarity search - Domain/homology
Amiloride-sensitive sodium channel subunit alpha / Amiloride-sensitive sodium channel subunit beta / Amiloride-sensitive sodium channel subunit gamma
Similarity search - Component
Biological speciesHomo sapiens (human) / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsNoreng S / Bharadwaj A
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/Office of the Director United States
CitationJournal: Elife / Year: 2018
Title: Structure of the human epithelial sodium channel by cryo-electron microscopy.
Authors: Sigrid Noreng / Arpita Bharadwaj / Richard Posert / Craig Yoshioka / Isabelle Baconguis /
Abstract: The epithelial sodium channel (ENaC), a member of the ENaC/DEG superfamily, regulates Na and water homeostasis. ENaCs assemble as heterotrimeric channels that harbor protease-sensitive domains ...The epithelial sodium channel (ENaC), a member of the ENaC/DEG superfamily, regulates Na and water homeostasis. ENaCs assemble as heterotrimeric channels that harbor protease-sensitive domains critical for gating the channel. Here, we present the structure of human ENaC in the uncleaved state determined by single-particle cryo-electron microscopy. The ion channel is composed of a large extracellular domain and a narrow transmembrane domain. The structure reveals that ENaC assembles with a 1:1:1 stoichiometry of α:β:γ subunits arranged in a counter-clockwise manner. The shape of each subunit is reminiscent of a hand with key gating domains of a 'finger' and a 'thumb.' Wedged between these domains is the elusive protease-sensitive inhibitory domain poised to regulate conformational changes of the 'finger' and 'thumb'; thus, the structure provides the first view of the architecture of inhibition of ENaC.
History
DepositionNov 28, 2017-
Header (metadata) releaseDec 20, 2017-
Map releaseOct 10, 2018-
UpdateOct 30, 2024-
Current statusOct 30, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 2.8
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 2.8
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6bqn
  • Surface level: 5
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6bqn
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_7130.png

Downloads & links

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Map

FileDownload / File: emd_7130.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationUnsharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.33 Å/pix.
x 384 pix.
= 510.72 Å		1.33 Å/pix.
x 384 pix.
= 510.72 Å		1.33 Å/pix.
x 384 pix.
= 510.72 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.33 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 2.8 / Movie #1: 2.8
Minimum - Maximum-6.5600395 - 18.49389
Average (Standard dev.)0.007006216 (±0.36086926)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 510.72003 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.331.331.33
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z510.720510.720510.720
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-6.56018.4940.007

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Supplemental data

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Mask #1

Fileemd_7130_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Sharpened map

Fileemd_7130_additional.map
AnnotationSharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 1

Fileemd_7130_half_map_1.map
AnnotationHalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2

Fileemd_7130_half_map_2.map
AnnotationHalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Membrane protein complex

EntireName: Membrane protein complex
Components
  • Cell: Membrane protein complex
    • Protein or peptide: SCNN1A
    • Protein or peptide: SCNN1B
    • Protein or peptide: EGFP-SCNN1G chimera
    • Protein or peptide: 7B1 fab
    • Protein or peptide: 7B1 fab
    • Protein or peptide: 10D4 fab
    • Protein or peptide: 10D4 fab

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Supramolecule #1: Membrane protein complex

SupramoleculeName: Membrane protein complex / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: SCNN1A

MacromoleculeName: SCNN1A / type: protein_or_peptide / ID: 1
Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to ...Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to flexible areas of the protein where density is missing. The full sequence is described in sequence details.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.038953 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) SYPVSLNINL NSDKL VFPA VTICTLNPYR ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) SYPVSLNINL NSDKL VFPA VTICTLNPYR YPEIKEELEE LDRITEQTLF DLYKYSSFTT LVAGSRSRAD LRGTLPHPLQ ALAVPPPPHG AAAAAS VAS SLRDNNPQVD WKDWKIGFQL CNQNKSDCFY QTYSSGVDAV AEWYAFHYIN ILSRLPETLP SLEEDTLGNF IFACRFN QV SCNQANYSHF HHPMYGNCYT FNDKNNSNLW MSSMPGINNG LSLMLRAEQN DFIPLLSTVT GARVMVHGQD EPAFMDDG G FNLRPGVETS ISMRKETLDR LGGDYGDCTK NGSDVPVENL YPSKYTQQVC IHSCFQESMI KECGCAYIFY PRPQNVEYC DYRKHSSWGY CYYKLQVDFS SDHLGCFTKC RKPCSVTSYQ LSAGYSRWPS VTSQEWVFQM LSRQNNYTVN NKRNGVAKVN IFFKELNYK TNSESPSVT(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #2: SCNN1B

