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- EMDB-51568: Human adult muscle nAChR in resting state in detergent with alpha... -

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Basic information

Entry
Database: EMDB / ID: EMD-51568
TitleHuman adult muscle nAChR in resting state in detergent with alpha-bungarotoxin
Map dataCryoSPARC map used for final model refinement, sharpened with a b-factor of -20
Sample
  • Complex: Human adult muscle nAChR in resting state in detergent with alpha-bungarotoxin
    • Protein or peptide: Acetylcholine receptor subunit alpha
    • Protein or peptide: Acetylcholine receptor subunit beta
    • Protein or peptide: Fab35 light chain
    • Protein or peptide: Acetylcholine receptor subunit delta
    • Protein or peptide: Acetylcholine receptor subunit epsilon,Green fluorescent protein
    • Protein or peptide: Fab35 heavy chain
    • Protein or peptide: Alpha-bungarotoxin
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
KeywordsLigand-gated ion channel / nicotinic receptor / pLGIC / cys-loop receptor / MEMBRANE PROTEIN
Function / homology
Function and homology information


postsynaptic membrane organization / skeletal muscle tissue growth / musculoskeletal movement / Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / Highly calcium permeable nicotinic acetylcholine receptors / Highly calcium permeable postsynaptic nicotinic acetylcholine receptors / acetylcholine receptor activity / acetylcholine-gated channel complex / behavioral response to nicotine / acetylcholine receptor inhibitor activity ...postsynaptic membrane organization / skeletal muscle tissue growth / musculoskeletal movement / Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / Highly calcium permeable nicotinic acetylcholine receptors / Highly calcium permeable postsynaptic nicotinic acetylcholine receptors / acetylcholine receptor activity / acetylcholine-gated channel complex / behavioral response to nicotine / acetylcholine receptor inhibitor activity / neuromuscular synaptic transmission / acetylcholine-gated monoatomic cation-selective channel activity / muscle cell development / ion channel regulator activity / acetylcholine binding / synaptic transmission, cholinergic / monoatomic cation transmembrane transporter activity / nervous system process / acetylcholine receptor signaling pathway / ligand-gated monoatomic ion channel activity / postsynaptic specialization membrane / neuromuscular process / muscle cell cellular homeostasis / neuromuscular junction development / monoatomic cation transport / membrane depolarization / skeletal muscle contraction / neuronal action potential / muscle contraction / bioluminescence / generation of precursor metabolites and energy / response to nicotine / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / neuromuscular junction / neuron cellular homeostasis / transmembrane signaling receptor activity / channel activity / toxin activity / monoatomic ion transmembrane transport / chemical synaptic transmission / postsynaptic membrane / neuron projection / synapse / cell surface / signal transduction / extracellular region / plasma membrane
Similarity search - Function
Snake toxin, conserved site / Snake toxins signature. / : / Snake toxin cobra-type / Snake three-finger toxin / Nicotinic acetylcholine receptor / Snake toxin-like superfamily / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain ...Snake toxin, conserved site / Snake toxins signature. / : / Snake toxin cobra-type / Snake three-finger toxin / Nicotinic acetylcholine receptor / Snake toxin-like superfamily / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Green fluorescent protein, GFP / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein
Similarity search - Domain/homology
Acetylcholine receptor subunit alpha / Acetylcholine receptor subunit beta / Green fluorescent protein / Alpha-bungarotoxin / Acetylcholine receptor subunit epsilon / Acetylcholine receptor subunit delta
Similarity search - Component
Biological speciesHomo sapiens (human) / Rattus norvegicus (Norway rat) / Bungarus multicinctus (many-banded krait)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.96 Å
AuthorsLi A / Pike ACW / Chi G / Webster R / Maxwell S / Liu W / Beeson D / Sauer DB / Dong YY
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Wellcome Trust102161/Z/13/Z United Kingdom
Medical Research Council (MRC, United Kingdom)MR/Y012623/1 United Kingdom
CitationJournal: Cell Rep / Year: 2025
Title: Structures of the human adult muscle-type nicotinic receptor in resting and desensitized states.
Authors: Anna Li / Ashley C W Pike / Richard Webster / Susan Maxwell / Wei-Wei Liu / Gamma Chi / Jacqueline Palace / David Beeson / David B Sauer / Yin Yao Dong /
Abstract: Muscle-type nicotinic acetylcholine receptor (AChR) is the key signaling molecule in neuromuscular junctions. Here, we present the structures of full-length human adult receptors in complex with ...Muscle-type nicotinic acetylcholine receptor (AChR) is the key signaling molecule in neuromuscular junctions. Here, we present the structures of full-length human adult receptors in complex with Fab35 in α-bungarotoxin (αBuTx)-bound resting states and ACh-bound desensitized states. In addition to identifying the conformational changes during recovery from desensitization, we also used electrophysiology to probe the effects of eight previously unstudied AChR genetic variants found in patients with congenital myasthenic syndrome (CMS), revealing they cause either slow- or fast-channel CMS characterized by prolonged or abbreviated ion channel bursts. The combined kinetic and structural data offer a better understanding of both the AChR state transition and the pathogenic mechanisms of disease variants.
History
DepositionSep 18, 2024-
Header (metadata) releaseMay 14, 2025-
Map releaseMay 14, 2025-
UpdateMay 14, 2025-
Current statusMay 14, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51568.png

