[English] 日本語
Yorodumi
- PDB-3g04: Crystal structure of the TSH receptor in complex with a thyroid-s... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3g04
TitleCrystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody
Components
  • (HUMAN THYROID STIMULATING AUTOANTIBODY M22 ...) x 2
  • Thyrotropin receptor
KeywordsIMMUNE SYSTEM / TSH RECEPTOR / GPCR / THYROID / GRAVES' DISEASE / AUTOIMMUNITY / RECEPTOR-AUTOANTIBODY COMPLEX
Function / homology
Function and homology information


thyroid-stimulating hormone signaling pathway / cellular response to glycoprotein / cellular response to thyrotropin-releasing hormone / thyroid-stimulating hormone receptor activity / Hormone ligand-binding receptors / G protein-coupled peptide receptor activity / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / hormone-mediated signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / cell-cell signaling ...thyroid-stimulating hormone signaling pathway / cellular response to glycoprotein / cellular response to thyrotropin-releasing hormone / thyroid-stimulating hormone receptor activity / Hormone ligand-binding receptors / G protein-coupled peptide receptor activity / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / hormone-mediated signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / cell-cell signaling / signaling receptor activity / positive regulation of cold-induced thermogenesis / G alpha (s) signalling events / basolateral plasma membrane / cell surface receptor signaling pathway / receptor complex / G protein-coupled receptor signaling pathway / positive regulation of cell population proliferation / protein-containing complex binding / cell surface / plasma membrane
Similarity search - Function
Thyrotropin receptor / Glycoprotein hormone receptor family / BspA type Leucine rich repeat region / BspA type Leucine rich repeat region (6 copies) / Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) / Ribonuclease Inhibitor / Alpha-Beta Horseshoe / Leucine-rich repeat domain superfamily / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like ...Thyrotropin receptor / Glycoprotein hormone receptor family / BspA type Leucine rich repeat region / BspA type Leucine rich repeat region (6 copies) / Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) / Ribonuclease Inhibitor / Alpha-Beta Horseshoe / Leucine-rich repeat domain superfamily / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family) / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Thyrotropin receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsSanders, J. / Chirgadze, D.Y. / Sanders, P. / Baker, S. / Sullivan, A. / Bhardwaja, A. / Bolton, J. / Reeve, M. / Nakatake, N. / Evans, M. ...Sanders, J. / Chirgadze, D.Y. / Sanders, P. / Baker, S. / Sullivan, A. / Bhardwaja, A. / Bolton, J. / Reeve, M. / Nakatake, N. / Evans, M. / Richards, T. / Powell, M. / Miguel, R.N. / Blundell, T.L. / Furmaniak, J. / Smith, B.R.
Citation
Journal: Thyroid / Year: 2007
Title: Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody
Authors: Sanders, J. / Chirgadze, D.Y. / Sanders, P. / Baker, S. / Sullivan, A. / Bhardwaja, A. / Bolton, J. / Reeve, M. / Nakatake, N. / Evans, M. / Richards, T. / Powell, M. / Miguel, R.N. / ...Authors: Sanders, J. / Chirgadze, D.Y. / Sanders, P. / Baker, S. / Sullivan, A. / Bhardwaja, A. / Bolton, J. / Reeve, M. / Nakatake, N. / Evans, M. / Richards, T. / Powell, M. / Miguel, R.N. / Blundell, T.L. / Furmaniak, J. / Smith, B.R.
#1: Journal: Lancet / Year: 2003
Title: Human monoclonal thyroid stimulating autoantibody
Authors: Sanders, J. / Evans, M. / Premawardhana, L.D.K.E. / Depraetere, H. / Jeffreys, J. / Richards, T. / Furmaniak, J. / Smith, B.R.
#2: Journal: Thyroid / Year: 2004
Title: Characteristics of a human monoclonal autoantibody to the thyrotropin receptor: sequence structure and function
Authors: Sanders, J. / Jeffreys, J. / Depraetere, H. / Evans, M. / Richards, T. / Kiddie, A. / Brereton, K. / Premawardhana, L.D.K.E. / Chirgadze, D.Y. / Miguel, R.N. / Blundell, T.L. / Furmaniak, J. / Smith, B.R.
#3: Journal: Thyroid / Year: 2004
Title: Analysis of the thyrotropin receptor-thyrotropin interaction by comparative modeling
Authors: Miguel, R.N. / Sanders, J. / Jeffreys, J. / Depraetere, H. / Evans, M. / Richards, T. / Blundell, T.L. / Rees Smith, B. / Furmaniak, J.
#4: Journal: Thyroid / Year: 2005
Title: Comparative Modelling of the Thyrotropin Receptor
Authors: Miguel, R.N. / Sanders, J. / Blundell, T.L. / Smith, B.R. / Furmaniak, J.
#5: Journal: Thyroid / Year: 2006
Title: Effects of TSH receptor mutations on binding and biological activity of monoclonal antibodies and TSH
Authors: Sanders, J. / Bolton, J. / Sanders, P. / Jeffreys, J. / Nakatake, N. / Richards, T. / Evans, M. / Kiddie, A. / Summerhayes, S. / Roberts, E. / Miguel, R.N. / Furmaniak, J. / Smith, B.R.
#6: Journal: Thyroid / Year: 2007
Title: Molecular interactions between the TSH receptor and a Thyroid-stimulating monoclonal autoantibody
Authors: Sanders, J. / Miguel, R.N. / Bolton, J. / Bhardwaja, A. / Sanders, P. / Nakatake, N. / Evans, M. / Furmaniak, J. / Smith, B.R.
#7: Journal: J.Mol.Endocrinol. / Year: 2008
Title: FSH and TSH binding to their respective receptors: similarities, differences and implication for glycoprotein hormone specificity
Authors: Miguel, R.N. / Sanders, J. / Chirgadze, D.Y. / Blundell, T.L. / Furmaniak, J. / Rees Smith, B.
#8: Journal: To be Published / Year: 2009
Title: Thyroid stimulating autoantibody M22 mimics TSH in its binding to the TSH receptor: a comparative structural study of protein-protein interactions
Authors: Miguel, R.N. / Sanders, J. / Chirgadze, D.Y. / Furmaniak, J. / Smith, B.R.
History
DepositionJan 27, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Aug 4, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Structure summary
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / pdbx_struct_special_symmetry / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HUMAN THYROID STIMULATING AUTOANTIBODY M22 LIGHT CHAIN
B: HUMAN THYROID STIMULATING AUTOANTIBODY M22 HEAVY CHAIN
C: Thyrotropin receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,12914
Polymers74,4753
Non-polymers1,65411
Water5,206289
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7710 Å2
ΔGint-79 kcal/mol
Surface area28610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)43.888, 175.784, 205.806
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number24
Space group name H-MI212121
Components on special symmetry positions
IDModelComponents
11A-245-

