[English] 日本語
Yorodumi
- PDB-8r7e: MutSbeta bound to compound CHDI-00898647 in the canonical DNA-mis... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8r7e
TitleMutSbeta bound to compound CHDI-00898647 in the canonical DNA-mismatch bound form
Components
  • (DNA mismatch repair protein ...) x 2
  • DNA (5'-D(*CP*AP*TP*CP*GP*AP*TP*CP*GP*CP*AP*GP*CP*TP*TP*CP*AP*GP*AP*TP*AP*GP*G)-3')
  • DNA (5'-D(*TP*CP*TP*AP*TP*CP*TP*GP*AP*AP*GP*CP*CP*GP*AP*TP*CP*GP*AP*TP*GP*G)-3')
KeywordsDNA BINDING PROTEIN / PROTEROS BIOSTRUCTURES GMBH / DNA mismatch Repair
Function / homology
Function and homology information


somatic recombination of immunoglobulin genes involved in immune response / MutSbeta complex / Defective Mismatch Repair Associated With MSH3 / MutSalpha complex / Defective Mismatch Repair Associated With MSH2 / Defective Mismatch Repair Associated With MSH6 / positive regulation of helicase activity / guanine/thymine mispair binding / somatic recombination of immunoglobulin gene segments / B cell mediated immunity ...somatic recombination of immunoglobulin genes involved in immune response / MutSbeta complex / Defective Mismatch Repair Associated With MSH3 / MutSalpha complex / Defective Mismatch Repair Associated With MSH2 / Defective Mismatch Repair Associated With MSH6 / positive regulation of helicase activity / guanine/thymine mispair binding / somatic recombination of immunoglobulin gene segments / B cell mediated immunity / maintenance of DNA repeat elements / positive regulation of isotype switching to IgA isotypes / centromeric DNA binding / positive regulation of isotype switching to IgG isotypes / mitotic recombination / mismatched DNA binding / negative regulation of DNA recombination / isotype switching / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / oxidative phosphorylation / response to UV-B / postreplication repair / mitotic intra-S DNA damage checkpoint signaling / ATP-dependent DNA damage sensor activity / germ cell development / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / ATP-dependent activity, acting on DNA / response to X-ray / somatic hypermutation of immunoglobulin genes / mismatch repair / B cell differentiation / determination of adult lifespan / TP53 Regulates Transcription of DNA Repair Genes / male gonad development / double-strand break repair / double-stranded DNA binding / negative regulation of neuron apoptotic process / in utero embryonic development / damaged DNA binding / chromosome, telomeric region / DNA repair / chromatin binding / enzyme binding / protein homodimerization activity / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / nucleus / membrane
Similarity search - Function
DNA mismatch repair Msh2-type / DNA mismatch repair protein Msh2 / DNA mismatch repair protein MutS-like, N-terminal / DNA mismatch repair protein MutS, connector domain / DNA mismatch repair protein MutS, clamp / DNA mismatch repair protein MutS, N-terminal / MutS, connector domain superfamily / MutS domain I / MutS domain II / MutS family domain IV ...DNA mismatch repair Msh2-type / DNA mismatch repair protein Msh2 / DNA mismatch repair protein MutS-like, N-terminal / DNA mismatch repair protein MutS, connector domain / DNA mismatch repair protein MutS, clamp / DNA mismatch repair protein MutS, N-terminal / MutS, connector domain superfamily / MutS domain I / MutS domain II / MutS family domain IV / MutS domain III / DNA mismatch repair MutS family / DNA mismatch repair protein MutS, C-terminal / DNA mismatch repair protein MutS, core / DNA mismatch repair protein MutS, core domain superfamily / MutS domain V / DNA mismatch repair proteins mutS family signature. / DNA-binding domain of DNA mismatch repair MUTS family / ATPase domain of DNA mismatch repair MUTS family / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / : / DNA / DNA (> 10) / DNA mismatch repair protein Msh3 / DNA mismatch repair protein Msh2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.783 Å
