[English] 日本語
Yorodumi
- PDB-6m93: Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-193... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6m93
TitleMonophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-1933 ternary complex
Components
  • Catenin beta-1
  • F-box/WD repeat-containing protein 1A
  • S-phase kinase-associated protein 1
KeywordsLIGASE / Ubiquitin Molecular Glue Enhancer
Function / homology
Function and homology information


positive regulation of heparan sulfate proteoglycan biosynthetic process / cranial ganglion development / CDH11 homotypic and heterotypic interactions / embryonic skeletal limb joint morphogenesis / Regulation of CDH19 Expression and Function / astrocyte-dopaminergic neuron signaling / beta-catenin-TCF7L2 complex / regulation of nephron tubule epithelial cell differentiation / protein phosphorylated amino acid binding / regulation of timing of anagen ...positive regulation of heparan sulfate proteoglycan biosynthetic process / cranial ganglion development / CDH11 homotypic and heterotypic interactions / embryonic skeletal limb joint morphogenesis / Regulation of CDH19 Expression and Function / astrocyte-dopaminergic neuron signaling / beta-catenin-TCF7L2 complex / regulation of nephron tubule epithelial cell differentiation / protein phosphorylated amino acid binding / regulation of timing of anagen / negative regulation of mitotic cell cycle, embryonic / Binding of TCF/LEF:CTNNB1 to target gene promoters / regulation of centriole-centriole cohesion / RUNX3 regulates WNT signaling / regulation of centromeric sister chromatid cohesion / Regulation of CDH11 function / regulation of fibroblast proliferation / Scrib-APC-beta-catenin complex / beta-catenin-TCF complex / Specification of the neural plate border / positive regulation of skeletal muscle tissue development / synaptic vesicle clustering / Formation of the nephric duct / dorsal root ganglion development / endothelial tube morphogenesis / hindbrain development / mesenchymal to epithelial transition / cranial skeletal system development / sympathetic ganglion development / presynaptic active zone cytoplasmic component / regulation of protein localization to cell surface / fascia adherens / mesenchymal stem cell differentiation / detection of muscle stretch / synaptic assembly at neuromuscular junction / positive regulation of odontoblast differentiation / F-box domain binding / alpha-catenin binding / cellular response to indole-3-methanol / regulation of epithelial to mesenchymal transition / regulation of calcium ion import / histone methyltransferase binding / hair cell differentiation / apicolateral plasma membrane / Germ layer formation at gastrulation / positive regulation of homotypic cell-cell adhesion / neuron projection extension / cell-cell adhesion mediated by cadherin / flotillin complex / positive regulation of circadian rhythm / Formation of definitive endoderm / PcG protein complex / regulation of smooth muscle cell proliferation / beta-catenin destruction complex / Formation of axial mesoderm / embryonic brain development / negative regulation of protein sumoylation / Apoptotic cleavage of cell adhesion proteins / midbrain dopaminergic neuron differentiation / catenin complex / LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production / regulation of xenophagy / maintenance of protein location in nucleus / positive regulation of blood vessel branching / protein localization to cell surface / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / Cul7-RING ubiquitin ligase complex / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / I-SMAD binding / Regulation of CDH1 Function / regulation of cell cycle process / neural crest cell differentiation / Wnt signalosome / Adherens junctions interactions / adherens junction assembly / positive regulation of neuroblast proliferation / Cardiogenesis / Disassembly of the destruction complex and recruitment of AXIN to the membrane / regulation of BMP signaling pathway / ubiquitin ligase activator activity / regulation of canonical Wnt signaling pathway / regulation of mitophagy / protein dephosphorylation / regulation of centrosome duplication / stem cell population maintenance / non-canonical NF-kappaB signal transduction / Myogenesis / regulation of TOR signaling / Regulation of CDH1 posttranslational processing and trafficking to plasma membrane / hypothalamus development / SCF ubiquitin ligase complex / Formation of paraxial mesoderm / regulation of DNA damage checkpoint / regulation of synapse assembly
Similarity search - Function
D domain of beta-TrCP / D domain of beta-TrCP / D domain of beta-TrCP / : / Monooxygenase - #50 / Beta-catenin / A Receptor for Ubiquitination Targets / F-box domain profile. / F-box-like / F-box-like domain superfamily ...D domain of beta-TrCP / D domain of beta-TrCP / D domain of beta-TrCP / : / Monooxygenase - #50 / Beta-catenin / A Receptor for Ubiquitination Targets / F-box domain profile. / F-box-like / F-box-like domain superfamily / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain / F-box domain / Monooxygenase / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / Armadillo/plakoglobin ARM repeat profile. / Armadillo/beta-catenin-like repeat / Armadillo/beta-catenin-like repeats / Armadillo / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / YVTN repeat-like/Quinoprotein amine dehydrogenase / SKP1/BTB/POZ domain superfamily / 7 Propeller / Methylamine Dehydrogenase; Chain H / Armadillo-like helical / WD domain, G-beta repeat / Armadillo-type fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Up-down Bundle / 2-Layer Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-J8Y / PHOSPHATE ION / Catenin beta-1 / S-phase kinase-associated protein 1 / F-box/WD repeat-containing protein 1A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.5 Å
AuthorsSimonetta, K.R. / Clifton, M.C. / Walter, R.L. / Ranieri, G.M. / Lee, S.J.
CitationJournal: Nat Commun / Year: 2019
Title: Prospective discovery of small molecule enhancers of an E3 ligase-substrate interaction.
Authors: Simonetta, K.R. / Taygerly, J. / Boyle, K. / Basham, S.E. / Padovani, C. / Lou, Y. / Cummins, T.J. / Yung, S.L. / von Soly, S.K. / Kayser, F. / Kuriyan, J. / Rape, M. / Cardozo, M. / Gallop, ...Authors: Simonetta, K.R. / Taygerly, J. / Boyle, K. / Basham, S.E. / Padovani, C. / Lou, Y. / Cummins, T.J. / Yung, S.L. / von Soly, S.K. / Kayser, F. / Kuriyan, J. / Rape, M. / Cardozo, M. / Gallop, M.A. / Bence, N.F. / Barsanti, P.A. / Saha, A.
History
DepositionAug 22, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 3, 2019Provider: repository / Type: Initial release
Revision 1.1Apr 10, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 9, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: F-box/WD repeat-containing protein 1A
B: S-phase kinase-associated protein 1
C: Catenin beta-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,8685
Polymers69,4233
Non-polymers4452
Water25214
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, fluorescence resonance energy transfer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4090 Å2
ΔGint-40 kcal/mol
Surface area23160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.530, 82.530, 111.260
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31

