[English] 日本語
Yorodumi
- PDB-5b4w: Crystal structure of Plexin inhibitor complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5b4w
TitleCrystal structure of Plexin inhibitor complex
Components
  • Plexin-B1
  • Synthesized cyclic peptide
KeywordsSIGNALING PROTEIN / Plexin / Inhibitor
Function / homology
Function and homology information


semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis / semaphorin receptor binding / negative regulation of osteoblast proliferation / semaphorin-plexin signaling pathway involved in axon guidance / semaphorin receptor complex / inhibitory synapse assembly / Sema4D induced cell migration and growth-cone collapse / RHOD GTPase cycle / semaphorin receptor activity / ossification involved in bone maturation ...semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis / semaphorin receptor binding / negative regulation of osteoblast proliferation / semaphorin-plexin signaling pathway involved in axon guidance / semaphorin receptor complex / inhibitory synapse assembly / Sema4D induced cell migration and growth-cone collapse / RHOD GTPase cycle / semaphorin receptor activity / ossification involved in bone maturation / negative regulation of cell adhesion / Sema4D mediated inhibition of cell attachment and migration / positive regulation of axonogenesis / semaphorin-plexin signaling pathway / GTPase activating protein binding / regulation of cytoskeleton organization / regulation of GTPase activity / neuron projection morphogenesis / regulation of cell migration / GTPase activator activity / G alpha (12/13) signalling events / positive regulation of GTPase activity / transmembrane signaling receptor activity / positive regulation of phosphatidylinositol 3-kinase signaling / cell migration / regulation of cell shape / intracellular signal transduction / integral component of plasma membrane / extracellular region / plasma membrane
Similarity search - Function
TIG domain found in plexin / Plexin, TIG domain 2 / Plexin, TIG domain 1 / TIG domain / Plexin cytoplasmic RasGAP domain / Plexin, cytoplasmic RasGAP domain / ligand-binding face of the semaphorins, domain 2 / ligand-binding face of the semaphorins, domain 2 / Plexin family / Plexin repeat ...TIG domain found in plexin / Plexin, TIG domain 2 / Plexin, TIG domain 1 / TIG domain / Plexin cytoplasmic RasGAP domain / Plexin, cytoplasmic RasGAP domain / ligand-binding face of the semaphorins, domain 2 / ligand-binding face of the semaphorins, domain 2 / Plexin family / Plexin repeat / Plexin repeat / Sema domain / semaphorin domain / Sema domain superfamily / Sema domain / Sema domain profile. / IPT/TIG domain / Rho GTPase activation protein / ig-like, plexins, transcription factors / PSI domain / domain found in Plexins, Semaphorins and Integrins / IPT domain / YVTN repeat-like/Quinoprotein amine dehydrogenase / Methylamine Dehydrogenase; Chain H / 7 Propeller / Immunoglobulin E-set / WD40/YVTN repeat-like-containing domain superfamily / Immunoglobulin-like fold / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
unidentified (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsMatsunaga, Y. / Kitago, Y. / Arimori, T. / Takagi, J.
Funding support Japan, 1items
OrganizationGrant numberCountry
AMED Japan
CitationJournal: Cell Chem Biol / Year: 2016
Title: Allosteric Inhibition of a Semaphorin 4D Receptor Plexin B1 by a High-Affinity Macrocyclic Peptide
Authors: Matsunaga, Y. / Bashiruddin, N.K. / Kitago, Y. / Takagi, J. / Suga, H.
History
DepositionApr 19, 2016Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 28, 2016Provider: repository / Type: Initial release
Revision 1.1Feb 26, 2020Group: Data collection / Category: chem_comp / diffrn_source
Item: _chem_comp.type / _diffrn_source.pdbx_synchrotron_site
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _entity.pdbx_description ..._chem_comp.name / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Plexin-B1
B: Plexin-B1
C: Plexin-B1
D: Plexin-B1
E: Plexin-B1
F: Plexin-B1
G: Synthesized cyclic peptide
H: Synthesized cyclic peptide
I: Synthesized cyclic peptide
J: Synthesized cyclic peptide
K: Synthesized cyclic peptide
L: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)385,26619
Polymers383,71712
Non-polymers1,5487
Water86548
1
A: Plexin-B1
G: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,1743
Polymers63,9532
Non-polymers2211
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1920 Å2
ΔGint-4 kcal/mol
Surface area19560 Å2
MethodPISA
2
B: Plexin-B1
H: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,3954
Polymers63,9532
Non-polymers4422
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2140 Å2
ΔGint0 kcal/mol
Surface area19550 Å2
MethodPISA
3
C: Plexin-B1
I: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,1743
Polymers63,9532
Non-polymers2211
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1930 Å2
ΔGint-3 kcal/mol
Surface area20350 Å2
MethodPISA
4
D: Plexin-B1
J: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,1743
Polymers63,9532
Non-polymers2211
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1920 Å2
ΔGint-2 kcal/mol
Surface area19820 Å2
MethodPISA
5
E: Plexin-B1
K: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,1743
Polymers63,9532
Non-polymers2211
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1950 Å2
ΔGint-3 kcal/mol
Surface area21670 Å2
MethodPISA
6
F: Plexin-B1
L: Synthesized cyclic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,1743
Polymers63,9532
Non-polymers2211
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1910 Å2
ΔGint-3 kcal/mol
Surface area19720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)92.426, 217.924, 106.475
Angle α, β, γ (deg.)90.00, 115.30, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Plexin-B1 / Semaphorin receptor SEP