AuthorsThomsen, M. / Thieulin-Pardo, G. / Steinbacher, S. / Brace, G. / Tillack, K. / Johnson, P. / Ritzefeld, M. / Schaertl, S. / Frush, E. / Warfield, B. ...Thomsen, M. / Thieulin-Pardo, G. / Steinbacher, S. / Brace, G. / Tillack, K. / Johnson, P. / Ritzefeld, M. / Schaertl, S. / Frush, E. / Warfield, B. / Ballantyne, G. / Lee, J.-H. / Witte, D. / Finley, M. / Prasad, B. / Monteagudo, E. / Plotnikov, N. / Pacifici, R. / Maillard, M. / Wilkinson, H. / Iyer, R. / Dominguez, C. / Vogt, T. / Felsenfeld, D. / Haque, T.
Funding support United States, 1items
OrganizationGrant numberCountry
CHDI Foundation United States
CitationJournal: Chemrxiv / Year: 2024
Title: Identification of orthosteric inhibitors of MutSbeta ATPase function
Authors: Brace, G. / Tillack, K. / Johnson, P. / Ritzefeld, M. / Schaertl, S. / Frush, E. / Warfield, B. / Ballantyne, G. / Lee, J.-H. / Thieulin-Pardo, G. / Steinbacher, S. / Thomsen, M. / Witte, D. ...Authors: Brace, G. / Tillack, K. / Johnson, P. / Ritzefeld, M. / Schaertl, S. / Frush, E. / Warfield, B. / Ballantyne, G. / Lee, J.-H. / Thieulin-Pardo, G. / Steinbacher, S. / Thomsen, M. / Witte, D. / Finley, M. / Prasad, B. / Monteagudo, E. / Plotnikov, N. / Pacifici, R. / Maillard, M. / Wilkinson, H. / Iyer, R. / Dominguez, C. / Vogt, T. / Felsenfeld, D. / Haque, T.
History
DepositionNov 24, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 27, 2024Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DNA mismatch repair protein Msh2
B: DNA mismatch repair protein Msh3
C: DNA (5'-D(*TP*CP*TP*AP*TP*CP*TP*GP*AP*AP*GP*CP*CP*GP*AP*TP*CP*GP*AP*TP*GP*G)-3')
D: DNA (5'-D(*CP*AP*TP*CP*GP*AP*TP*CP*GP*CP*AP*GP*CP*TP*TP*CP*AP*GP*AP*TP*AP*GP*G)-3')
E: DNA mismatch repair protein Msh2
F: DNA mismatch repair protein Msh3
G: DNA (5'-D(*TP*CP*TP*AP*TP*CP*TP*GP*AP*AP*GP*CP*CP*GP*AP*TP*CP*GP*AP*TP*GP*G)-3')
H: DNA (5'-D(*CP*AP*TP*CP*GP*AP*TP*CP*GP*CP*AP*GP*CP*TP*TP*CP*AP*GP*AP*TP*AP*GP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)449,61227
Polymers446,8158
Non-polymers2,79719
Water2,108117
1
A: DNA mismatch repair protein Msh2
B: DNA mismatch repair protein Msh3
C: DNA (5'-D(*TP*CP*TP*AP*TP*CP*TP*GP*AP*AP*GP*CP*CP*GP*AP*TP*CP*GP*AP*TP*GP*G)-3')
D: DNA (5'-D(*CP*AP*TP*CP*GP*AP*TP*CP*GP*CP*AP*GP*CP*TP*TP*CP*AP*GP*AP*TP*AP*GP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)224,86714
Polymers223,4074
Non-polymers1,46010
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14900 Å2
ΔGint-165 kcal/mol
Surface area82340 Å2
MethodPISA
2
E: DNA mismatch repair protein Msh2
F: DNA mismatch repair protein Msh3
G: DNA (5'-D(*TP*CP*TP*AP*TP*CP*TP*GP*AP*AP*GP*CP*CP*GP*AP*TP*CP*GP*AP*TP*GP*G)-3')
H: DNA (5'-D(*CP*AP*TP*CP*GP*AP*TP*CP*GP*CP*AP*GP*CP*TP*TP*CP*AP*GP*AP*TP*AP*GP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)224,74513
Polymers223,4074
Non-polymers1,3379
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15510 Å2
ΔGint-168 kcal/mol
Surface area81850 Å2
MethodPISA
Unit cell
Length a, b, c (Å)100.473, 104.096, 122.016
Angle α, β, γ (deg.)109.331, 91.808, 109.505
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21E
32B
42F
53C
63G
74D
84H

