[English] 日本語
Yorodumi
- PDB-5nx1: Combinatorial Engineering of Proteolytically Resistant APPI Varia... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5nx1
TitleCombinatorial Engineering of Proteolytically Resistant APPI Variants that Selectively Inhibit Human Kallikrein 6 for Cancer Therapy
Components
  • (Amyloid-beta A4 protein) x 3
  • Kallikrein-6
KeywordsHYDROLASE / Serine_protease / inhibitor / complex
Function / homology
Function and homology information


cornified envelope / tissue regeneration / positive regulation of G protein-coupled receptor signaling pathway / amyloid-beta complex / growth cone lamellipodium / cellular response to norepinephrine stimulus / growth cone filopodium / microglia development / collateral sprouting in absence of injury / amyloid precursor protein metabolic process ...cornified envelope / tissue regeneration / positive regulation of G protein-coupled receptor signaling pathway / amyloid-beta complex / growth cone lamellipodium / cellular response to norepinephrine stimulus / growth cone filopodium / microglia development / collateral sprouting in absence of injury / amyloid precursor protein metabolic process / hormone metabolic process / Formyl peptide receptors bind formyl peptides and many other ligands / axo-dendritic transport / regulation of Wnt signaling pathway / regulation of synapse structure or activity / axon midline choice point recognition / astrocyte activation involved in immune response / NMDA selective glutamate receptor signaling pathway / regulation of spontaneous synaptic transmission / mating behavior / growth factor receptor binding / peptidase activator activity / Golgi-associated vesicle / PTB domain binding / positive regulation of amyloid fibril formation / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / Lysosome Vesicle Biogenesis / astrocyte projection / neuron remodeling / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / nuclear envelope lumen / regulation of neuron projection development / dendrite development / positive regulation of protein metabolic process / TRAF6 mediated NF-kB activation / protein autoprocessing / regulation of cell differentiation / collagen catabolic process / Advanced glycosylation endproduct receptor signaling / signaling receptor activator activity / negative regulation of long-term synaptic potentiation / modulation of excitatory postsynaptic potential / The NLRP3 inflammasome / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / transition metal ion binding / main axon / intracellular copper ion homeostasis / regulation of multicellular organism growth / ECM proteoglycans / regulation of presynapse assembly / positive regulation of T cell migration / neuronal dense core vesicle / Purinergic signaling in leishmaniasis infection / intercellular bridge / positive regulation of chemokine production / cellular response to manganese ion / Notch signaling pathway / clathrin-coated pit / myelination / extracellular matrix organization / neuron projection maintenance / Mitochondrial protein degradation / astrocyte activation / ionotropic glutamate receptor signaling pathway / positive regulation of calcium-mediated signaling / positive regulation of mitotic cell cycle / axonogenesis / response to interleukin-1 / protein serine/threonine kinase binding / cellular response to copper ion / secretory granule / platelet alpha granule lumen / cellular response to cAMP / protein maturation / positive regulation of glycolytic process / central nervous system development / endosome lumen / positive regulation of interleukin-1 beta production / dendritic shaft / trans-Golgi network membrane / positive regulation of long-term synaptic potentiation / adult locomotory behavior / learning / positive regulation of JNK cascade / Post-translational protein phosphorylation / locomotory behavior / serine-type endopeptidase inhibitor activity / microglial cell activation / positive regulation of non-canonical NF-kappaB signal transduction / TAK1-dependent IKK and NF-kappa-B activation / regulation of long-term neuronal synaptic plasticity / cellular response to nerve growth factor stimulus / synapse organization / recycling endosome / visual learning / response to lead ion / response to wounding / positive regulation of interleukin-6 production / Golgi lumen / cognition
Similarity search - Function
Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Amyloidogenic glycoprotein, copper-binding / Amyloidogenic glycoprotein, copper-binding domain conserved site / Amyloidogenic glycoprotein, copper-binding domain superfamily / Copper-binding of amyloid precursor, CuBD / Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. / Amyloidogenic glycoprotein, amyloid-beta peptide superfamily / Beta-amyloid peptide (beta-APP) / Amyloidogenic glycoprotein, amyloid-beta peptide ...Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Amyloidogenic glycoprotein, copper-binding / Amyloidogenic glycoprotein, copper-binding domain conserved site / Amyloidogenic glycoprotein, copper-binding domain superfamily / Copper-binding of amyloid precursor, CuBD / Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. / Amyloidogenic glycoprotein, amyloid-beta peptide superfamily / Beta-amyloid peptide (beta-APP) / Amyloidogenic glycoprotein, amyloid-beta peptide / Beta-amyloid precursor protein C-terminal / Amyloidogenic glycoprotein, intracellular domain, conserved site / Beta-amyloid precursor protein C-terminus / Amyloid precursor protein (APP) intracellular domain signature. / Amyloidogenic glycoprotein, extracellular / Amyloidogenic glycoprotein, heparin-binding / Amyloidogenic glycoprotein, E2 domain / E2 domain superfamily / Amyloidogenic glycoprotein, heparin-binding domain superfamily / Amyloid A4 N-terminal heparin-binding / E2 domain of amyloid precursor protein / Amyloid precursor protein (APP) E1 domain profile. / Amyloid precursor protein (APP) E2 domain profile. / amyloid A4 / Amyloidogenic glycoprotein / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / Few Secondary Structures / Irregular / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / PH-like domain superfamily / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Amyloid-beta precursor protein / Kallikrein-6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.853 Å
AuthorsShahar, A. / Sananes, A. / Radisky, E.S. / Papo, N.
CitationJournal: J.Biol.Chem. / Year: 2018
Title: A potent, proteolysis-resistant inhibitor of kallikrein-related peptidase 6 (KLK6) for cancer therapy, developed by combinatorial engineering.
Authors: Sananes, A. / Cohen, I. / Shahar, A. / Hockla, A. / De Vita, E. / Miller, A.K. / Radisky, E.S. / Papo, N.
History
DepositionMay 9, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 30, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2019Group: Data collection / Source and taxonomy / Category: entity_src_gen / Item: _entity_src_gen.pdbx_host_org_cell_line
Revision 1.2Jun 12, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _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 1.3Jan 17, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Kallikrein-6
B: Amyloid-beta A4 protein
D: Amyloid-beta A4 protein
C: Amyloid-beta A4 protein


