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- PDB-8d9v: gamma-Arf1 homodimeric interface within AP-1, Arf1, Nef lattice o... -

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Basic information

Entry
Database: PDB / ID: 8d9v
Titlegamma-Arf1 homodimeric interface within AP-1, Arf1, Nef lattice on narrow membrane tubes
Components
  • (AP-1 complex subunit ...) x 4
  • ADP ribosylation factor 1
  • HLA class I histocompatibility antigen, A alpha chain
  • Protein Nef
KeywordsVIRAL PROTEIN / nef / AP / HIV / trafficking
Function / homology
Function and homology information


basolateral protein secretion / : / AP-1 adaptor complex / endosome to melanosome transport / Lysosome Vesicle Biogenesis / mitotic cleavage furrow ingression / protein trimerization / platelet dense granule organization / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / melanosome assembly ...basolateral protein secretion / : / AP-1 adaptor complex / endosome to melanosome transport / Lysosome Vesicle Biogenesis / mitotic cleavage furrow ingression / protein trimerization / platelet dense granule organization / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / melanosome assembly / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / Golgi Associated Vesicle Biogenesis / symbiont-mediated suppression of host apoptosis / symbiont-mediated suppression of host autophagy / clathrin adaptor activity / MHC class II antigen presentation / CD4 receptor binding / thioesterase binding / determination of left/right symmetry / clathrin-coated vesicle / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / TAP complex binding / clathrin binding / Golgi medial cisterna / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / Lysosome Vesicle Biogenesis / CD8 receptor binding / Golgi Associated Vesicle Biogenesis / antigen processing and presentation of exogenous peptide antigen via MHC class I / cell leading edge / beta-2-microglobulin binding / MHC class I protein binding / endoplasmic reticulum exit site / host cell Golgi membrane / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / TAP binding / protection from natural killer cell mediated cytotoxicity / intracellular copper ion homeostasis / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / detection of bacterium / protein targeting / T cell receptor binding / vesicle-mediated transport / clathrin-coated pit / regulation of calcium-mediated signaling / viral life cycle / Neutrophil degranulation / MHC class II antigen presentation / cytoplasmic vesicle membrane / Nef mediated downregulation of MHC class I complex cell surface expression / sarcomere / trans-Golgi network membrane / kidney development / lumenal side of endoplasmic reticulum membrane / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / intracellular protein transport / trans-Golgi network / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / MHC class I peptide loading complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / cellular response to virus / peptide antigen binding / SH3 domain binding / positive regulation of T cell mediated cytotoxicity / virion component / positive regulation of type II interferon production / recycling endosome membrane / phagocytic vesicle membrane / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon gamma signaling / Interferon alpha/beta signaling / antibacterial humoral response / synaptic vesicle / protein transport / E3 ubiquitin ligases ubiquitinate target proteins / presynapse / T cell receptor signaling pathway / heart development / ATPase binding / ER-Phagosome pathway / early endosome membrane / early endosome / defense response to Gram-positive bacterium / immune response / symbiont-mediated suppression of host innate immune response / protein domain specific binding / Golgi membrane / external side of plasma membrane / signaling receptor binding / lysosomal membrane / innate immune response
Similarity search - Function
AP-1 complex subunit sigma / Adaptor protein complex AP-1, gamma subunit / Gamma-adaptin ear (GAE) domain / Gamma-adaptin ear (GAE) domain profile. / HIV-1 Nef protein, anchor domain superfamily / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / HIV negative factor Nef / AP-1/2/4 complex subunit beta / Adaptor protein complex, sigma subunit ...AP-1 complex subunit sigma / Adaptor protein complex AP-1, gamma subunit / Gamma-adaptin ear (GAE) domain / Gamma-adaptin ear (GAE) domain profile. / HIV-1 Nef protein, anchor domain superfamily / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / HIV negative factor Nef / AP-1/2/4 complex subunit beta / Adaptor protein complex, sigma subunit / HIV-1 Nef protein, core domain superfamily / Negative factor, (F-Protein) or Nef / : / Beta-adaptin appendage, C-terminal subdomain / Beta2-adaptin appendage, C-terminal sub-domain / ADP-ribosylation factor 1-5 / AP complex subunit beta / Clathrin adaptor complex, small chain / Clathrin adaptor complexes small chain signature. / Clathrin adaptor complexes medium chain signature 1. / Clathrin adaptor, mu subunit / Clathrin