-
Components

-
Protein , 2 types, 2 molecules AB

#1: Protein F-box/WD repeat-containing protein 1A / E3RSIkappaB / Epididymis tissue protein Li 2a / F-box and WD repeats protein beta-TrCP / ...E3RSIkappaB / Epididymis tissue protein Li 2a / F-box and WD repeats protein beta-TrCP / pIkappaBalpha-E3 receptor subunit


Mass: 49418.418 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BTRC, BTRCP, FBW1A, FBXW1A / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y297
#2: Protein S-phase kinase-associated protein 1 / Cyclin-A/CDK2-associated protein p19 / p19A / Organ of Corti protein 2 / OCP-2 / Organ of Corti ...Cyclin-A/CDK2-associated protein p19 / p19A / Organ of Corti protein 2 / OCP-2 / Organ of Corti protein II / OCP-II / RNA polymerase II elongation factor-like protein / SIII / Transcription elongation factor B polypeptide 1-like / p19skp1


Mass: 16459.746 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SKP1, EMC19, OCP2, SKP1A, TCEB1L / Production host: Escherichia coli (E. coli) / References: UniProt: P63208

-
Protein/peptide , 1 types, 1 molecules C

#3: Protein/peptide Catenin beta-1 / Beta-catenin


Mass: 3544.714 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P35222

-
Non-polymers , 3 types, 16 molecules

#4: Chemical ChemComp-J8Y / 2-oxo-N-[3-(1H-tetrazol-5-yl)phenyl]-6-(trifluoromethyl)-1,2-dihydropyridine-3-carboxamide