Mass: 61933.488 Da / Num. of mol.: 6 / Fragment: UNP residues 20-535
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PLXNB1, KIAA0407, PLXN5, SEP / Plasmid: pcDNA3.1 / Cell line (production host): HEK293S GnT1- / Production host: Homo sapiens (human) / References: UniProt: O43157
#2: Protein/peptide
Synthesized cyclic peptide


Mass: 2019.380 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) unidentified (others)
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 7
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
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsThese residues are signal peptide

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.53 Å3/Da / Density % sol: 51.32 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.2 / Details: 0.1M tri-sodium citrate, 13% PEG 8000

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU / Wavelength: 1 Å
DetectorType: RAYONIX MX225HE / Detector: CCD / Date: Jul 3, 2014 / Details: KB mirror
RadiationMonochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.6→50 Å / Num. obs: 116573 / % possible obs: 97.2 % / Redundancy: 3 % / Biso Wilson estimate: 58.7 Å2 / CC1/2: 0.57 / Rmerge(I) obs: 0.15 / Net I/σ(I): 10
Reflection shellResolution: 2.6→2.64 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.737 / Mean I/σ(I) obs: 1.21 / % possible all: 88.7

-
Processing

Software
NameVersionClassification
PHENIX(dev_2341: ???)refinement
DENZOdata collection
SCALEPACKdata scaling
PHASER2.5.5phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3OL2
Resolution: 2.6→40.805 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 29.67 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2653 5686 5.02 %Random selection
Rwork0.2245 ---
obs0.2266 113157 97.11 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.6→40.805 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21089 0 98 48 21235
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00721750
X-RAY DIFFRACTIONf_angle_d1.01429741
X-RAY DIFFRACTIONf_dihedral_angle_d16.29312984
X-RAY DIFFRACTIONf_chiral_restr0.0553327
X-RAY DIFFRACTIONf_plane_restr0.0073933
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.62960.35611620.32113157X-RAY DIFFRACTION86
2.6296-2.66050.35661860.31043311X-RAY DIFFRACTION90
2.6605-2.69290.3411720.30783373X-RAY DIFFRACTION92
2.6929-2.7270.34771730.29733433X-RAY DIFFRACTION92
2.727-2.76290.37031830.29513448X-RAY DIFFRACTION94
2.7629-2.80070.32751880.29643474X-RAY DIFFRACTION94
2.8007-2.84070.30911840.29523474X-RAY DIFFRACTION95
2.8407-2.88310.32121650.28143582X-RAY DIFFRACTION96
2.8831-2.92820.29721830.2813499X-RAY DIFFRACTION96
2.9282-2.97620.36971950.27423603X-RAY DIFFRACTION97
2.9762-3.02750.30471900.27173553X-RAY DIFFRACTION97
3.0275-3.08250.35881840.27383639X-RAY DIFFRACTION98
