[English] 日本語
Yorodumi
- PDB-8rlv: TCR in complex with HLA-E*01:03 bound to HBV envelope 371-379 L6I... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8rlv
TitleTCR in complex with HLA-E*01:03 bound to HBV envelope 371-379 L6I peptide
Components
  • (T cell receptor ...) x 2
  • Beta-2-microglobulin
  • HLA class I histocompatibility antigen, alpha chain E
  • Large envelope protein
KeywordsIMMUNE SYSTEM / TCR-MHC / TCR / HLA-E / HBV / affinity matured / pHLA
Function / homology
Function and homology information


detection of tumor cell / positive regulation of antibody-dependent cellular cytotoxicity / regulation of natural killer cell mediated immunity / positive regulation of TRAIL production / antigen processing and presentation of exogenous peptide antigen via MHC class Ib / MHC class Ib protein complex / positive regulation of natural killer cell mediated immunity / positive regulation of natural killer cell cytokine production / natural killer cell lectin-like receptor binding / natural killer cell tolerance induction ...detection of tumor cell / positive regulation of antibody-dependent cellular cytotoxicity / regulation of natural killer cell mediated immunity / positive regulation of TRAIL production / antigen processing and presentation of exogenous peptide antigen via MHC class Ib / MHC class Ib protein complex / positive regulation of natural killer cell mediated immunity / positive regulation of natural killer cell cytokine production / natural killer cell lectin-like receptor binding / natural killer cell tolerance induction / negative regulation of natural killer cell activation / positive regulation of natural killer cell activation / caveolin-mediated endocytosis of virus by host cell / positive regulation of natural killer cell mediated cytotoxicity / positive regulation of interleukin-13 production / alpha-beta T cell receptor complex / positive regulation of natural killer cell proliferation / negative regulation of natural killer cell mediated cytotoxicity / T cell mediated cytotoxicity directed against tumor cell target / positive regulation of immunoglobulin production / 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 / T cell receptor complex / positive regulation of interleukin-4 production / beta-2-microglobulin binding / MHC class I protein binding / protection from natural killer cell mediated cytotoxicity / 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 / T cell receptor binding / negative regulation of T cell proliferation / : / : / positive regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / negative regulation of receptor binding / DAP12 interactions / cellular response to iron ion / lumenal side of endoplasmic reticulum membrane / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / response to bacterium / peptide antigen assembly with MHC class II protein complex / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / MHC class II protein complex / negative regulation of forebrain neuron differentiation / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / response to molecule of bacterial origin / HFE-transferrin receptor complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / antigen processing and presentation of exogenous peptide antigen via MHC class II / MHC class I protein complex / positive regulation of immune response / peptide antigen binding / negative regulation of neurogenesis / positive regulation of T cell mediated cytotoxicity / positive regulation of receptor-mediated endocytosis / multicellular organismal-level iron ion homeostasis / positive regulation of T cell activation / cellular response to nicotine / specific granule lumen / recycling endosome membrane / phagocytic vesicle membrane / positive regulation of cellular senescence / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / negative regulation of epithelial cell proliferation / Interferon gamma signaling / positive regulation of tumor necrosis factor production / MHC class II protein complex binding / Interferon alpha/beta signaling / Modulation by Mtb of host immune system / antibacterial humoral response / late endosome membrane / sensory perception of smell / positive regulation of protein binding / tertiary granule lumen / DAP12 signaling / signaling receptor activity / negative regulation of neuron projection development / iron ion transport / T cell differentiation in thymus / ER-Phagosome pathway / early endosome membrane / protein refolding / protein homotetramerization / adaptive immune response / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / cell surface receptor signaling pathway / defense response to Gram-positive bacterium
Similarity search - Function
Large envelope protein S / Major surface antigen from hepadnavirus / : / : / : / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I alpha chain, alpha1 alpha2 domains ...Large envelope protein S / Major surface antigen from hepadnavirus / : / : / : / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / 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 / Immunoglobulin V-Type / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / Immunoglobulin V-set domain / MHC classes I/II-like antigen recognition protein / Immunoglobulin V-set domain / : / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
T cell receptor alpha variable 12-2 / T cell receptor beta variable 6-5 / T cell receptor alpha chain MC.7.G5 / T cell receptor beta chain MC.7.G5 / HLA class I histocompatibility antigen, alpha chain E / Beta-2-microglobulin / Large envelope protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Hepatitis B virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.609 Å
AuthorsPengelly, R.J. / Godinho, L.F.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Not funded United Kingdom
CitationJournal: Nat Commun / Year: 2024
Title: Viral sequence determines HLA-E-restricted T cell recognition of hepatitis B surface antigen.
Authors: Murugesan, G. / Paterson, R.L. / Kulkarni, R. / Ilkow, V. / Suckling, R.J. / Connolly, M.M. / Karuppiah, V. / Pengelly, R. / Jadhav, A. / Donoso, J. / Heunis, T. / Bunjobpol, W. / Philips, G. ...Authors: Murugesan, G. / Paterson, R.L. / Kulkarni, R. / Ilkow, V. / Suckling, R.J. / Connolly, M.M. / Karuppiah, V. / Pengelly, R. / Jadhav, A. / Donoso, J. / Heunis, T. / Bunjobpol, W. / Philips, G. / Ololade, K. / Kay, D. / Sarkar, A. / Barber, C. / Raj, R. / Perot, C. / Grant, T. / Treveil, A. / Walker, A. / Dembek, M. / Gibbs-Howe, D. / Hock, M. / Carreira, R.J. / Atkin, K.E. / Dorrell, L. / Knox, A. / Leonard, S. / Salio, M. / Godinho, L.F.
History
DepositionJan 3, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 16, 2024Provider: repository / Type: Initial release
Revision 1.1Feb 12, 2025Group: 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.year

