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- EMDB-16820: Cryo-EM structure of a pre-dimerized murine IL-12 complete extrac... -

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Entry
Database: EMDB / ID: EMD-16820
TitleCryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 1).
Map dataMain map: Anisotropy sharpened map of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex (Class 1), used for model refinement in Phenix. Additional map: DeepEMhancer sharpened map.
Sample
  • Complex: Murine IL-12 in complex with mIL-12Rbeta1-DAPK1 and mIL-12Rbeta2-Calmodulin.
    • Protein or peptide: Interleukin-12 subunit alpha
    • Protein or peptide: Interleukin-12 subunit beta
    • Protein or peptide: Interleukin-12 receptor subunit beta-1,Death-associated protein kinase 1
    • Protein or peptide: Interleukin-12 receptor subunit beta-2,Calmodulin-1
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: water
KeywordsComplex / Cytokine / Receptor / SIGNALING PROTEIN
Function / homology
Function and homology information


interleukin-12 beta subunit binding / Interleukin-12 signaling / Interleukin-23 signaling / interleukin-23 receptor binding / Interleukin-35 Signalling / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / T-helper 1 cell activation / natural killer cell activation involved in immune response ...interleukin-12 beta subunit binding / Interleukin-12 signaling / Interleukin-23 signaling / interleukin-23 receptor binding / Interleukin-35 Signalling / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / T-helper 1 cell activation / natural killer cell activation involved in immune response / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of vascular endothelial growth factor signaling pathway / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / cellular response to hydroperoxide / positive regulation of T-helper 1 type immune response / regulation of response to tumor cell / positive regulation of autophagic cell death / DAPK1-calmodulin complex / positive regulation of smooth muscle cell apoptotic process / interleukin-12 receptor binding / T-helper cell differentiation / interleukin-23 receptor complex / defense response to tumor cell / natural killer cell activation / Caspase activation via Dependence Receptors in the absence of ligand / interleukin-12-mediated signaling pathway / negative regulation of interleukin-17 production / positive regulation of NK T cell proliferation / positive regulation of osteoclast differentiation / calcium/calmodulin-dependent protein kinase activity / regulation of NMDA receptor activity / response to UV-B / positive regulation of natural killer cell proliferation / positive regulation of granulocyte macrophage colony-stimulating factor production / CaM pathway / Cam-PDE 1 activation / cytokine receptor activity / syntaxin-1 binding / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / positive regulation of T cell differentiation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / positive regulation of cyclic-nucleotide phosphodiesterase activity / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / autophagosome membrane docking / mitochondrion-endoplasmic reticulum membrane tethering / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / regulation of cardiac muscle cell action potential / negative regulation of interleukin-10 production / positive regulation of ryanodine-sensitive calcium-release channel activity / regulation of cell communication by electrical coupling involved in cardiac conduction / defense response to protozoan / Synthesis of IP3 and IP4 in the cytosol / negative regulation of peptidyl-threonine phosphorylation / : / Negative regulation of NMDA receptor-mediated neuronal transmission / Phase 0 - rapid depolarisation / positive regulation of activated T cell proliferation / Unblocking of NMDA receptors, glutamate binding and activation / negative regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / positive regulation of interleukin-17 production / RHO GTPases activate PAKs / cytokine binding / Ion transport by P-type ATPases / : / Uptake and function of anthrax toxins / positive regulation of interleukin-10 production / Long-term potentiation / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / catalytic complex / DARPP-32 events / detection of calcium ion / regulation of cardiac muscle contraction / extrinsic apoptotic signaling pathway via death domain receptors / Smooth Muscle Contraction / negative regulation of protein secretion / regulation of ryanodine-sensitive calcium-release channel activity / immunoglobulin mediated immune response / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / calcium channel inhibitor activity / cellular response to interferon-beta / eNOS activation / Protein methylation / positive regulation of autophagy / coreceptor activity / voltage-gated potassium channel complex / Activation of AMPK downstream of NMDARs
Similarity search - Function