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111SERSERILEILEAA13 - 93013 - 930
221SERSERILEILEEE13 - 93013 - 930
332SERSERLYSLYSBB227 - 112111 - 905
442SERSERLYSLYSFF227 - 112111 - 905
553DCDCDGDGCC4 - 234 - 23
663DCDCDGDGGG4 - 234 - 23
774DCDCDGDGDD27 - 492 - 24
884DCDCDGDGHH27 - 492 - 24

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

-
DNA mismatch repair protein ... , 2 types, 4 molecules AEBF

#1: Protein DNA mismatch repair protein Msh2


Mass: 104431.359 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MSH2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P43246
#2: Protein DNA mismatch repair protein Msh3


Mass: 104260.594 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MSH3 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P20585

-
DNA chain , 2 types, 4 molecules CGDH

#3: DNA chain DNA (5'-D(*TP*CP*TP*AP*TP*CP*TP*GP*AP*AP*GP*CP*CP*GP*AP*TP*CP*GP*AP*TP*GP*G)-3')


Mass: 7345.741 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#4: DNA chain DNA (5'-D(*CP*AP*TP*CP*GP*AP*TP*CP*GP*CP*AP*GP*CP*TP*TP*CP*AP*GP*AP*TP*AP*GP*G)-3')


Mass: 7369.766 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)

-
Non-polymers , 6 types, 136 molecules

#5: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-YKQ / Abivertinib / ~{N}-[3-[[2-[[3-fluoranyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-7~{H}-pyrrolo[2,3-d]pyrimidin-4-yl]oxy]phenyl]prop-2-enamide


Mass: 487.529 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C26H26FN7O2 / Feature type: SUBJECT OF INVESTIGATION
#9: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 117 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 50.95 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop
Details: 0.1 MES pH 6.5; 0.2 M NH4 Acetate; 20-25 % w/v PEG 3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER2 S 16M / Detector: PIXEL / Date: Aug 24, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.783→113.659 Å / Num. obs: 79309 / % possible obs: 92 % / Redundancy: 2.3 % / CC1/2: 0.98 / Rmerge(I) obs: 0.071 / Rpim(I) all: 0.062 / Net I/σ(I): 9
Reflection shellResolution: 2.783→3.008 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.888 / Mean I/σ(I) obs: 1.5 / Num. unique obs: 3965 / CC1/2: 0.353 / Rpim(I) all: 0.643 / % possible all: 57.7