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HLA class I histocompatibility antigen, alpha chain E
B: Beta-2-microglobulin
C: Large envelope protein
D: T cell receptor alpha variable 12-2,T cell receptor alpha chain MC.7.G5
E: T cell receptor beta variable 6-5,T cell receptor beta chain MC.7.G5
F: HLA class I histocompatibility antigen, alpha chain E
G: Beta-2-microglobulin
H: Large envelope protein
I: T cell receptor alpha variable 12-2,T cell receptor alpha chain MC.7.G5
J: T cell receptor beta variable 6-5,T cell receptor beta chain MC.7.G5


Theoretical massNumber of molelcules
Total (without water)188,19310
Polymers188,19310
Non-polymers00
Water2,342130
1
A: HLA class I histocompatibility antigen, alpha chain E
B: Beta-2-microglobulin
C: Large envelope protein
D: T cell receptor alpha variable 12-2,T cell receptor alpha chain MC.7.G5
E: T cell receptor beta variable 6-5,T cell receptor beta chain MC.7.G5


Theoretical massNumber of molelcules
Total (without water)94,0975
Polymers94,0975
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: HLA class I histocompatibility antigen, alpha chain E
G: Beta-2-microglobulin
H: Large envelope protein
I: T cell receptor alpha variable 12-2,T cell receptor alpha chain MC.7.G5
J: T cell receptor beta variable 6-5,T cell receptor beta chain MC.7.G5


Theoretical massNumber of molelcules
Total (without water)94,0975
Polymers94,0975
Non-polymers00
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)80.185, 153.813, 93.400
Angle α, β, γ (deg.)90.000, 96.628, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
32A
42A
53A
63A
74A
84A

NCS domain segments:

Refine code: 1 / Auth asym-ID: A / Label asym-ID: A

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth seq-IDLabel seq-ID
111GLYGLYPROPRO1 - 2761 - 276
211GLYGLYPROPRO1 - 2761 - 276
322GLYGLYHISHIS1 - 991 - 99
422GLYGLYHISHIS1 - 991 - 99
533SERSERTHRTHR2 - 1902 - 190
633SERSERTHRTHR2 - 1902 - 190
744HISHISASPASP3 - 2383 - 238
844HISHISASPASP3 - 2383 - 238

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8

-
Components

-
Protein , 2 types, 4 molecules AFBG

#1: Protein HLA class I histocompatibility antigen, alpha chain E / MHC class I antigen E


Mass: 31824.008 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-E, HLA-6.2, HLAE / Production host: Escherichia coli (E. coli) / References: UniProt: P13747
#2: Protein Beta-2-microglobulin


Mass: 11879.356 Da / Num. of mol.: 2 / Fragment: UNP residues 21-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli (E. coli) / References: UniProt: P61769

-
T cell receptor ... , 2 types, 4 molecules DIEJ

#4: Protein T cell receptor alpha variable 12-2,T cell receptor alpha chain MC.7.G5 / MC.7.G5 TRA / TR alpha chain TRAV38-2DV8*01J31*01C*01


Mass: 21944.373 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRAV12-2, TRA / Production host: Escherichia coli (E. coli) / References: UniProt: A0A075B6T6, UniProt: P0DTU3
#5: Protein T cell receptor beta variable 6-5,T cell receptor beta chain MC.7.G5 / TR beta chain TRBV25-1*01J2S3*01C2*01 / MC.7.G5 TRB


Mass: 27436.559 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRBV6-5, TRB / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0K0K1A5, UniProt: P0DTU4

-
Protein/peptide / Non-polymers , 2 types, 132 molecules CH

#3: Protein/peptide Large envelope protein / L glycoprotein / L-HBsAg / LHB / Large S protein / Large surface protein / Major surface antigen


Mass: 1012.285 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Hepatitis B virus / References: UniProt: Q67953
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 130 / 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: 3.04 Å3/Da / Density % sol: 59.54 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 20% (w/v) PEG 3350, 100 mM BIS-TRIS propane pH 8.5, 200 mM sodium sulfate Collection Temp: 100

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Feb 14, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.609→79.65 Å / Num. obs: 67783 / % possible obs: 99.2 % / Redundancy: 7.1 % / CC1/2: 0.998 / Rmerge(I) obs: 0.142 / Rpim(I) all: 0.057 / Net I/σ(I): 0.142
Reflection shellResolution: 2.609→2.65 Å / Rmerge(I) obs: 3.246 / Mean I/σ(I) obs: 0.4 / Num. unique obs: 3323 / CC1/2: 0.313 / Rpim(I) all: 1.345