Interleukin-12 alpha / Interleukin-12 alpha subunit / Interleukin-12 beta / Interleukin-12 beta, central domain / : / Cytokine interleukin-12p40 C-terminus / Death-associated protein kinase 1 / Long hematopoietin receptor, soluble alpha chain, conserved site / Long hematopoietin receptor, soluble alpha chains family signature. / Immunoglobulin C2-set-like, ligand-binding ...Interleukin-12 alpha / Interleukin-12 alpha subunit / Interleukin-12 beta / Interleukin-12 beta, central domain / : / Cytokine interleukin-12p40 C-terminus / Death-associated protein kinase 1 / Long hematopoietin receptor, soluble alpha chain, conserved site / Long hematopoietin receptor, soluble alpha chains family signature. / Immunoglobulin C2-set-like, ligand-binding / Ig-like C2-type domain / Long hematopoietin receptor, Gp130 family 2, conserved site / Long hematopoietin receptor, gp130 family signature. / : / Roc domain profile. / Roc domain / Ankyrin repeats (many copies) / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / Four-helical cytokine-like, core / : / Death-like domain superfamily / Ankyrin repeat / Fibronectin type III domain / Fibronectin type 3 domain / EF-hand domain pair / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Fibronectin type III / Fibronectin type III superfamily / Ankyrin repeat / EF-hand, calcium binding motif / Ankyrin repeat-containing domain superfamily / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Ig-like domain profile. / Immunoglobulin-like domain / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Immunoglobulin-like domain superfamily / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Calmodulin-1 / Interleukin-12 subunit alpha / Interleukin-12 subunit beta / Death-associated protein kinase 1 / Interleukin-12 receptor subunit beta-2 / Interleukin-12 receptor subunit beta-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsFelix J / Bloch Y / Savvides SN
Funding support Belgium, 2 items
OrganizationGrant numberCountry
Research Foundation - Flanders (FWO)12S0519N Belgium
Research Foundation - Flanders (FWO)G0B4918N Belgium
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Structures of complete extracellular receptor assemblies mediated by IL-12 and IL-23.
Authors: Yehudi Bloch / Jan Felix / Romain Merceron / Mathias Provost / Royan Alipour Symakani / Robin De Backer / Elisabeth Lambert / Ahmad R Mehdipour / Savvas N Savvides /
Abstract: Cell-surface receptor complexes mediated by pro-inflammatory interleukin (IL)-12 and IL-23, both validated therapeutic targets, are incompletely understood due to the lack of structural insights into ...Cell-surface receptor complexes mediated by pro-inflammatory interleukin (IL)-12 and IL-23, both validated therapeutic targets, are incompletely understood due to the lack of structural insights into their complete extracellular assemblies. Furthermore, there is a paucity of structural details describing the IL-12-receptor interaction interfaces, in contrast to IL-23-receptor complexes. Here we report structures of fully assembled mouse IL-12/human IL-23-receptor complexes comprising the complete extracellular segments of the cognate receptors determined by electron cryo-microscopy. The structures reveal key commonalities but also surprisingly diverse features. Most notably, whereas IL-12 and IL-23 both utilize a conspicuously presented aromatic residue on their α-subunit as a hotspot to interact with the N-terminal Ig domain of their high-affinity receptors, only IL-12 juxtaposes receptor domains proximal to the cell membrane. Collectively, our findings will help to complete our understanding of cytokine-mediated assemblies of tall cytokine receptors and will enable a cytokine-specific interrogation of IL-12/IL-23 signaling in physiology and disease.
History
DepositionMar 10, 2023-
Header (metadata) releaseFeb 7, 2024-
Map releaseFeb 7, 2024-
UpdateNov 13, 2024-
Current statusNov 13, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_16820.png

Downloads & links

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Map

FileDownload / File: emd_16820.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMain map: Anisotropy sharpened map of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex (Class 1), used for model refinement in Phenix. Additional map: DeepEMhancer sharpened map.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
0.76 Å/pix.
x 440 pix.
= 332.2 Å		0.76 Å/pix.
x 440 pix.
= 332.2 Å		0.76 Å/pix.
x 440 pix.
= 332.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.755 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.06
Minimum - Maximum-0.35257882 - 0.47756088
Average (Standard dev.)0.000069268 (±0.0072278683)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 332.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_16820_msk_1.map
Projections & Slices
AxesZYX

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Histogram

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Additional map: DeepEMhancer sharpened map of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex...

Fileemd_16820_additional_1.map
AnnotationDeepEMhancer sharpened map of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex (Class 1), used for model building in Coot and visualization in ChimeraX.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 1 of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex...