Downloads & links

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Map

FileDownload / File: emd_51568.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryoSPARC map used for final model refinement, sharpened with a b-factor of -20
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.93 Å/pix.
x 432 pix.
= 402.624 Å		0.93 Å/pix.
x 432 pix.
= 402.624 Å		0.93 Å/pix.
x 432 pix.
= 402.624 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.932 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.57571495 - 1.0713643
Average (Standard dev.)0.00047831837 (±0.024210691)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions432432432
Spacing432432432
CellA=B=C: 402.624 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_51568_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Mask #2

Fileemd_51568_msk_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: unsharpened map from cryoSPARC non-uniform refinement

Fileemd_51568_additional_1.map
Annotationunsharpened map from cryoSPARC non-uniform refinement
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map B from cryoSPARC non-uniform refinement

Fileemd_51568_half_map_1.map
Annotationhalf map B from cryoSPARC non-uniform refinement
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map A from cryoSPARC non-uniform refinement

Fileemd_51568_half_map_2.map
Annotationhalf map A from cryoSPARC non-uniform refinement
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human adult muscle nAChR in resting state in detergent with alpha...

EntireName: Human adult muscle nAChR in resting state in detergent with alpha-bungarotoxin
Components
  • Complex: Human adult muscle nAChR in resting state in detergent with alpha-bungarotoxin
    • Protein or peptide: Acetylcholine receptor subunit alpha
    • Protein or peptide: Acetylcholine receptor subunit beta
    • Protein or peptide: Fab35 light chain
    • Protein or peptide: Acetylcholine receptor subunit delta
    • Protein or peptide: Acetylcholine receptor subunit epsilon,Green fluorescent protein
    • Protein or peptide: Fab35 heavy chain
    • Protein or peptide: Alpha-bungarotoxin
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Human adult muscle nAChR in resting state in detergent with alpha...

SupramoleculeName: Human adult muscle nAChR in resting state in detergent with alpha-bungarotoxin
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 / Details: nAChR in complex with alpha-bungarotoxin and Fab35
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 402 KDa

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Macromolecule #1: Acetylcholine receptor subunit alpha

MacromoleculeName: Acetylcholine receptor subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 49.747645 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SEHETRLVAK LFKDYSSVVR PVEDHRQVVE VTVGLQLIQL INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPD LVLYNNADGD FAIVKFTKVL LQYTGHITWT PPAIFKSYCE IIVTHFPFDE QNCSMKLGTW TYDGSVVAIN P ESDQPDLS ...String:
SEHETRLVAK LFKDYSSVVR PVEDHRQVVE VTVGLQLIQL INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPD LVLYNNADGD FAIVKFTKVL LQYTGHITWT PPAIFKSYCE IIVTHFPFDE QNCSMKLGTW TYDGSVVAIN P ESDQPDLS NFMESGEWVI KESRGWKHSV TYSCCPDTPY LDITYHFVMQ RLPLYFIVNV IIPCLLFSFL TGLVFYLPTD SG EKMTLSI SVLLSLTVFL LVIVELIPST SSAVPLIGKY MLFTMVFVIA SIIITVIVIN THHRSPSTHV MPNWVRKVFI DTI PNIMFF STMKRPSREK QDKKIFTEDI DISDISGKPG PPPMGFHSPL IKHPEVKSAI EGIKYIAETM KSDQESNNAA AEWK YVAMV MDHILLGVFM LVCIIGTLAV FAGRLIELNQ QG

UniProtKB: Acetylcholine receptor subunit alpha

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Macromolecule #2: Acetylcholine receptor subunit beta

