[English] 日本語
Yorodumi
- PDB-7tue: Crystal structure of Tapasin in complex with HLA-B*44:05 (T73C) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7tue
TitleCrystal structure of Tapasin in complex with HLA-B*44:05 (T73C)
Components
  • Beta-2-microglobulin
  • HLA class I histocompatibility antigen, B alpha chain
  • Tapasin
KeywordsIMMUNE SYSTEM / tapasin / histocompatibility complex class I / MHC-I / HLA / peptide editing / peptide loading complex / PLC / antigen presentation / immune response
Function / homology
Function and homology information


MHC class Ib protein complex assembly / peptide antigen stabilization / Tapasin-ERp57 complex / MHC class I protein complex binding / TAP2 binding / TAP1 binding / regulation of protein complex stability / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / TAP complex binding / MHC class I protein binding ...MHC class Ib protein complex assembly / peptide antigen stabilization / Tapasin-ERp57 complex / MHC class I protein complex binding / TAP2 binding / TAP1 binding / regulation of protein complex stability / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / TAP complex binding / MHC class I protein binding / endoplasmic reticulum-Golgi intermediate compartment membrane / protein folding chaperone / : / : / 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 / 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 / MHC class II protein complex binding / positive regulation of protein binding / Modulation by Mtb of host immune system / late endosome membrane / sensory perception of smell / unfolded protein binding / tertiary granule lumen / DAP12 signaling / negative regulation of neuron projection development / iron ion transport / T cell differentiation in thymus / ER-Phagosome pathway / regulation of gene expression / protein refolding / protein-containing complex assembly / early endosome membrane / molecular adaptor activity / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / Amyloid fiber formation / endoplasmic reticulum lumen / Golgi membrane / external side of plasma membrane / lysosomal membrane / focal adhesion / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane / cytosol
Similarity search - Function
Tapasin / : / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Beta-2-Microglobulin / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set ...Tapasin / : / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Beta-2-Microglobulin / : / 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 / Immunoglobulins / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Tapasin / Beta-2-microglobulin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsJiang, J. / Natarajan, K. / Kim, E. / Boyd, L.F. / Margulies, D.H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Nat Commun / Year: 2022
Title: Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.
Authors: Jiang, J. / Taylor, D.K. / Kim, E.J. / Boyd, L.F. / Ahmad, J. / Mage, M.G. / Truong, H.V. / Woodward, C.H. / Sgourakis, N.G. / Cresswell, P. / Margulies, D.H. / Natarajan, K.
History
DepositionFeb 2, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 7, 2022Provider: repository / Type: Initial release
Revision 1.1Sep 28, 2022Group: Database references
Category: citation / citation_author / pdbx_database_related
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
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HLA class I histocompatibility antigen, B alpha chain
D: Tapasin
B: Beta-2-microglobulin


Theoretical massNumber of molelcules
Total (without water)88,4233
Polymers88,4233
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)116.866, 116.866, 131.141
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number169
Space group name H-MP61
Space group name HallP61
Symmetry operation#1: x,y,z
#2: x-y,x,z+1/6
#3: y,-x+y,z+5/6
#4: -y,x-y,z+1/3
#5: -x+y,-x,z+2/3
#6: -x,-y,z+1/2

-
Components

#1: Protein HLA class I histocompatibility antigen, B alpha chain


Mass: 31804.158 Da / Num. of mol.: 1 / Mutation: T73C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-B44:05 / Plasmid: pET21b / Production host: Escherichia coli BL21(DE3) (bacteria)
#2: Protein Tapasin / TPN / TPSN / NGS-17 / TAP-associated protein / TAP-binding protein


Mass: 44739.641 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TAPBP, NGS17, TAPA / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): S2 / References: UniProt: O15533
#3: Protein Beta-2-microglobulin


Mass: 11879.356 Da / Num. of mol.: 1 / Fragment: UNP residues 21-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Plasmid: pET3A / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P61769
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.92 Å3/Da / Density % sol: 57.93 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 / Details: 2.0M AmSO4, 0.1M Tris / PH range: 6.5-8.5

-
Data collection

DiffractionMean temperature: 273 K / Ambient temp details: LN blow / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 30, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.1→80.12 Å / Num. obs: 18395 / % possible obs: 99.83 % / Redundancy: 5.8 % / CC1/2: 0.94 / CC star: 0.985 / Rmerge(I) obs: 0.3367 / Rpim(I) all: 0.1488 / Rrim(I) all: 0.3687 / Net I/σ(I): 3.22
Reflection shellResolution: 3.1→3.216 Å / Redundancy: 6 % / Rmerge(I) obs: 0.978 / Mean I/σ(I) obs: 0.9 / Num. unique obs: 1831 / CC1/2: 0.587 / CC star: 0.86 / Rpim(I) all: 0.435 / % possible all: 99.62