Fileemd_16820_half_map_1.map
AnnotationHalf map 1 of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex (Class 1).
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2 of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex...

Fileemd_16820_half_map_2.map
AnnotationHalf map 2 of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex (Class 1).
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Murine IL-12 in complex with mIL-12Rbeta1-DAPK1 and mIL-12Rbeta2-...

EntireName: Murine IL-12 in complex with mIL-12Rbeta1-DAPK1 and mIL-12Rbeta2-Calmodulin.
Components
  • Complex: Murine IL-12 in complex with mIL-12Rbeta1-DAPK1 and mIL-12Rbeta2-Calmodulin.
    • Protein or peptide: Interleukin-12 subunit alpha
    • Protein or peptide: Interleukin-12 subunit beta
    • Protein or peptide: Interleukin-12 receptor subunit beta-1,Death-associated protein kinase 1
    • Protein or peptide: Interleukin-12 receptor subunit beta-2,Calmodulin-1
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: water

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Supramolecule #1: Murine IL-12 in complex with mIL-12Rbeta1-DAPK1 and mIL-12Rbeta2-...

SupramoleculeName: Murine IL-12 in complex with mIL-12Rbeta1-DAPK1 and mIL-12Rbeta2-Calmodulin.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 216 KDa

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Macromolecule #1: Interleukin-12 subunit alpha

MacromoleculeName: Interleukin-12 subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 25.927496 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQK TSLMMTLCLG SIYEDLKMYQ TEFQAINAAL QNHNHQQIIL DKGMLVAIDE LMQSLNHNGE TLRQKPPVGE A DPYRVKMK ...String:
RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQK TSLMMTLCLG SIYEDLKMYQ TEFQAINAAL QNHNHQQIIL DKGMLVAIDE LMQSLNHNGE TLRQKPPVGE A DPYRVKMK LCILLHAFST RVVTINRVMG YLSSAGTSDE VDGGSGGSGL NDIFEAQKIE WHEGRTKHHH HHH

UniProtKB: Interleukin-12 subunit alpha

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Macromolecule #2: Interleukin-12 subunit beta

MacromoleculeName: Interleukin-12 subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 35.83732 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGI WSTEILKNFK NKTFLKCEAP NYSGRFTCSW LVQRNMDLKF NIKSSSSSPD SRAVTCGMAS LSAEKVTLDQ R DYEKYSVS ...String:
MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGI WSTEILKNFK NKTFLKCEAP NYSGRFTCSW LVQRNMDLKF NIKSSSSSPD SRAVTCGMAS LSAEKVTLDQ R DYEKYSVS CQEDVTCPTA EETLPIELAL EARQQNKYEN YSTSFFIRDI IKPDPPKNLQ MKPLKNSQVE VSWEYPDSWS TP HSYFSLK FFVRIQRKKE KMKETEEGCN QKGAFLVEKT STEVQCKGGN VCVQAQDRYY NSSCSKWACV PCRVRS

UniProtKB: Interleukin-12 subunit beta

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Macromolecule #3: Interleukin-12 receptor subunit beta-1,Death-associated protein k...

MacromoleculeName: Interleukin-12 receptor subunit beta-1,Death-associated protein kinase 1
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: non-specific serine/threonine protein kinase
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 63.789156 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QLGASGPGDG CCVEKTSFPE GASGSPLGPR NLSCYRVSKT DYECSWQYDG PEDNVSHVLW CCFVPPNHTH TGQERCRYFS SGPDRTVQF WEQDGIPVLS KVNFWVESRL GNRTMKSQKI SQYLYNWTKT TPPLGHIKVS QSHRQLRMDW NVSEEAGAEV Q FRRRMPTT ...String:
QLGASGPGDG CCVEKTSFPE GASGSPLGPR NLSCYRVSKT DYECSWQYDG PEDNVSHVLW CCFVPPNHTH TGQERCRYFS SGPDRTVQF WEQDGIPVLS KVNFWVESRL GNRTMKSQKI SQYLYNWTKT TPPLGHIKVS QSHRQLRMDW NVSEEAGAEV Q FRRRMPTT NWTLGDCGPQ VNSGSGVLGD IRGSMSESCL CPSENMAQEI QIRRRRRLSS GAPGGPWSDW SMPVCVPPEV LP QAKIKFL VEPLNQGGRR RLTMQGQSPQ LAVPEGCRGR PGAQVKKHLV LVRMLSCRCQ AQTSKTVPLG KKLNLSGATY DLN VLAKTR FGRSTIQKWH LPAQELTETR ALNVSVGGNM TSMQWAAQAP GTTYCLEWQP WFQHRNHTHC TLIVPEEEDP AKMV THSWS SKPTLEQEEC YRITVFASKN PKNPMLWATV LSSYYFGGNA SRAGTPRHVS VRNQTGDSVS VEWTASQLST CPGVL TQYV VRCEAEDGAW ESEWLVPPTK TQVTLDGLRS RVMYKVQVRA DTARLPGAWS HPQRFSFEGT GGSGGSGGAA RKKWKQ SVR LISLCQRLS