3.0825-3.14180.31841710.27213641X-RAY DIFFRACTION98
3.1418-3.20590.32731920.26343614X-RAY DIFFRACTION98
3.2059-3.27550.31841980.24763631X-RAY DIFFRACTION99
3.2755-3.35170.27822020.24673640X-RAY DIFFRACTION99
3.3517-3.43550.28441950.2373670X-RAY DIFFRACTION99
3.4355-3.52830.26021930.22543630X-RAY DIFFRACTION99
3.5283-3.63210.28171880.22173646X-RAY DIFFRACTION99
3.6321-3.74920.26821930.21013649X-RAY DIFFRACTION99
3.7492-3.88310.23551830.21033667X-RAY DIFFRACTION99
3.8831-4.03850.23852110.2113657X-RAY DIFFRACTION99
4.0385-4.22210.24082010.19333671X-RAY DIFFRACTION99
4.2221-4.44440.22821940.17463683X-RAY DIFFRACTION99
4.4444-4.72250.19122050.16953624X-RAY DIFFRACTION99
4.7225-5.08650.19742020.17543710X-RAY DIFFRACTION100
5.0865-5.59720.25471980.19443667X-RAY DIFFRACTION100
5.5972-6.40450.24622090.21783678X-RAY DIFFRACTION100
6.4045-8.05880.26841970.21193712X-RAY DIFFRACTION100
8.0588-40.810.24591890.22213735X-RAY DIFFRACTION100
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)
10.7627-0.26080.16210.4060.18011.7797-0.0104-0.2233-0.02010.15750.0359-0.01530.0973-0.0836-0.0920.31520.0754-0.03810.4514-0.01430.3338108.6351-37.72181.4437
20.7567-0.01690.43850.7246-0.11051.81750.02960.0121-0.0840.0148-0.00380.01650.0952-0.1075-0.09560.21710.0643-0.04370.3541-0.0320.367395.2681-35.1234.9478
31.51410.0015-0.28130.78120.15081.8860.12710.1590.0337-0.0235-0.1071-0.0104-0.2518-0.0639-0.08670.4383-0.01240.11690.23780.01150.316679.48654.098128.2936
41.0471-0.2217-0.63840.84710.2561.93790.0256-0.0829-0.11030.1626-0.06460.1284-0.3114-0.6365-0.06370.58130.08590.18190.61650.01250.380751.74325.337167.7011
50.82850.11540.66690.76520.00431.64710.1043-0.0279-0.03670.23150.0954-0.09380.36060.3058-0.08540.44330.1171-0.08350.3952-0.11250.4123142.5361-61.403247.905
60.77330.26190.08891.4213-0.65261.08980.19030.06120.46330.0578-0.2406-0.0196-0.47510.4355-0.09980.4531-0.17060.07840.639-0.06780.6601148.3117-30.505126.1891
70.6161-0.36640.25850.8250.33691.92450.2210.2689-0.212-0.2185-0.08790.19030.43980.0911-0.02260.65710.1184-0.18310.3511-0.14590.4778121.5588-70.144.9775
81.3237-0.49640.16721.13610.90861.0392-0.10740.1548-0.1407-0.26630.08650.3296-0.0563-0.0136-0.1010.31870.1219-0.04110.65990.01910.428987.8347-36.656564.6973
90.4924-0.49540.34570.97520.00050.49230.07380.0710.16620.29120.124-0.2922-0.10040.3673-0.1140.3620.098-0.03590.5228-0.08150.4205113.6183-27.550152.8947
101.1202-0.07640.10241.3299-0.16751.2407-0.1019-0.2452-0.18330.46050.133-0.0135-0.2319-0.0507-0.09010.4587-0.02920.10030.3182-0.02440.382679.73785.901555.0235
111.4241-0.24230.3121.37230.23211.34710.05370.354-0.0298-0.31180.1482-0.0078-0.3534-0.529-0.09060.65470.17250.15530.76320.01460.386953.726811.69541.969
121.5161-0.11260.08730.9316-0.32751.08410.1050.4340.0863-0.0705-0.06170.0416-0.05450.0838-0.0730.3704-0.0175-0.00760.3977-0.0890.3157135.8777-50.973224.1341