-
Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3F8U
Resolution: 3.1→80.12 Å / Cross valid method: FREE R-VALUE / σ(F): 242.33 / Phase error: 28.661
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.3088 920 5 %
Rwork0.2856 17472 -
obs0.2982 18392 99.82 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 71.76 Å2
Refinement stepCycle: LAST / Resolution: 3.1→80.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5630 0 0 0 5630
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00235796
X-RAY DIFFRACTIONf_angle_d0.63777918
X-RAY DIFFRACTIONf_chiral_restr0.0431845
X-RAY DIFFRACTIONf_plane_restr0.00561046
X-RAY DIFFRACTIONf_dihedral_angle_d17.02212121
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1-3.270.35141310.32182501X-RAY DIFFRACTION94.63
3.27-3.470.37331300.28562472X-RAY DIFFRACTION94.97
3.47-3.740.27531310.27372489X-RAY DIFFRACTION94.82
3.74-4.120.26861300.27982478X-RAY DIFFRACTION94.98
4.12-4.710.32021320.26462516X-RAY DIFFRACTION95.02
4.72-5.940.31161310.28932486X-RAY DIFFRACTION94.78
5.94-80.120.36971340.3372531X-RAY DIFFRACTION94.62
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.309250655876-0.1194337035680.2075519259240.0604742206009-0.0586308395690.1718116414690.1899932273050.0194350846042-0.0503146973812-0.0868390719617-0.009349827781960.0476889333250.1203965832370.043143982362-0.003585714116510.510259378618-0.124659017507-0.1945699871790.2234402918180.1003055590870.643349762598-46.3829.492-42.022
20.0186237794453-0.010184183858-0.01184259531960.01099354834770.02248529938250.0611476488842-0.016631441374-0.0124855190604-0.04678171900520.1113047473620.0706427691739-0.06155778031610.04422928276340.027792827152-0.003394394644450.83099356881-0.0380411291111-0.1431614577270.251775482718-0.1465350775240.829128745109-51.85721.568-31.175
30.007890387089350.0115424811922-0.01590311821380.0287676159449-0.04546834766610.07258597766780.000179075698248-0.0210524894233-0.071928707830.0737014183148-0.01041350183070.0410821628045-0.0189248521107-0.00524516927959-0.034267441870.823520313977-0.190418371279-0.06066518968850.226562903329-0.02231967539140.840745053787-42.81719.471-43.867
40.00101772758947-0.006105893255550.001732833955420.04105292741910.01960962328270.1591686268480.0009038276029510.06295535201730.06090421875180.05855288619040.06503332883090.0353647751598-0.130475880276-0.0568468779245-0.00992405904630.719327243024-0.1723799640640.2810157245030.5907576480760.2475002481160.729545253417-43.04629.107-37.858
53.1183792172E-6-0.00010249088664-0.000120158174245-8.13195426319E-5-4.77236078877E-5-0.000124429371945-0.01340430619780.0186105973978-0.0074247597766-0.00834033909994-0.0388600330517-0.015021458660.0377784428420.007660817463-0.05661997966350.4689808227050.1710262240460.08211927399190.560528551026-0.2057379211450.358533667578-41.80337.794-28.654
60.203766700102-9.57805956511E-5-0.2041566168970.0614253329853-0.05410826989310.2510833602-0.07993128569310.005353628995350.0507181693167-0.0225660187253-0.00187567723635-0.02867216463-0.03712236620270.0285417424757-0.1776290841110.264314861264-0.0930486441867-0.1016183612470.6051900349930.1630460451030.210729659444-35.33823.561-39.72
70.02941258490240.0848550662821-0.01847420728110.221620362609-0.08877051510020.112043393457-0.174540796145-0.0437977025842-0.112676953372-0.0139592160356-0.01194899997910.2150997349980.1002112471050.0459916167813-0.3134015141260.389368373785-0.01317912519190.04464682822590.1419256340280.2588898602980.728376274304-25.64562.349-2.565
80.1812725157010.001034928214740.2665506504290.153295861881-0.1961338398050.642296335149-0.2499551836850.320015194431-0.108088269190.157603468416-0.188353014164-0.0468731023334-0.0466025369754-0.255091182572-0.3058947686510.189848323921-0.1017295195010.1846271093860.376331272369-0.01082053773480.635649425014-30.7253.8837.391
90.00284155309118-0.0146130549517-0.002856733405660.07710339393310.0431359783145-0.002878513292570.07097666972670.220656917452-0.234887122045-0.0231850814835-0.0586609554765-0.0331679344480.04783777154090.05996985129150.05998888792910.1341211546270.104837336517-0.1774467808410.482509704688-0.2140777386031.15694258603-25.56642.89315.612
100.340196562486-0.1554561382230.2227825430060.158929154316-0.2634025774480.4391929852140.3401859251910.153742195812-0.137919842857-0.1667200559040.05612937491060.05939436563490.4423851212260.004816985182220.3085891053530.526955867122-0.0219283648924-0.4760953115980.2418282039730.1330064761561.07459453851-25.66233.406-1.965