Theoretical massNumber of molelcules
Total (without water)42,8824
Polymers42,8824
Non-polymers00
Water3,513195
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3380 Å2
ΔGint-24 kcal/mol
Surface area15260 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.543, 77.702, 92.207
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Kallikrein-6 / Neurosin / Protease M / SP59 / Serine protease 18 / Serine protease 9 / Zyme


Mass: 24417.695 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KLK6, PRSS18, PRSS9 / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper)
References: UniProt: Q92876, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
#2: Protein/peptide Amyloid-beta A4 protein / ABPP / APPI / APP / Alzheimer disease amyloid protein / Amyloid precursor protein / Amyloid-beta ...ABPP / APPI / APP / Alzheimer disease amyloid protein / Amyloid precursor protein / Amyloid-beta precursor protein / Cerebral vascular amyloid peptide / CVAP / PreA4 / Protease nexin-II / PN-II


Mass: 2945.086 Da / Num. of mol.: 1 / Fragment: UNP residues 289-301
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APP, A4, AD1 / Production host: Komagataella phaffii GS115 (fungus) / References: UniProt: P05067
#3: Protein Amyloid-beta A4 protein / ABPP / APPI / APP / Alzheimer disease amyloid protein / Amyloid precursor protein / Amyloid-beta ...ABPP / APPI / APP / Alzheimer disease amyloid protein / Amyloid precursor protein / Amyloid-beta precursor protein / Cerebral vascular amyloid peptide / CVAP / PreA4 / Protease nexin-II / PN-II