HOH

21B-235-

HOH

31B-255-

HOH

41C-294-

HOH

-
Components

-
Antibody , 2 types, 2 molecules AB

#1: Antibody HUMAN THYROID STIMULATING AUTOANTIBODY M22 LIGHT CHAIN


Mass: 23043.408 Da / Num. of mol.: 1 / Fragment: FAB fragment light chain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Production host: mouse-human heterohybridoma cell line (others)
#2: Antibody HUMAN THYROID STIMULATING AUTOANTIBODY M22 HEAVY CHAIN


Mass: 24487.438 Da / Num. of mol.: 1 / Fragment: FAB fragment heavy chain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Production host: mouse-human heterohybridoma cell line (others)

-
Protein / Sugars , 2 types, 7 molecules C

#3: Protein Thyrotropin receptor / Thyroid-stimulating hormone receptor / TSH-R


Mass: 26943.828 Da / Num. of mol.: 1 / Fragment: LEUCINE RICH REPEAT DOMAIN (SEGMENT 22-260)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TSHR / Production host: TRICHOPLUSIA NI (cabbage looper) / Strain (production host): HIGH FIVE / References: UniProt: P16473
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

-
Non-polymers , 2 types, 294 molecules

#5: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 289 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.66 Å3/Da / Density % sol: 53.82 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 8% PEG 8000, 0.1M MES, 0.25M ZINC ACETATE, pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 292K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX14.2 / Wavelength: 0.98 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 6, 2006
RadiationMonochromator: SI 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.55→30 Å / Num. all: 26775 / Num. obs: 25731 / % possible obs: 96.1 % / Observed criterion σ(I): 2.5 / Redundancy: 4.6 % / Biso Wilson estimate: 47.7 Å2 / Rmerge(I) obs: 0.071 / Rsym value: 0.071 / Net I/σ(I): 10.5
Reflection shellResolution: 2.55→2.61 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.361 / Rsym value: 0.361 / % possible all: 99.2

-
Processing

Software
NameVersionClassification
PXGENdata collection
AMoREphasing
REFMAC5.2.0005refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1XWD

1xwd


Resolution: 2.55→26.72 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.904 / SU B: 17.888 / SU ML: 0.208 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.665 / ESU R Free: 0.303 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.245 1301 5.1 %RANDOM
Rwork0.181 ---
obs0.184 24426 96 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 36 Å2
Baniso -1Baniso -2Baniso -3
1-0.16 Å20 Å20 Å2
2---0.19 Å20 Å2
3---0.03 Å2
Refinement stepCycle: LAST / Resolution: 2.55→26.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5036 0 89 289 5414
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0225255
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2361.9817173
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5285651
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.59924.604202
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.20715834
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.9341518
X-RAY DIFFRACTIONr_chiral_restr0.0820.2831
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.023901
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2010.22170
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3060.23515
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1460.2322
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.1770.23
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.250.251
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1640.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined0.0460.21
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.77553363
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.67365320
X-RAY DIFFRACTIONr_scbond_it2.26152175
X-RAY DIFFRACTIONr_scangle_it3.3927.51853
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.55→2.61 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.331 95 -
Rwork0.224 1803 -
obs-1898 97.99 %
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)
10.1583-0.20310.01191.71880.82031.4269-0.03240.05790.0065-0.0352-0.0012-0.0419-0.079-0.04570.0336-0.0992-0.01020.0096-0.0050.0087-0.07966.82274.08616.829
20.68760.2497-0.3280.2971-0.22163.03670.02250.0778-0.01430.0199-0.0828-0.00210.2942-0.24160.0603-0.0899-0.06330.033-0.002-0.0539-0.0185-5.70560.60938.709
33.38680.8695-1.48423.63961.28534.7819-0.1155-0.25180.46320.1353-0.02250.2909-0.3013-0.39290.138-0.11060.062-0.01540.0031-0.04340.0174-16.45162.81673.889
40.33220.17260.26091.14520.74241.96060.00790.0186-0.0030.1340.0002-0.04810.04470.0818-0.0081-0.11180.01250.0205-0.01110.0152-0.003712.25571.28145.001
50.82011.1967-0.02493.2481-0.48841.0542-0.0206-0.1103-0.01050.09960.00510.0388-0.0492-0.01880.0154-0.0636-0.03120.0285-0.0159-0.0223-0.0933-1.04658.47579.463
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1C30 - 257
2X-RAY DIFFRACTION2B1 - 114
3X-RAY DIFFRACTION3B115 - 213
4X-RAY DIFFRACTION4A1 - 108
5X-RAY DIFFRACTION5A109 - 208

+
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://pdbjlvh1.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