MacromoleculeName: SCNN1B / type: protein_or_peptide / ID: 2
Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to ...Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to flexible areas of the protein where density is missing. The full sequence is described in sequence details.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.038633 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)TYLS WEVSVSLSVG FKTMDFPAVT ICNASPFKYS K IKHLLKDL DELMEAVLER ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)TYLS WEVSVSLSVG FKTMDFPAVT ICNASPFKYS K IKHLLKDL DELMEAVLER ILAPELSHAN ATRNLNFSIW NHTPLVLIDE RNPHHPMVLD LFGDNHNGLT SSSASEKICN AH GCKMAMR LCSLNRTQCT FRNFTSATQA LTEWYILQAT NIFAQVPQQE LVEMSYPGEQ MILACLFGAE PCNYRNFTSI FYP HYGNCY IFNWGMTEKA LPSANPGTEF GLKLILDIGQ EDYVPFLAST AGVRLMLHEQ RSYPFIRDEG IYAMSGTETS IGVL VDKLQ RMGEPYSPCT VNGSEVPVQN FYSDYNTTYS IQACLRSCFQ DHMIRNCNCG HYLYPLPRGE KYCNNRDFPD WAHCY SDLQ MSVAQRETCI GMCKESCNDT QYKMTISMAD WPSEASEDWI FHVLSQERDQ STNITLSRKG IVKLNIYFQE FNYRTI EES AANNI(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)

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Macromolecule #3: EGFP-SCNN1G chimera

MacromoleculeName: EGFP-SCNN1G chimera / type: protein_or_peptide / ID: 3
Details: The protein is EGFP-SCNN1G chimera. Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. ...Details: The protein is EGFP-SCNN1G chimera. Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to flexible areas of the protein where density is missing. The first 260 residues is a His8 tag and a strep-tag followed by EGFP (UniProt accession code: C5MKY7). The full sequence is described in sequence details.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.834457 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) FYTVSVSIKV HFRKL DFPA VTICNINPYK ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) FYTVSVSIKV HFRKL DFPA VTICNINPYK YSTVRHLLAD LEQETREALK SLYGFPESAA AAEAESWNSV SEGKQPRFSH RIPLLIFDQD EKGKAR DFF TGQQQQVGGS IIHKASNVMH IESKQVVGFQ LCSNDTSDCA TYTFSSGINA IQEWYKLHYM NIMAQVPLEK KINMSYS AE ELLVTCFFDG VSCDARNFTL FHHPMHGNCY TFNNRENETI LSTSMGGSEY GLQVILYINE EEYNPFLVSS TGAKVIIH R QDEYPFVEDV GTEIETAMVT SIGMHLTESF KLSEPYSQCT EDGSDVPIRN IYNAAYSLQI CLHSCFQTKM VEKCGCAQY SQPLPPAANY CNYQQHPNWM YCYYQLHRAF VQEELGCQSV CKEACSFKEW TLTTSLAQWP SVVSEKWLLP VLTWDQGRQV NKKLNKTDL AKLLIFYKDL NQRSIMESPA NSI(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)

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Macromolecule #4: 7B1 fab

MacromoleculeName: 7B1 fab / type: protein_or_peptide / ID: 4 / Details: Sequence unknown, built with poly UNK. / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 9.039134 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)

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Macromolecule #5: 7B1 fab

MacromoleculeName: 7B1 fab / type: protein_or_peptide / ID: 5 / Details: Sequence unknown, built with poly UNK. / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 10.315707 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #6: 10D4 fab

MacromoleculeName: 10D4 fab / type: protein_or_peptide / ID: 6 / Details: Sequence unknown, built with poly UNK. / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 9.805078 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)

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Macromolecule #7: 10D4 fab

MacromoleculeName: 10D4 fab / type: protein_or_peptide / ID: 7 / Details: Sequence unknown, built with poly UNK. / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 9.549763 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 304615
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: PROJECTION MATCHING

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