UniProtKB: Interleukin-12 receptor subunit beta-1, Death-associated protein kinase 1

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Macromolecule #4: Interleukin-12 receptor subunit beta-2,Calmodulin-1

MacromoleculeName: Interleukin-12 receptor subunit beta-2,Calmodulin-1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 85.723344 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: NIDVCKLGTV TVQPAPVIPL GSAANISCSL NPKQGCSHYP SSNELILLKF VNDVLVENLH GKKVHDHTGH SSTFQVTNLS LGMTLFVCK LNCSNSQKKP PVPVCGVEIS VGVAPEPPQN ISCVQEGENG TVACSWNSGK VTYLKTNYTL QLSGPNNLTC Q KQCFSDNR ...String:
NIDVCKLGTV TVQPAPVIPL GSAANISCSL NPKQGCSHYP SSNELILLKF VNDVLVENLH GKKVHDHTGH SSTFQVTNLS LGMTLFVCK LNCSNSQKKP PVPVCGVEIS VGVAPEPPQN ISCVQEGENG TVACSWNSGK VTYLKTNYTL QLSGPNNLTC Q KQCFSDNR QNCNRLDLGI NLSPDLAESR FIVRVTAIND LGNSSSLPHT FTFLDIVIPL PPWDIRINFL NASGSRGTLQ WE DEGQVVL NQLRYQPLNS TSWNMVNATN AKGKYDLRDL RPFTEYEFQI SSKLHLSGGS WSNWSESLRT RTPEEEPVGI LDI WYMKQD IDYDRQQISL FWKSLNPSEA RGKILHYQVT LQEVTKKTTL QNTTRHTSWT RVIPRTGAWT ASVSAANSKG ASAP THINI VDLCGTGLLA PHQVSAKSEN MDNILVTWQP PKKADSAVRE YIVEWRALQP GSITKFPPHW LRIPPDNMSA LISEN IKPY ICYEIRVHAL SESQGGCSSI RGDSKHKAPV SGPHITAITE KKERLFISWT HIPFPEQRGC ILHYRIYWKE RDSTAQ PEL CEIQYRRSQN SHPISSLQPR VTYVLWMTAV TAAGESPQGN EREFCPQGKA NGTGGSGGSG GLTEEQIAEF KEAFSLF DK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGY I SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

UniProtKB: Interleukin-12 receptor subunit beta-2, Calmodulin-1

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Macromolecule #6: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 6 / Number of copies: 5 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

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

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Macromolecule #7: water

MacromoleculeName: water / type: ligand / ID: 7 / Number of copies: 1 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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: 7.4
Component:
ConcentrationFormulaName
150.0 mMNaClsodium chloride
25.0 mMC8H18N2O4SHEPES
5.0 mMCaClcalcium chloride

Details: HEPES-buffered saline (HBS) with added calcium chloride: 25 mM HEPES, pH 7.4, 150 mM NaCl, 5 mM CaCl
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Instrument: LEICA PLUNGER / Details: Leica EM GP2, 5 s. blotting time..

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Electron microscopy

MicroscopeJEOL CRYO ARM 300
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number real images: 8145 / Average exposure time: 3.37 sec. / Average electron dose: 61.8 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 60000
Sample stageCooling holder cryogen: NITROGEN

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Image processing

Particle selectionNumber selected: 2151468
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 268498
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationNumber classes: 2 / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT
Output model

PDB-8odz:
Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 1).

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