adaptor, mu subunit, conserved site / Clathrin adaptor complexes medium chain signature 2. / : / Coatomer/calthrin adaptor appendage, C-terminal subdomain / Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain / Adaptin C-terminal domain / Adaptin C-terminal domain / AP complex, mu/sigma subunit / Clathrin adaptor complex small chain / Adaptor complexes medium subunit family / AP-2 complex subunit mu, C-terminal superfamily / Clathrin/coatomer adaptor, adaptin-like, N-terminal / Adaptin N terminal region / Mu homology domain / Mu homology domain (MHD) profile. / Clathrin adaptor, appendage, Ig-like subdomain superfamily / Small GTPase superfamily, ARF type / small GTPase Arf family profile. / Sar1p-like members of the Ras-family of small GTPases / Small GTPase superfamily, ARF/SAR type / ADP-ribosylation factor family / Longin-like domain superfamily / ARF-like small GTPases; ARF, ADP-ribosylation factor / TBP domain superfamily / Armadillo/beta-catenin-like repeats / Armadillo / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / Rab subfamily of small GTPases / MHC classes I/II-like antigen recognition protein / Armadillo-like helical / Small GTP-binding protein domain / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Armadillo-type fold / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / ADP-ribosylation factor / HLA class I histocompatibility antigen, A alpha chain / AP-1 complex subunit gamma-1 / AP-1 complex subunit mu-1 / AP-1 complex subunit beta-1 / Protein Nef / AP-1 complex subunit sigma-3
Similarity search - Component
Biological speciesHomo sapiens (human)
Human immunodeficiency virus 1
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 9.4 Å
AuthorsHooy, R.M. / Hurley, J.H.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)F32 AI152971 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI120691 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)P50 AI150476 United States
CitationJournal: Sci Adv / Year: 2022
Title: Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat.
Authors: Richard M Hooy / Yuichiro Iwamoto / Dan A Tudorica / Xuefeng Ren / James H Hurley /
Abstract: The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to ...The adaptor protein (AP) complexes not only form the inner layer of clathrin coats but also have clathrin-independent roles in membrane traffic whose mechanisms are unknown. HIV-1 Nef hijacks AP-1 to sequester major histocompatibility complex class I (MHC-I), evading immune detection. We found that AP-1:Arf1:Nef:MHC-I forms a coat on tubulated membranes without clathrin and determined its structure. The coat assembles via Arf1 dimer interfaces. AP-1-positive tubules are enriched in cells upon clathrin knockdown. Nef localizes preferentially to AP-1 tubules in cells, explaining how Nef sequesters MHC-I. Coat contact residues are conserved across Arf isoforms and the Arf-dependent AP complexes AP-1, AP-3, and AP-4. Thus, AP complexes can self-assemble with Arf1 into tubular coats without clathrin or other scaffolding factors. The AP-1:Arf1 coat defines the structural basis of a broader class of tubulovesicular membrane coats as an intermediate in clathrin vesicle formation from internal membranes and as an MHC-I sequestration mechanism in HIV-1 infection.
History
DepositionJun 11, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 9, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 12, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: ADP ribosylation factor 1
H: ADP ribosylation factor 1
N: Protein Nef
Y: HLA class I histocompatibility antigen, A alpha chain
B: AP-1 complex subunit beta-1
G: AP-1 complex subunit gamma-1
L: Protein Nef
M: AP-1 complex subunit mu-1
S: AP-1 complex subunit sigma-3
D: ADP ribosylation factor 1
F: ADP ribosylation factor 1
K: Protein Nef
P: HLA class I histocompatibility antigen, A alpha chain
A: AP-1 complex subunit beta-1
E: AP-1 complex subunit gamma-1
I: Protein Nef
J: AP-1 complex subunit mu-1
O: AP-1 complex subunit sigma-3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)671,02126
Polymers668,83118
Non-polymers2,1908
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1chain "B"
d_2ens_1chain "A"
d_1ens_2chain "F"
d_2ens_2chain "D"
d_3ens_2chain "C"
d_4ens_2chain "H"
d_1ens_3chain "G"
d_2ens_3chain "E"
d_1ens_4chain "L"
d_2ens_4chain "I"
d_1ens_5chain "M"
d_2ens_5chain "J"
d_1ens_6chain "N"
d_2ens_6chain "K"
d_1ens_7chain "O"
d_2ens_7chain "S"
d_1ens_8chain "Y"
d_2ens_8chain "P"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg label comp-IDEnd label comp-IDLabel asym-IDLabel seq-ID
d_11ens_1GLUGLUI1 - 570
d_21ens_1GLUGLUV1 - 570
d_11ens_2GLYLYSQ1 - 180
d_12ens_2GTPGTPR
d_21ens_2GLYLYSN1 - 180
d_22ens_2GTPGTPO
d_31ens_2GLYLYSA1 - 180
d_32ens_2GTPGTPB
d_41ens_2GLYLYSD1 - 180
d_42ens_2GTPGTPE
d_11ens_3PROGLUJ1 - 585
d_21ens_3PROGLUW1 - 585
d_11ens_4LYSPROK1 - 10
d_21ens_4LYSPROX1 - 10
d_11ens_5SERGLNL1 - 415
d_21ens_5SERGLNY1 - 415
d_11ens_6SERLYSG1 - 137
d_21ens_6SERLYST1 - 137
d_11ens_7METGLNZ1 - 142
d_21ens_7METGLNM1 - 142
d_11ens_8ASPGLYH1 - 18
d_21ens_8ASPGLYU1 - 18