Mass: 6295.999 Da / Num. of mol.: 1 / Fragment: UNP residues 302-346
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APP, A4, AD1 / Production host: Komagataella phaffii GS115 (fungus) / References: UniProt: P05067
#4: Protein Amyloid-beta A4 protein / ABPP / APPI / APP / Alzheimer disease amyloid protein / Amyloid precursor protein / Amyloid-beta ...ABPP / APPI / APP / Alzheimer disease amyloid protein / Amyloid precursor protein / Amyloid-beta precursor protein / Cerebral vascular amyloid peptide / CVAP / PreA4 / Protease nexin-II / PN-II


Mass: 9223.071 Da / Num. of mol.: 1 / Fragment: UNP residues 289-346
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APP, A4, AD1 / Production host: Komagataella phaffii GS115 (fungus) / References: UniProt: P05067
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 195 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.57 %
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: 0.2M Ammonium Sulfate, 0.1M Bis-Tris pH 5.5, 25% Polyethylene Glycol 3350

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.969 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jul 22, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.969 Å / Relative weight: 1
ReflectionResolution: 1.853→47.262 Å / Num. obs: 36867 / % possible obs: 99.52 % / Redundancy: 2 % / Rpim(I) all: 0.031 / Net I/σ(I): 13.48
Reflection shellResolution: 1.853→1.92 Å / Redundancy: 2 % / Mean I/σ(I) obs: 1.08 / Num. unique all: 3528 / CC1/2: 0.574 / Rpim(I) all: 0.642 / % possible all: 96.37

-
Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1AAP & 1LO6

1aap

1lo6


Resolution: 1.853→47.262 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.78
RfactorNum. reflection% reflection
Rfree0.2255 1848 5.01 %
Rwork0.1839 --
obs0.186 36853 99.42 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.853→47.262 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2536 0 0 195 2731
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0062646
X-RAY DIFFRACTIONf_angle_d0.8723602
X-RAY DIFFRACTIONf_dihedral_angle_d10.9072040
X-RAY DIFFRACTIONf_chiral_restr0.054374
X-RAY DIFFRACTIONf_plane_restr0.005475
LS refinement shell