MacromoleculeName: Acetylcholine receptor subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.596477 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: SEAEGRLREK LFSGYDSSVR PAREVGDRVR VSVGLILAQL ISLNEKDEEM STKVYLDLEW TDYRLSWDPA EHDGIDSLRI TAESVWLPD VVLLNNNDGN FDVALDISVV VSSDGSVRWQ PPGIYRSSCS IQVTYFPFDW QNCTMVFSSY SYDSSEVSLQ T GLGPDGQG ...String:
SEAEGRLREK LFSGYDSSVR PAREVGDRVR VSVGLILAQL ISLNEKDEEM STKVYLDLEW TDYRLSWDPA EHDGIDSLRI TAESVWLPD VVLLNNNDGN FDVALDISVV VSSDGSVRWQ PPGIYRSSCS IQVTYFPFDW QNCTMVFSSY SYDSSEVSLQ T GLGPDGQG HQEIHIHEGT FIENGQWEII HKPSRLIQPP GDPRGGREGQ RQEVIFYLII RRKPLFYLVN VIAPCILITL LA IFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE TSLSVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMP LWVRQI FIHKLPLYLR LKRPKPERDL MPEPPHCSSP GSGWGRGTDE YFIRKPPSDF LFPKPNRFQP ELSAPDLRRF IDGP NRAVA LLPELREVVS SISYIARQLQ EQEDHDALKE DWQFVAMVVD RLFLWTFIIF TSVGTLVIFL DATYHLPPPD PFP

UniProtKB: Acetylcholine receptor subunit beta

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Macromolecule #3: Fab35 light chain

MacromoleculeName: Fab35 light chain / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 23.392982 KDa
Recombinant expressionOrganism: Rattus norvegicus (Norway rat)
SequenceString: DIVITQSPSL LSASVGDRVT LTCKGSQNID NYLAWYQQKL GEAPKLLIYK TNSLQTGIPS RFSGSGSGTD YTLTISSLHS EDLATYYCY QYINGYTFGT GTKLELKRAD AAPTVSIFPP STEQLATGGA SVVCLMNNFY PRDISVKWKI DGTERRDGVL D SVTDQDSK ...String:
DIVITQSPSL LSASVGDRVT LTCKGSQNID NYLAWYQQKL GEAPKLLIYK TNSLQTGIPS RFSGSGSGTD YTLTISSLHS EDLATYYCY QYINGYTFGT GTKLELKRAD AAPTVSIFPP STEQLATGGA SVVCLMNNFY PRDISVKWKI DGTERRDGVL D SVTDQDSK DSTYSMSSTL SLTKADYESH NLYTCEVVHK TSSSPVVKSF NRNEC

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Macromolecule #4: Acetylcholine receptor subunit delta

MacromoleculeName: Acetylcholine receptor subunit delta / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 56.915359 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: LNEEERLIRH LFQEKGYNKE LRPVAHKEES VDVALALTLS NLISLKEVEE TLTTNVWIEH GWTDNRLKWN AEEFGNISVL RLPPDMVWL PEIVLENNND GSFQISYSCN VLVYHYGFVY WLPPAIFRSS CPISVTYFPF DWQNCSLKFS SLKYTAKEIT L SLKQDAKE ...String:
LNEEERLIRH LFQEKGYNKE LRPVAHKEES VDVALALTLS NLISLKEVEE TLTTNVWIEH GWTDNRLKWN AEEFGNISVL RLPPDMVWL PEIVLENNND GSFQISYSCN VLVYHYGFVY WLPPAIFRSS CPISVTYFPF DWQNCSLKFS SLKYTAKEIT L SLKQDAKE NRTYPVEWII IDPEGFTENG EWEIVHRPAR VNVDPRAPLD SPSRQDITFY LIIRRKPLFY IINILVPCVL IS FMVNLVF YLPADSGEKT SVAISVLLAQ SVFLLLISKR LPATSMAIPL IGKFLLFGMV LVTMVVVICV IVLNIHFRTP STH VLSEGV KKLFLETLPE LLHMSRPAED GPSPGALVRR SSSLGYISKA EEYFLLKSRS DLMFEKQSER HGLARRLTTA RRPP ASSEQ AQQELFNELK PAVDGANFIV NHMRDQNNYN EEKDSWNRVA RTVDRLCLFV VTPVMVVGTA WIFLQGVYNQ PPPQP FPGD PYSYNVQDKR FI

UniProtKB: Acetylcholine receptor subunit delta

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Macromolecule #5: Acetylcholine receptor subunit epsilon,Green fluorescent protein