Mass: 350.255 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H9F3N6O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.15 Å3/Da / Density % sol: 60.97 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 8% PEG 4000 0.1M BTP pH 5.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Jan 27, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.5→41.265 Å / Num. obs: 29168 / % possible obs: 99.5 % / Redundancy: 4.115 % / Biso Wilson estimate: 73.77 Å2 / CC1/2: 0.991 / Rmerge(I) obs: 0.115 / Rrim(I) all: 0.134 / Χ2: 0.957 / Net I/σ(I): 10.91
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.5-2.574.4361.940.9421730.3192.201100
2.57-2.644.4391.41.2820890.4241.589100
2.64-2.714.411.041.7720500.6091.183100
2.71-2.84.3820.7332.5520000.7570.834100
2.8-2.894.320.5433.3719540.8860.62100
2.89-2.994.2640.4074.4618580.9150.465100
2.99-3.14.2290.3096.1417940.9410.35499.9
3.1-3.234.1240.2158.4817580.9720.24799.9
3.23-3.374.0860.1711.4116620.9850.19699.8
3.37-3.543.9790.12514.2415850.9880.14499.9
3.54-3.733.9280.10217.1215190.990.11899.9
3.73-3.953.8660.09218.914590.9930.10799.5
3.95-4.233.8330.07820.9413050.9930.09199.5
4.23-4.563.7560.07122.5612390.9930.08398.9
4.56-53.7680.06424.0211390.9960.07499.5
5-5.593.7520.07623.4910330.9920.08998.8
5.59-6.463.8780.11523.579260.9820.13399
6.46-7.913.8630.14124.77670.9810.16399.4
7.91-11.183.6480.08725.545710.980.10396.1
11.18-41.2653.30.09323.082870.9740.11186.4