Refine-ID: X-RAY DIFFRACTION

Resolution (Å)Highest resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.853-1.90270.34971230.3604248894
1.9027-1.95870.34231450.31012677100
1.9587-2.02190.30771290.26712659100
2.0219-2.09420.28111380.23982690100
2.0942-2.1780.26751410.21882658100
2.178-2.27710.24641490.20382692100
2.2771-2.39720.2561520.19542658100
2.3972-2.54740.22751320.18532697100
2.5474-2.7440.22451450.18892703100
2.744-3.02010.23131530.18812706100
3.0201-3.4570.22751390.18222728100
3.457-4.3550.16761490.13862753100
4.3550.2121530.15852896100
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)
12.3288-0.3744-0.49862.5395-0.16564.0502-0.07370.0328-0.1134-0.0946-0.07140.12260.1186-0.17040.16130.32140.00990.00580.1953-0.03730.1947-1.085353.037-35.2911
23.63550.9283.5693.6123.62337.99110.22240.4303-0.3075-0.3820.299-0.51980.34230.9106-0.38410.44870.04920.06870.31360.00190.35039.283153.7206-38.3311
36.62545.07830.02167.37350.91496.4687-0.15810.5505-0.0223-0.72130.08410.1820.3903-0.37960.07290.40390.1512-0.00490.2463-0.00390.27150.306150.7208-42.8447
45.1322-0.38131.15053.53750.96494.75570.10220.06540.13340.0029-0.0901-0.206-0.20060.18370.02830.29150.01050.00580.10750.0420.1993.690461.9102-36.5542
54.42070.1773-0.61272.7381-1.19610.71930.1303-0.25320.34650.08-0.02850.7004-0.7254-0.3937-0.04310.67070.0377-0.00080.3539-0.08350.2858-7.178265.6401-24.414
67.0683-1.64113.39953.4279-3.2484.07050.1638-0.1244-0.73790.3147-0.14080.32081.27710.3084-0.05540.55410.00010.11690.2112-0.00040.3528-0.909142.5144-27.6651
77.61522.93712.87947.83494.59378.388-0.0961-1.2390.970.4549-0.52630.5131-0.4821-0.54280.57340.57850.08470.00960.3696-0.08410.2769-2.759960.4638-15.6764
88.7222.6309-1.68643.2343-0.20038.6534-0.0203-0.2050.49830.78610.169-0.1887-1.00180.5024-0.11560.54270.0258-0.07760.2498-0.07510.31496.3164.2536-16.8814
93.63491.0739-5.15897.444-1.72327.4709-0.2195-0.20350.07160.76020.14180.34070.5323-0.33870.1960.47750.03160.0450.32610.01150.2512-1.967151.371-19.6542
103.2822-0.38361.06242.1197-0.97655.7433-0.3245-0.34720.06470.64110.0552-0.0671-0.089-0.03880.19760.37590.04840.00140.2279-0.02810.1742-0.232357.4921-21.0385
112.62320.5057-0.75896.7872-0.1132.9735-0.00820.1450.37750.05310.0033-0.2013-1.1077-0.134-0.06480.48980.0213-0.03830.2241-0.0040.3534.114369.5276-32.207
126.94942.9097-1.34646.9361-1.93526.8782-0.2480.03520.1048-0.46390.1446-0.13220.01420.19460.11330.3113-0.0008-0.03330.1836-0.00990.1628-15.660271.626-38.9758
138.8209-3.17110.92781.908-2.31625.9845-0.07020.34550.5517-0.3564-0.3247-0.4668-0.83280.49810.38760.7175-0.122-0.12340.38620.03870.3703-12.865979.4773-45.2557
147.5373-7.31914.27468.7872-4.13848.4006-0.42980.14430.49580.5222-0.1411-0.79880.10210.53440.53060.3217-0.0120.00760.27470.08320.302217.140445.6099-20.3335
158.9389-6.33911.89977.9768-1.0113.86960.5130.4277-0.4828-0.4868-0.5263-0.19330.91730.6861-0.05440.48310.1408-0.00890.34730.02920.334319.232938.5087-25.831
169.1365-4.5188-5.89523.62932.63235.0560.48030.64860.6994-1.2049-0.946-1.0984-0.39250.63490.250.39750.0530.09830.42910.17260.47321.394347.2015-24.9084
172.1791.2161-1.89922.17792.42239.95370.00890.548-0.3319-1.2295-0.7365-0.46510.93930.94540.75850.70860.28950.1330.92180.21760.591928.298838.8116-29.2013
186.7943.9272-0.35293.91182.68195.30770.0999-0.43730.3284-0.3959-0.33110.7018-0.2424-0.20730.16420.4056-0.0041-0.06220.3426-0.05080.2492-21.670372.2944-34.8604
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 16 through 54 )
2X-RAY DIFFRACTION2chain 'A' and (resid 55 through 67 )
3X-RAY DIFFRACTION3chain 'A' and (resid 69 through 90 )
4X-RAY DIFFRACTION4chain 'A' and (resid 91 through 123 )
5X-RAY DIFFRACTION5chain 'A' and (resid 124 through 140 )
6X-RAY DIFFRACTION6chain 'A' and (resid 141 through 155 )
7X-RAY DIFFRACTION7chain 'A' and (resid 156 through 171 )
8X-RAY DIFFRACTION8chain 'A' and (resid 172 through 184 )
9X-RAY DIFFRACTION9chain 'A' and (resid 185 through 197 )
10X-RAY DIFFRACTION10chain 'A' and (resid 198 through 226 )
11X-RAY DIFFRACTION11chain 'A' and (resid 227 through 245 )
12X-RAY DIFFRACTION12chain 'D' and (resid 16 through 47 )
13X-RAY DIFFRACTION13chain 'D' and (resid 48 through 57 )
14X-RAY DIFFRACTION14chain 'C' and (resid 3 through 17 )
15X-RAY DIFFRACTION15chain 'C' and (resid 18 through 35 )
16X-RAY DIFFRACTION16chain 'C' and (resid 36 through 47 )
17X-RAY DIFFRACTION17chain 'C' and (resid 48 through 56 )
18X-RAY DIFFRACTION18chain 'B' and (resid 3 through 15 )

+
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