NCS ensembles :
ID
ens_1
ens_2
ens_3
ens_4
ens_5
ens_6
ens_7
ens_8

NCS oper:
IDCodeMatrixVector
1given(-0.999999629142, 0.000861211760579, -5.53001807752E-6), (-0.000861210605514, -0.999999608026, -0.000205583336096), (-5.70706669672E-6, -0.000205578497344, 0.999999978852)235.100913953, 235.288344955, 0.0205865086117
2given(-0.993739314804, 0.108141707501, 0.0280632377316), (-0.0996686239617, -0.971586985235, 0.214673928363), (0.0504810817128, 0.210532898189, 0.97628252016)330.349423617, 265.546994334, -35.7644513124
3given(0.993824537847, -0.107305342448, -0.0282551137934), (0.098801284665, 0.971636433358, -0.214850989107), (0.0505083569518, 0.210732543414, 0.976238035022)-95.2742761217, -30.1690505505, -35.7919389805
4given(-0.999999628412, -0.000862059015746, -5.51816587449E-6), (0.000862060137116, -0.999999607096, -0.000206544378008), (-5.34011026317E-6, -0.00020654905825, 0.999999978654)235.303498507, 235.085746163, 0.0291099457927
5given(-0.999999629072, 0.000861296865025, -4.88622813456E-6), (-0.000861295844792, -0.999999608053, -0.000205092539925), (-5.06287178109E-6, -0.000205088255363, 0.999999978957)235.100817348, 235.288292716, 0.0204939653975
6given(-0.999999646369, 0.000840216134835, 3.60261524949E-5), (-0.000840222789217, -0.999999629883, -0.000185094198866), (3.58706200287E-5, -0.000185124403405, 0.999999982221)235.098683513, 235.285022754, 0.0162285167741
7given(-0.999999628644, 0.000861793951073, -4.71165955588E-6), (-0.000861792966478, -0.999999607618, -0.000205124079663), (-4.88843239818E-6, -0.000205119943014, 0.999999978951)235.100746566, 235.288319915, 0.0204859207736
8given(-0.999999629277, 0.000861056683809, -5.31496163844E-6), (-0.000861055577081, -0.999999608313, -0.000204832560078), (-5.49133200156E-6, -0.000204827907664, 0.999999979008)235.100871093, 235.288264625, 0.0204977875798
9given(-0.999999629454, -0.000860862543179, -2.62739708819E-6), (0.000860863064468, -0.999999608381, -0.000205309425745), (-2.45065286487E-6, -0.000205311611497, 0.999999978921)235.303024306, 235.085824452, 0.028512624191
10given(-0.999999625322, 0.00086563658434, 5.31170080156E-6), (-0.0008656376634, -0.999999603989, -0.00020662437719), (5.13283707795E-6, -0.000206628897781, 0.999999978639)235.099610535, 235.288783825, 0.0196531687537

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Components

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Protein , 2 types, 8 molecules CHDFNLKI

#1: Protein
ADP ribosylation factor 1


Mass: 20721.742 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: N-terminal myristoylation at Gly-2 / Source: (gene. exp.) Homo sapiens (human) / Gene: ARF1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A8C2UGL4
#2: Protein
Protein Nef / 3'ORF / Negative factor / F-protein


Mass: 24285.244 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: N-terminal myristoylation at Gly-2 / Source: (gene. exp.) Human immunodeficiency virus 1 / Gene: nef / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q90VU7

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Protein/peptide , 1 types, 2 molecules YP

#3: Protein/peptide HLA class I histocompatibility antigen, A alpha chain / Human leukocyte antigen A / HLA-A


Mass: 4558.884 Da / Num. of mol.: 2 / Fragment: MHC-I cytosolic tail (HLA-A/B) / Mutation: T345S, S349G, G355S, C363S
Source method: isolated from a genetically manipulated source
Details: conjugated to MPB-PE lipid / Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P04439

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AP-1 complex subunit ... , 4 types, 8 molecules BAGEMJSO

