[English] 日本語
Yorodumi
- EMDB-16821: Cryo-EM structure of a pre-dimerized murine IL-12 complete extrac... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-16821
TitleCryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 2).
Map dataMain map: Anisotropy sharpened map of the murine IL12:IL12Rbeta1-DAPK1:IL12Rbeta2-Calmodulin complex (Class 2), 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
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 / negative regulation of vascular endothelial growth factor signaling pathway ...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 / negative regulation of vascular endothelial growth factor signaling pathway / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / cellular response to hydroperoxide / positive regulation of smooth muscle cell apoptotic process / regulation of response to tumor cell / positive regulation of autophagic cell death / DAPK1-calmodulin complex / positive regulation of T-helper 1 type immune response / interleukin-12 receptor binding / T-helper cell differentiation / interleukin-23 receptor complex / Caspase activation via Dependence Receptors in the absence of ligand / interleukin-12-mediated signaling pathway / defense response to tumor cell / positive regulation of NK T cell proliferation / positive regulation of osteoclast differentiation / regulation of NMDA receptor activity / negative regulation of interleukin-17 production / calcium/calmodulin-dependent protein kinase activity / cytokine receptor activity / natural killer cell activation / response to UV-B / positive regulation of granulocyte macrophage colony-stimulating factor production / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / syntaxin-1 binding / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / positive regulation of T cell differentiation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / CaMK IV-mediated phosphorylation of CREB / PKA activation / negative regulation of high voltage-gated calcium channel activity / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / negative regulation of ryanodine-sensitive calcium-release channel activity / organelle localization by membrane tethering / negative regulation of interleukin-10 production / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / defense response to protozoan / presynaptic endocytosis / Synthesis of IP3 and IP4 in the cytosol / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / calcineurin-mediated signaling / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of interleukin-17 production / RHO GTPases activate PAKs / positive regulation of natural killer cell proliferation / positive regulation of activated T cell proliferation / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / regulation of ryanodine-sensitive calcium-release channel activity / positive regulation of interleukin-10 production / Long-term potentiation / protein phosphatase activator activity / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / extrinsic apoptotic signaling pathway via death domain receptors / DARPP-32 events / catalytic complex / Smooth Muscle Contraction / detection of calcium ion / negative regulation of protein secretion / regulation of cardiac muscle contraction / cell surface receptor signaling pathway via JAK-STAT / RHO GTPases activate IQGAPs / T cell proliferation / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / cellular response to interferon-beta / Protein methylation / calcium channel inhibitor activity / coreceptor activity / presynaptic cytosol / Activation of AMPK downstream of NMDARs / Ion homeostasis / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / eNOS activation / titin binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / sperm midpiece
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. ...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 / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / EF-hand domain pair / Fibronectin type-III domain profile. / Ankyrin repeats (3 copies) / Fibronectin type III / Fibronectin type III superfamily / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / 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 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Ig-like domain profile. / Immunoglobulin-like domain / 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: 4.6 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: Bloch Y / Felix J / Merceron R / Provost M / Symakani RA / De Backer R / Lambert E / Mehdipour AR / Savvides SN
History
DepositionMar 10, 2023-
Header (metadata) releaseFeb 7, 2024-
Map releaseFeb 7, 2024-
UpdateNov 20, 2024-
Current statusNov 20, 2024Processing site: PDBe / Status: Released

-
Structure visualization

Downloads & links

-
Map

FileDownload / File: emd_16821.map.gz / Format: CCP4 / Size: 40.6 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 2), used for model refinement in Phenix. Additional map: DeepEMhancer sharpened map.
Voxel sizeX=Y=Z: 1.51 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.36380848 - 0.6111633
Average (Standard dev.)0.0003129092 (±0.013889578)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions220220220
Spacing220220220
CellA=B=C: 332.2 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

-
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

-
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

-
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

-
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

-
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

-
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

-
Macromolecule #7: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 7 / Number of copies: 3 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

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

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
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..

-
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

+
Image processing

Particle selectionNumber selected: 2151468
Startup modelType of model: NONE
Final reconstructionNumber classes used: 2 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 209938
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationNumber classes: 2 / Software - Name: cryoSPARC

-
Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT
Output model

PDB-8oe0:
Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 2).

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more