-
Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
autoPROCdata reduction
autoPROCdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.783→113.659 Å / Cor.coef. Fo:Fc: 0.915 / Cor.coef. Fo:Fc free: 0.886 / SU B: 20.868 / SU ML: 0.395 / Cross valid method: FREE R-VALUE / ESU R Free: 0.507
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2657 3915 4.936 %
Rwork0.2226 75393 -
all0.225 --
obs-79308 72.825 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 60.459 Å2
Baniso -1Baniso -2Baniso -3
1--0.266 Å2-0.193 Å20.096 Å2
2---0.035 Å2-0.067 Å2
3---0.356 Å2
Refinement stepCycle: LAST / Resolution: 2.783→113.659 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms26824 1819 176 117 28936
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0030.01328281
X-RAY DIFFRACTIONr_bond_other_d0.0020.01726048
X-RAY DIFFRACTIONr_ext_dist_refined_d0.0730.051
X-RAY DIFFRACTIONr_angle_refined_deg1.2971.60138698
X-RAY DIFFRACTIONr_angle_other_deg1.1121.62959524
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.24153340
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.00422.91193
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.54615.0114349
X-RAY DIFFRACTIONr_dihedral_angle_other_3_deg6.018201
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.21315121
X-RAY DIFFRACTIONr_dihedral_angle_6_deg12.934206
X-RAY DIFFRACTIONr_chiral_restr0.0470.23887
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0230746
X-RAY DIFFRACTIONr_gen_planes_other0.0020.026326
X-RAY DIFFRACTIONr_nbd_refined0.1460.25178
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1420.223345
X-RAY DIFFRACTIONr_nbtor_refined0.1480.213165
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0720.212124
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.0990.2560
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0520.22
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1250.219
X-RAY DIFFRACTIONr_nbd_other0.1380.267
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1440.28
X-RAY DIFFRACTIONr_mcbond_it2.3526.7813453
X-RAY DIFFRACTIONr_mcbond_other2.3526.77913452
X-RAY DIFFRACTIONr_mcangle_it4.05310.15716762
X-RAY DIFFRACTIONr_mcangle_other4.05310.15716763
X-RAY DIFFRACTIONr_scbond_it1.957.03914828
X-RAY DIFFRACTIONr_scbond_other1.957.03914829
X-RAY DIFFRACTIONr_scangle_it3.43410.56721936
X-RAY DIFFRACTIONr_scangle_other3.43410.56721937
X-RAY DIFFRACTIONr_lrange_it6.38479.27130467
X-RAY DIFFRACTIONr_lrange_other6.38379.27230467
X-RAY DIFFRACTIONr_ncsr_local_group_10.0350.059490
X-RAY DIFFRACTIONr_ncsr_local_group_20.030.059802
X-RAY DIFFRACTIONr_ncsr_local_group_30.0410.05465
X-RAY DIFFRACTIONr_ncsr_local_group_40.0370.05536
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.035160.05
12EX-RAY DIFFRACTIONLocal ncs0.035160.05
23BX-RAY DIFFRACTIONLocal ncs0.029650.05
24FX-RAY DIFFRACTIONLocal ncs0.029650.05
35CX-RAY DIFFRACTIONLocal ncs0.040950.05
36GX-RAY DIFFRACTIONLocal ncs0.040950.05
47DX-RAY DIFFRACTIONLocal ncs0.036970.05
48HX-RAY DIFFRACTIONLocal ncs0.036970.05
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.783-2.8550.378210.3494810.3580640.8050.7996.22520.343
2.855-2.9330.321590.34612280.34578730.7440.74316.3470.347
2.933-3.0180.3841400.3423780.34375960.6640.70933.1490.336
3.018-3.1110.3661730.30934180.31274410.7360.75948.25960.302
3.111-3.2130.3322100.29141880.29371950.7750.78761.12580.278
3.213-3.3260.3272580.27848040.2869130.8120.81173.22440.259
3.326-3.4510.3132740.26554510.26767440.8160.83384.89030.246
3.451-3.5920.2783190.24557580.24764530.8670.8794.17330.225
3.592-3.7520.2733200.23557430.23761690.8740.87898.28170.217
3.752-3.9350.2432790.21855770.21959150.9060.9199.00250.201
3.935-4.1470.252740.19853200.20156410.9090.92699.16680.186
4.147-4.3980.2222880.18649850.18853290.9320.93998.94910.18
4.398-4.7010.2332210.18347180.18549980.9210.93698.81950.182
4.701-5.0770.2312280.18343710.18546420.9250.9499.07370.184
5.077-5.5610.2742320.21540340.21842920.8880.91299.39420.218
5.561-6.2150.2941720.23836730.2438670.8930.9199.43110.242
6.215-7.1730.2951520.24232360.24534020.8970.90599.58850.257
7.173-8.7770.2351320.20727550.20929010.9220.92899.51740.237
8.777-12.3760.2421080.17521020.17822270.9280.9599.23660.22
12.376-113.6590.265550.28511730.28412400.9410.88699.03230.423

+
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