110.07488356794750.117441369965-0.004401460320630.1669293009730.06276818760450.5165346474190.1867532402290.009926528165520.194991018319-0.1080286339190.1641836864760.156521924173-0.0930206554638-0.236760008840.1122350117070.42839304142-0.2055715378990.05120727860260.2398865712060.2022141766321.09235960398-20.21621.019-37.907
120.3648605600430.0707323149265-0.06438592653060.282025461506-0.1433583073950.0565402024184-0.137640837076-0.339045894274-0.5818715719-0.108842387932-0.146403794038-0.08155715573540.2463916632540.109376258747-0.0152285299550.3295391488520.1660751397190.12157549710.302015937521-0.04632611335070.717147557339-55.07533.962-11.62
130.03572007181640.028365963918-0.02759791739160.0102679681514-0.0164154029970.0137754187696-0.199663310073-0.116243618112-0.005495557067040.132342472906-0.211627806743-0.145153920824-0.148226931856-0.1564892422550.000142603672110.3274691377420.00906571819744-0.08119706915580.486706169470.005858401598150.946107253565-47.60533.3682.186
140.01687183679230.00426071491197-0.009125031187610.0166433921713-0.0301531302010.03022236512320.04336985601570.02077980020920.1931775822230.150393931757-0.003337589244890.0794561964811-0.01709338408550.1545099860220.002445220970390.400090380873-0.145737705404-0.1417603099080.361664717937-0.0286719210980.501939938277-40.96610.996-15.06
150.07088518669110.1662495380650.2899210532560.3775102720910.6661460762651.16713544520.0875437127829-0.0220011517585-0.152371147655-0.09722017434720.395964286188-0.3240505022890.0332395463220.1663747089330.2267463503510.2991260264940.00971845917660.04540270728390.2465696470250.1539015052961.11929060658-31.48714.692-12.494
160.00147416014669-0.004193485705710.003282750085060.0118641937267-0.01257277139460.0133920794554-0.150974684072-0.0415619470053-0.0648839060834-0.1588898802990.0290079744714-0.07206711250040.126013497799-0.04235090568220.0001089888000720.810695834129-0.03260999283630.1156550545850.4287254719510.04588155976170.806915047411-38.99723.826-28.499
170.02296975856320.0205105338211-0.03147324709720.08470459203050.03597233682750.104656872791-0.07189695727610.02076660778790.140136938560.0939066399058-0.0135476954675-0.0829469069071-0.011926322685-0.0437776123586-0.01920897909730.337332666545-0.0169272789626-0.1450777598840.387134687180.1735664625810.311386787262-39.20710.241-44.278
180.04078237381720.03032426302090.02272275311040.0419258160434-0.01659351355830.06869379044790.0649340507483-0.09939064910590.0429581999770.005456780653450.02030809006730.02655818417120.01464140391290.02042113217150.01994992892180.192319543251-0.0608209800739-0.03196356930440.5909717615410.3157509786390.621400271877-43.14418.028-35.165
190.07863804597020.08400354661580.01151166088660.106194370124-0.006375590298180.02216361245080.00857977429851-0.0449638278970.0186365719965-0.0281255966389-0.00528795926422-0.03028206082-0.03819422970720.0142090651687-0.04235441369610.743438502358-0.29653935133-0.1012515388160.420392214629-0.1670378485750.775707842938-48.03830.104-23.009
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN B AND RESID 36:46 )B36 - 46
2X-RAY DIFFRACTION2( CHAIN B AND RESID 47:64 )B47 - 64
3X-RAY DIFFRACTION3( CHAIN B AND RESID 65:77 )B65 - 77
4X-RAY DIFFRACTION4( CHAIN B AND RESID 78:83 )B78 - 83
5X-RAY DIFFRACTION5( CHAIN B AND RESID 84:90 )B84 - 90
6X-RAY DIFFRACTION6( CHAIN B AND RESID 91:98 )B91 - 98
7X-RAY DIFFRACTION7( CHAIN D AND RESID 1:69 )D1 - 69
8X-RAY DIFFRACTION8( CHAIN D AND RESID 70:155 )D70 - 155
9X-RAY DIFFRACTION9( CHAIN D AND RESID 156:238 )D156 - 238
10X-RAY DIFFRACTION10( CHAIN D AND RESID 239:277 )D239 - 277
11X-RAY DIFFRACTION11( CHAIN D AND RESID 278:381 )D278 - 381
12X-RAY DIFFRACTION12( CHAIN A AND RESID 1:103 )A1 - 103
13X-RAY DIFFRACTION13( CHAIN A AND RESID 104:174 )A104 - 174
14X-RAY DIFFRACTION14( CHAIN A AND RESID 175:197 )A175 - 197
15X-RAY DIFFRACTION15( CHAIN A AND RESID 198:274 )A198 - 274
16X-RAY DIFFRACTION16( CHAIN B AND RESID 3:11 )B3 - 11
17X-RAY DIFFRACTION17( CHAIN B AND RESID 12:19 )B12 - 19
18X-RAY DIFFRACTION18( CHAIN B AND RESID 20:28 )B20 - 28
19X-RAY DIFFRACTION19( CHAIN B AND RESID 29:35 )B29 - 35

+
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