#4: Protein AP-1 complex subunit beta-1 / Adaptor protein complex AP-1 subunit beta-1 / Adaptor-related protein complex 1 subunit beta-1 / ...Adaptor protein complex AP-1 subunit beta-1 / Adaptor-related protein complex 1 subunit beta-1 / Beta-1-adaptin / Beta-adaptin 1 / Clathrin assembly protein complex 1 beta large chain / Golgi adaptor HA1/AP1 adaptin beta subunit


Mass: 104736.461 Da / Num. of mol.: 2 / Mutation: K359R,E476K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AP1B1, ADTB1, BAM22, CLAPB2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q10567
#5: Protein AP-1 complex subunit gamma-1 / Adaptor protein complex AP-1 subunit gamma-1 / Adaptor-related protein complex 1 subunit gamma-1 / ...Adaptor protein complex AP-1 subunit gamma-1 / Adaptor-related protein complex 1 subunit gamma-1 / Clathrin assembly protein complex 1 gamma-1 large chain / Gamma-adaptin / Gamma1-adaptin / Golgi adaptor HA1/AP1 adaptin subunit gamma-1


Mass: 68194.094 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ap1g1, Adtg, Clapg1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P22892
#6: Protein AP-1 complex subunit mu-1 / AP-mu chain family member mu1A / Adaptor protein complex AP-1 subunit mu-1 / Adaptor-related ...AP-mu chain family member mu1A / Adaptor protein complex AP-1 subunit mu-1 / Adaptor-related protein complex 1 subunit mu-1 / Clathrin assembly protein complex 1 mu-1 medium chain 1 / Clathrin coat assembly protein AP47 / Clathrin coat-associated protein AP47 / Golgi adaptor HA1/AP1 adaptin mu-1 subunit / Mu-adaptin 1 / Mu1A-adaptin


Mass: 48606.730 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ap1m1, Cltnm / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P35585
#7: Protein AP-1 complex subunit sigma-3 / Adaptor protein complex AP-1 subunit sigma-1C / Adaptor-related protein complex 1 subunit sigma-1C ...Adaptor protein complex AP-1 subunit sigma-1C / Adaptor-related protein complex 1 subunit sigma-1C / Clathrin assembly protein complex 1 sigma-1C small chain / Golgi adaptor HA1/AP1 adaptin sigma-1C subunit / Sigma 1C subunit of AP-1 clathrin / Sigma-adaptin 1C / Sigma1C-adaptin


Mass: 18305.273 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AP1S3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q96PC3

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Non-polymers , 2 types, 8 molecules

#8: Chemical
ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: GTP, energy-carrying molecule*YM
#9: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: subtomogram averaging

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Sample preparation

ComponentName: AP-1, Arf1, Nef lattice on MHC-I lipopeptide incorporated narrow membrane tubes
Type: COMPLEX / Entity ID: #1-#7 / Source: MULTIPLE SOURCES
Molecular weightExperimental value: NO
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
31Human immunodeficiency virus 111676
41Mus musculus (house mouse)10090
Source (recombinant)Organism: Escherichia coli BL21(DE3) (bacteria)
Buffer solutionpH: 7.2
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 4500 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 3 e/Å2 / Avg electron dose per subtomogram: 123 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

Software
NameVersionClassificationNB
phenix.real_space_refine1.20_4459refinement
PHENIX1.20_4459refinement
EM software
IDNameCategory
7UCSF Chimeramodel fitting
13PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING ONLY
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 9.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8615 / Symmetry type: POINT
EM volume selectionNum. of tomograms: 38 / Num. of volumes extracted: 37976
Atomic model buildingProtocol: RIGID BODY FIT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 32.79 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.000618008
ELECTRON MICROSCOPYf_angle_d0.221322514
ELECTRON MICROSCOPYf_chiral_restr0.08516
ELECTRON MICROSCOPYf_plane_restr0.00084454
ELECTRON MICROSCOPYf_dihedral_angle_d5.88474506
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AELECTRON MICROSCOPYNCS constraints2.49507074873E-13
ens_2d_2DELECTRON MICROSCOPYNCS constraints2.02554958242E-13
ens_2d_3CELECTRON MICROSCOPYNCS constraints9.0321263665E-14
ens_2d_4HELECTRON MICROSCOPYNCS constraints8.7265714295E-14
ens_3d_2EELECTRON MICROSCOPYNCS constraints1.93079964173E-10
ens_4d_2IELECTRON MICROSCOPYNCS constraints4.27726956386E-12
ens_5d_2JELECTRON MICROSCOPYNCS constraints1.35559005344E-11
ens_6d_2KELECTRON MICROSCOPYNCS constraints1.99712140995E-11
ens_7d_2SELECTRON MICROSCOPYNCS constraints1.05030864284E-12
ens_8d_2PELECTRON MICROSCOPYNCS constraints1.31174587262E-11

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