MacromoleculeName: Acetylcholine receptor subunit epsilon,Green fluorescent protein
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 80.60375 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: KNEELRLYHH LFNNYDPGSR PVREPEDTVT ISLKVTLTNL ISLNEKEETL TTSVWIGIDW QDYRLNYSKD DFGGIETLRV PSELVWLPE IVLENNIDGQ FGVAYDANVL VYEGGSVTWL PPAIYRSVCA VEVTYFPFDW QNCSLIFRSQ TYNAEEVEFT F AVDNDGKT ...String:
KNEELRLYHH LFNNYDPGSR PVREPEDTVT ISLKVTLTNL ISLNEKEETL TTSVWIGIDW QDYRLNYSKD DFGGIETLRV PSELVWLPE IVLENNIDGQ FGVAYDANVL VYEGGSVTWL PPAIYRSVCA VEVTYFPFDW QNCSLIFRSQ TYNAEEVEFT F AVDNDGKT INKIDIDTEA YTENGEWAID FCPGVIRRHH GGATDGPGET DVIYSLIIRR KPLFYVINII VPCVLISGLV LL AYFLPAQ AGGQKCTVSI NVLLAQTVFL FLIAQKIPET SLSVPLLGRF LIFVMVVATL IVMNCVIVLN VSQRTPTTHA MSP RLRHVL LELLPRLLGS PPPPEAPRAP PVATMVSKGE ELFTGVVPIL VELDGDVNGH KFSVSGEGEG DATYGKLTLK FICT TGKLP VPWPTLVTTL TYGVQCFSRY PDHMKQHDFF KSAMPEGYVQ ERTIFFKDDG NYKTRAEVKF EGDTLVNRIE LKGID FKED GNILGHKLEY NYNSHNVYIM ADKQKNGIKV NFKIRHNIED GSVQLADHYQ QNTPIGDGPV LLPDNHYLST QSALSK DPN EKRDHMVLLE FVTAAGITLG MDELYKAPRA ASPPRRASSV GLLLRAEELI LKKPRSELVF EGQRHRQGTW TAAFCQS LG AAAPEVRCCV DAVNFVAEST RDQEATGEEV SDWVRMGNAL DNICFWAALV LFSVGSSLIF LGAYFNRVPD LPYAPCIQ P

UniProtKB: Acetylcholine receptor subunit epsilon, Green fluorescent protein, Acetylcholine receptor subunit epsilon

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Macromolecule #6: Fab35 heavy chain

MacromoleculeName: Fab35 heavy chain / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 23.879758 KDa
Recombinant expressionOrganism: Rattus norvegicus (Norway rat)
SequenceString: EVQLQESGPG LVQPSETLSL TCTVSGFSLT SYSVSWLRQP SGKGPEWMGR MWDDGGTVYN SGLKSRLSIS RDTSKNQVFL KMNSLQTDD TGTYYCTRDE RIRAINWFAY WGQGTLVTVS SAETTAPSVY PLAPGTALKS NSMVTLGCLV KGYFPEPVTV T WNSGALSS ...String:
EVQLQESGPG LVQPSETLSL TCTVSGFSLT SYSVSWLRQP SGKGPEWMGR MWDDGGTVYN SGLKSRLSIS RDTSKNQVFL KMNSLQTDD TGTYYCTRDE RIRAINWFAY WGQGTLVTVS SAETTAPSVY PLAPGTALKS NSMVTLGCLV KGYFPEPVTV T WNSGALSS GVHTFPAVLQ SGLYTLTSSV TVPSSTWPSQ TVTCNVAHPG QQHQRWTRKL C

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Macromolecule #7: Alpha-bungarotoxin

MacromoleculeName: Alpha-bungarotoxin / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bungarus multicinctus (many-banded krait)
Molecular weightTheoretical: 8.005281 KDa
SequenceString:
IVCHTTATSP ISAVTCPPGE NLCYRKMWCD AFCSSRGKVV ELGCAATCPS KKPYEEVTCC STDKCNPHPK QRPG

UniProtKB: Alpha-bungarotoxin

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Macromolecule #13: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 13 / Number of copies: 1 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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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

Concentration1.68 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
150.0 mMNaClsodium chloride
0.013 %C24H46O11n-Dodecyl-beta-D-Maltopyaranoside
0.0013 %C31H50O4Cholesteryl hemisuccinate

Details: 20 mM HEPES pH 7.5, 150 mM NaCl, 0.013% DDM, 0.0013% CHS
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.35 K / Instrument: FEI VITROBOT MARK IV / Details: blot time 2s, blot force -10.
DetailsThis sample was monodisperse

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV
Detailsobjective aperture 70 um
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Number real images: 18672 / Average exposure time: 4.71 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1249235 / Details: Extracted by topaz picking
CTF correctionSoftware - Name: cryoSPARC (ver. 3.3.1) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: ab-initio model from cryoSPARC
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.96 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.3.1) / Details: Non-uniform refinement / Number images used: 31022
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.1)
Final 3D classificationNumber classes: 10 / Avg.num./class: 34490 / Software - Name: RELION (ver. 3.1.3)
Details: Class3D without alignment (10 classes, t=20) with a mask covering the transmembrane domain of nAChR
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

2708

source_name: AlphaFold, initial_model_type: in silico model

1230

source_name: AlphaFold, initial_model_type: in silico model

7001

source_name: AlphaFold, initial_model_type: in silico model

4844

source_name: AlphaFold, initial_model_type: in silico model
DetailsInitial fitting of alphafold models using chimeraX followed by manual rebuilding in COOT and final refinement in ISOLDE and PHENIX
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9gu0:
Human adult muscle nAChR in resting state in detergent with alpha-bungarotoxin

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