131.2419-0.4734-0.66030.60380.1371.17510.0092-0.0873-0.31790.11390.2098-0.02170.36470.3541-0.12150.80280.2266-0.17960.3647-0.20550.5794136.1798-80.753424.7975
148.7751-2.17974.92745.3453-0.44873.4925-0.45580.2561.58190.57130.1436-1.13480.07860.05760.3370.8315-0.0497-0.11320.67150.12050.6119106.027-53.109264.3387
150.6388-0.54740.31031.1703-0.81031.42670.13680.1811-0.0266-0.06590.0003-0.01050.0557-0.0095-0.09570.4880.0209-0.20880.68430.00750.6999101.7429-31.842929.7109
164.86463.21944.41552.57742.80914.0364-0.2992-0.24310.2557-0.56610.03790.0408-0.8412-0.65870.33450.69270.0680.04830.55150.06640.630670.0995-12.186541.8394
178.7996.29694.30542220.60320.65580.87830.4487-1.8965-1.15430.42021.4151.31580.7140.01030.32011.0303-0.14640.986855.8137-10.880251.5652
184.5123.0545-3.48883.4351-1.59362-0.4384-0.4913-0.5759-1.0161-0.311-0.58461.55890.42040.73170.71690.1439-0.1220.50220.05020.6232120.7557-61.502940.6748
195.9343-3.83715.21944.2995-0.51699.08190.00240.30320.40920.0155-0.1497-0.45490.2319-0.06670.17030.848-0.1017-0.33750.4496-0.04640.6902114.2575-69.898727.1401
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 26:481 )A26 - 481
2X-RAY DIFFRACTION2( CHAIN B AND RESID 26:481 )B26 - 481
3X-RAY DIFFRACTION3( CHAIN C AND RESID 26:481 )C26 - 481
4X-RAY DIFFRACTION4( CHAIN D AND RESID 24:481 )D24 - 481
5X-RAY DIFFRACTION5( CHAIN E AND RESID 26:482 )E26 - 482
6X-RAY DIFFRACTION6( CHAIN E AND RESID 483:528 )E483 - 528
7X-RAY DIFFRACTION7( CHAIN F AND RESID 26:481 )F26 - 481
8X-RAY DIFFRACTION8( CHAIN G AND ( RESID 0:16 OR RESID 17:17 ) )G0 - 16
9X-RAY DIFFRACTION8( CHAIN G AND ( RESID 0:16 OR RESID 17:17 ) )G17
10X-RAY DIFFRACTION9( CHAIN H AND ( RESID 0:16 OR RESID 17:17 ) )H0 - 16
11X-RAY DIFFRACTION9( CHAIN H AND ( RESID 0:16 OR RESID 17:17 ) )H17
12X-RAY DIFFRACTION10( CHAIN I AND ( RESID 0:16 OR RESID 17:17 ) )I0 - 16
13X-RAY DIFFRACTION10( CHAIN I AND ( RESID 0:16 OR RESID 17:17 ) )I17
14X-RAY DIFFRACTION11( CHAIN J AND ( RESID 0:16 OR RESID 17:17 ) )J0 - 16
15X-RAY DIFFRACTION11( CHAIN J AND ( RESID 0:16 OR RESID 17:17 ) )J17
16X-RAY DIFFRACTION12( CHAIN K AND ( RESID 0:16 OR RESID 17:17 ) )K0 - 16
17X-RAY DIFFRACTION12( CHAIN K AND ( RESID 0:16 OR RESID 17:17 ) )K17
18X-RAY DIFFRACTION13( CHAIN L AND ( RESID 0:16 OR RESID 17:17 ) )L0 - 16
19X-RAY DIFFRACTION13( CHAIN L AND ( RESID 0:16 OR RESID 17:17 ) )L17
20X-RAY DIFFRACTION14( CHAIN A AND RESID 601:601 )A601
21X-RAY DIFFRACTION15( CHAIN B AND RESID 601:602 )B601 - 602
22X-RAY DIFFRACTION16( CHAIN C AND RESID 601:601 )C601
23X-RAY DIFFRACTION17( CHAIN D AND RESID 601:601 )D601
24X-RAY DIFFRACTION18( CHAIN E AND RESID 601:601 )E601
25X-RAY DIFFRACTION19( CHAIN F AND RESID 601:601 )F601

+
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