-
Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIX1.13_2998refinement
PDB_EXTRACT3.24data extraction
XDSdata reduction
PHASERphasing
RefinementResolution: 2.5→41.265 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.98 / Phase error: 27.07
RfactorNum. reflection% reflection
Rfree0.23 2013 6.91 %
Rwork0.2135 --
obs0.2147 29129 99.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 154.71 Å2 / Biso mean: 90.1758 Å2 / Biso min: 52.49 Å2
Refinement stepCycle: final / Resolution: 2.5→41.265 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4123 0 30 14 4167
Biso mean--77.61 69.52 -
Num. residues----542
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5001-2.56260.34641400.315819392079100
2.5626-2.63190.31151380.290419342072100
2.6319-2.70930.33531540.291919662120100
2.7093-2.79680.30841420.285919142056100
2.7968-2.89670.32631440.280119662110100
2.8967-3.01260.31151420.26819542096100
3.0126-3.14970.28351480.258719552103100
3.1497-3.31570.28431540.251219572111100
3.3157-3.52330.25881350.230119282063100
3.5233-3.79520.23681440.213819372081100
3.7952-4.17680.22191490.20111949209899
4.1768-4.78040.16891330.16531950208399
4.7804-6.01980.20451520.19141915206799
6.0198-41.27060.1971380.19951852199095
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.0323-0.0233-0.01360.03140.04530.04210.0724-0.13690.024-0.05840.09980.11710.36950.08890.00021.3722-0.38380.53261.62590.03811.11385.9045-73.7519-9.3383
20.04450.0156-0.00740.0198-0.01010.00250.2445-0.2798-0.20670.68-0.2632-0.415-0.0899-0.293501.10430.02860.30421.60380.10480.81459.1319-75.7508-6.3631
30.04670.0245-0.00380.0142-0.00960.01530.10720.07110.0183-0.1352-0.38010.3026-0.14310.09560.00021.15870.46590.1661.7964-0.29511.24375.1545-62.3158-8.3512
40.0147-0.0042-0.00770.028-0.01480.0388-0.34820.05470.0429-0.18610.4170.5253-0.0127-0.198400.80860.30010.26591.68050.17681.26896.6697-64.7422-16.5233
50.0320.03520.05670.05050.06880.1086-0.8626-0.38270.1820.0342-0.29170.2314-0.2306-0.2635-0.00641.10320.16540.28862.37190.11621.26443.285-70.9967-18.9775
60.0737-0.13190.06760.2174-0.12270.0688-0.42530.191-0.10730.5238-0.4234-0.6325-0.221-0.46920.00020.95420.06880.38281.33950.06550.95314.5934-73.1369-12.4196
71.0621-0.48170.57070.4457-0.16940.3138-0.249-1.00920.62810.4006-0.5381-0.2242-0.5779-0.5956-0.07661.30170.12160.60951.43830.140.973612.9095-66.1704-0.9685
80.24590.8422-0.36443.3032-1.50720.7081-0.4499-0.6602-0.23940.5987-1.4013-0.1395-0.2668-0.2625-0.30581.39420.16340.27771.6664-0.18190.822818.6302-59.66524.9669
90.16410.1902-0.01340.1771-0.02930.02970.31150.0111-0.55661.3742-0.1470.63550.4986-0.39160.00061.16240.32380.23071.21310.06870.848721.4563-64.5247-7.9146
101.3291-0.98511.03550.7677-0.82580.9382-0.30710.07870.28960.9273-0.17510.4426-0.5525-0.2169-0.13221.30590.48430.27381.1411-0.10480.795524.0109-55.3601-3.4367
111.69291.2296-0.09131.7777-0.19240.02790.1676-1.0641-0.45831.0566-0.4007-0.5570.26770.5007-0.07751.41010.4612-0.07920.7917-0.19010.749442.6849-57.4814-2.6423
120.0510.0195-0.04150.008-0.01390.0228-0.67430.1917-0.01120.03920.47990.31160.1156-0.409900.98060.2432-0.16451.05410.27681.573150.8056-48.7889-10.1095
130.02390.0179-0.00550.03740.06150.0490.4903-0.28480.43480.4458-0.0988-0.12910.3256-0.077400.87490.06190.06570.5826-0.07750.71576.0739-0.63245.747
141.0197-0.26830.30160.85090.52850.28920.0115-0.07430.4641-0.0711-0.0811-0.25770.20090.11010.01181.00580.33370.07010.6642-0.06330.917133.687-43.649-11.4505
152.8972-0.2947-0.33781.9711-0.31272.48740.16460.0856-0.1186-0.00040.0106-0.28340.161-0.1397-00.76880.137-0.07010.4175-0.03150.647511.4286-13.167-1.5616
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'B' and (resid 3 through 8 )B3 - 8
2X-RAY DIFFRACTION2chain 'B' and (resid 9 through 17 )B9 - 17
3X-RAY DIFFRACTION3chain 'B' and (resid 18 through 24 )B18 - 24
4X-RAY DIFFRACTION4chain 'B' and (resid 25 through 32 )B25 - 32
5X-RAY DIFFRACTION5chain 'B' and (resid 33 through 38 )B33 - 38
6X-RAY DIFFRACTION6chain 'B' and (resid 39 through 45 )B39 - 45
7X-RAY DIFFRACTION7chain 'B' and (resid 46 through 58 )B46 - 58
8X-RAY DIFFRACTION8chain 'B' and (resid 59 through 78 )B59 - 78
9X-RAY DIFFRACTION9chain 'B' and (resid 79 through 94 )B79 - 94
10X-RAY DIFFRACTION10chain 'B' and (resid 95 through 109 )B95 - 109
11X-RAY DIFFRACTION11chain 'B' and (resid 110 through 128 )B110 - 128
12X-RAY DIFFRACTION12chain 'B' and (resid 129 through 139 )B129 - 139
13X-RAY DIFFRACTION13chain 'C' and (resid 30 through 40 )C30 - 40
14X-RAY DIFFRACTION14chain 'A' and (resid 138 through 252 )A138 - 252
15X-RAY DIFFRACTION15chain 'A' and (resid 253 through 547 )A253 - 547

+
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