-
Processing

Software
NameVersionClassification
REFMAC5.8.0403refinement
DIALS3.8.2data reduction
DIALS3.8.2data scaling
PHASER2.8.3phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.609→79.65 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.928 / SU B: 20.743 / SU ML: 0.36 / Cross valid method: FREE R-VALUE / ESU R: 0.544 / ESU R Free: 0.3
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2506 3360 4.961 %
Rwork0.1976 64366 -
all0.2 --
obs-67726 99.097 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 94.35 Å2
Baniso -1Baniso -2Baniso -3
1-0.208 Å20 Å24.013 Å2
2--2.416 Å2-0 Å2
3----3.464 Å2
Refinement stepCycle: LAST / Resolution: 2.609→79.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12910 0 0 130 13040
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01213270
X-RAY DIFFRACTIONr_bond_other_d0.0020.01611887
X-RAY DIFFRACTIONr_angle_refined_deg1.6251.65618036
X-RAY DIFFRACTIONr_angle_other_deg0.5471.57527417
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.4351597
X-RAY DIFFRACTIONr_dihedral_angle_2_deg11.812591
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.556102134
X-RAY DIFFRACTIONr_dihedral_angle_6_deg16.02410675
X-RAY DIFFRACTIONr_chiral_restr0.0670.21901
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0215749
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023223
X-RAY DIFFRACTIONr_nbd_refined0.210.22570
X-RAY DIFFRACTIONr_symmetry_nbd_other0.2050.211666
X-RAY DIFFRACTIONr_nbtor_refined0.1840.26214
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0870.27302
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1520.2394
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.020.23
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1050.211
X-RAY DIFFRACTIONr_nbd_other0.1890.252
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2170.23
X-RAY DIFFRACTIONr_mcbond_it8.6989.5366430
X-RAY DIFFRACTIONr_mcbond_other8.6889.5366429
X-RAY DIFFRACTIONr_mcangle_it12.5917.1148013
X-RAY DIFFRACTIONr_mcangle_other12.58917.1148014
X-RAY DIFFRACTIONr_scbond_it8.5649.776840
X-RAY DIFFRACTIONr_scbond_other8.5639.776841
X-RAY DIFFRACTIONr_scangle_it12.67317.79510023
X-RAY DIFFRACTIONr_scangle_other12.67217.79510024
X-RAY DIFFRACTIONr_lrange_it15.95889.14314400
X-RAY DIFFRACTIONr_lrange_other15.95789.14714399
X-RAY DIFFRACTIONr_ncsr_local_group_10.0910.058849
X-RAY DIFFRACTIONr_ncsr_local_group_20.0930.053126
X-RAY DIFFRACTIONr_ncsr_local_group_30.1130.055112
X-RAY DIFFRACTIONr_ncsr_local_group_40.1230.057132
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.091370.05009
12AX-RAY DIFFRACTIONLocal ncs0.091370.05009
23AX-RAY DIFFRACTIONLocal ncs0.092880.05009
24AX-RAY DIFFRACTIONLocal ncs0.092880.05009
35AX-RAY DIFFRACTIONLocal ncs0.11260.05009
36AX-RAY DIFFRACTIONLocal ncs0.11260.05009
47AX-RAY DIFFRACTIONLocal ncs0.123110.05008
48AX-RAY DIFFRACTIONLocal ncs0.123110.05008
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.609-2.6770.4352260.4084705X-RAY DIFFRACTION97.3352
2.677-2.750.3942480.3784632X-RAY DIFFRACTION98.9858
2.75-2.830.3842210.3694458X-RAY DIFFRACTION98.7756
2.83-2.9170.3492160.3484357X-RAY DIFFRACTION98.7689
2.917-3.0120.3262100.3154224X-RAY DIFFRACTION98.8849
3.012-3.1180.3082090.2924087X-RAY DIFFRACTION99.009
3.118-3.2350.3372230.2623937X-RAY DIFFRACTION99.0712
3.235-3.3670.2951700.2343834X-RAY DIFFRACTION99.1826
3.367-3.5160.2851860.2243679X-RAY DIFFRACTION99.2808
3.516-3.6880.3021860.2143493X-RAY DIFFRACTION99.3519
3.688-3.8870.2061920.1693313X-RAY DIFFRACTION99.4044
3.887-4.1220.2151820.1533135X-RAY DIFFRACTION99.4305
4.122-4.4060.2021620.1272969X-RAY DIFFRACTION99.4284
4.406-4.7570.1651520.1162756X-RAY DIFFRACTION99.4868
4.757-5.210.1741320.1172564X-RAY DIFFRACTION99.741
5.21-5.8210.231190.1632324X-RAY DIFFRACTION99.633
5.821-6.7160.2651200.182052X-RAY DIFFRACTION99.8162
6.716-8.2110.2281010.1541699X-RAY DIFFRACTION99.8336
8.211-11.5510.207700.1421371X-RAY DIFFRACTION99.7922
11.551-79.650.337350.279777X-RAY DIFFRACTION100

+
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