[English] 日本語
Yorodumi
- PDB-5iu7: Crystal structure of stabilized A2A adenosine receptor A2AR-StaR2... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5iu7
TitleCrystal structure of stabilized A2A adenosine receptor A2AR-StaR2-bRIL in complex with compound 12c at 1.9A resolution
ComponentsAdenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a
KeywordsMEMBRANE PROTEIN / G-protein-coupled receptor / integral membrane protein / chimera / thermostabilizing mutations
Function / homology
Function and homology information


positive regulation of acetylcholine secretion, neurotransmission / positive regulation of circadian sleep/wake cycle, sleep / regulation of norepinephrine secretion / negative regulation of alpha-beta T cell activation / Adenosine P1 receptors / G protein-coupled adenosine receptor activity / G protein-coupled adenosine receptor signaling pathway / response to purine-containing compound / sensory perception / positive regulation of urine volume ...positive regulation of acetylcholine secretion, neurotransmission / positive regulation of circadian sleep/wake cycle, sleep / regulation of norepinephrine secretion / negative regulation of alpha-beta T cell activation / Adenosine P1 receptors / G protein-coupled adenosine receptor activity / G protein-coupled adenosine receptor signaling pathway / response to purine-containing compound / sensory perception / positive regulation of urine volume / NGF-independant TRKA activation / Surfactant metabolism / protein kinase C-activating G protein-coupled receptor signaling pathway / synaptic transmission, dopaminergic / synaptic transmission, cholinergic / inhibitory postsynaptic potential / negative regulation of vascular permeability / type 5 metabotropic glutamate receptor binding / positive regulation of glutamate secretion / blood circulation / intermediate filament / response to caffeine / eating behavior / presynaptic active zone / alpha-actinin binding / membrane depolarization / regulation of calcium ion transport / asymmetric synapse / axolemma / response to inorganic substance / cellular defense response / prepulse inhibition / phagocytosis / positive regulation of apoptotic signaling pathway / response to amphetamine / excitatory postsynaptic potential / presynaptic modulation of chemical synaptic transmission / positive regulation of synaptic transmission, glutamatergic / neuron projection morphogenesis / locomotory behavior / regulation of mitochondrial membrane potential / synaptic transmission, glutamatergic / central nervous system development / positive regulation of long-term synaptic potentiation / astrocyte activation / apoptotic signaling pathway / positive regulation of protein secretion / positive regulation of synaptic transmission, GABAergic / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / negative regulation of inflammatory response / vasodilation / blood coagulation / cell-cell signaling / presynaptic membrane / G alpha (s) signalling events / postsynaptic membrane / negative regulation of neuron apoptotic process / electron transfer activity / periplasmic space / calmodulin binding / response to xenobiotic stimulus / inflammatory response / iron ion binding / negative regulation of cell population proliferation / dendrite / neuronal cell body / glutamatergic synapse / lipid binding / apoptotic process / heme binding / protein-containing complex binding / regulation of DNA-templated transcription / enzyme binding / membrane / identical protein binding / plasma membrane
Similarity search - Function
Adenosine A2A receptor / Adenosine receptor / Cytochrome b562 / Cytochrome b562 / Cytochrome c/b562 / Serpentine type 7TM GPCR chemoreceptor Srsx / 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)
Similarity search - Domain/homology
Chem-6DY / CHOLESTEROL / OLEIC ACID / (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate / (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate / Soluble cytochrome b562 / Adenosine receptor A2a
Similarity search - Component
Biological speciesHomo sapiens (human)
Escherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsSegala, E. / Guo, D. / Cheng, R.K.Y. / Bortolato, A. / Deflorian, F. / Dore, A.S. / Errey, J.C. / Heitman, L.H. / Ijzerman, A.P. / Marshall, F.H. / Cooke, R.M.
Funding support1items
OrganizationGrant numberCountry
Innovative Medicines Initiative Joint Undertaking115366
CitationJournal: J.Med.Chem. / Year: 2016
Title: Controlling the Dissociation of Ligands from the Adenosine A2A Receptor through Modulation of Salt Bridge Strength.
Authors: Segala, E. / Guo, D. / Cheng, R.K. / Bortolato, A. / Deflorian, F. / Dore, A.S. / Errey, J.C. / Heitman, L.H. / IJzerman, A.P. / Marshall, F.H. / Cooke, R.M.
History
DepositionMar 17, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jun 29, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2016Group: Database references
Revision 1.2Jan 10, 2024Group: 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,90733
Polymers47,9971
Non-polymers9,91132
Water2,828157
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10390 Å2
ΔGint47 kcal/mol
Surface area21400 Å2
MethodPISA
Unit cell
Length a, b, c (Å)39.384, 180.036, 139.835
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

-
Components

-
Protein , 1 types, 1 molecules A

#1: Protein Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a / Cytochrome b-562


Mass: 47996.746 Da / Num. of mol.: 1
Mutation: A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, ...Mutation: A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A,A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Escherichia coli (E. coli)
Gene: ADORA2A, ADORA2, cybC / Plasmid: pFAST-bac / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P29274, UniProt: P0ABE7

-
Non-polymers , 7 types, 189 molecules

#2: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#3: Chemical ChemComp-6DY / 2-(furan-2-yl)-N~5~-[2-(4-phenylpiperidin-1-yl)ethyl][1,2,4]triazolo[1,5-a][1,3,5]triazine-5,7-diamine


Mass: 404.468 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H24N8O
#4: Chemical
ChemComp-CLR / CHOLESTEROL / Cholesterol


Mass: 386.654 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H46O
#5: Chemical
ChemComp-OLA / OLEIC ACID / Oleic acid


Mass: 282.461 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: C18H34O2
#6: Chemical
ChemComp-OLB / (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate


Mass: 356.540 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C21H40O4
#7: Chemical ChemComp-OLC / (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate / 1-Oleoyl-R-glycerol


Mass: 356.540 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H40O4
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 157 / 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: 2.58 Å3/Da / Density % sol: 52.36 % / Description: rectangular
Crystal growTemperature: 293 K / Method: lipidic cubic phase
Details: 0.lM tri-sodium citrate pH 5.3-5.4, 0.05M sodium thiocyanate, 29-32% PEG400, 2% (v/v) 2,5-hexanediol
PH range: 5.3-5.4

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9686 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 6, 2015 / Details: (double) KB mirror pair
RadiationMonochromator: Double Si(111) crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9686 Å / Relative weight: 1
ReflectionResolution: 1.9→33.71 Å / Num. obs: 39593 / % possible obs: 99.4 % / Redundancy: 4.4 % / Biso Wilson estimate: 28.9 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.103 / Net I/σ(I): 10
Reflection shellResolution: 1.9→1.94 Å / Redundancy: 4.4 % / Rmerge(I) obs: 1.007 / Mean I/σ(I) obs: 1.5 / % possible all: 99.8

-
Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSVERSION March 1, 2015data reduction
Aimlessversion 0.5.9data scaling
PHASER2.5.7phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5IU4

5iu4


Resolution: 1.9→33.708 Å / SU ML: 0.2 / Cross valid method: FREE R-VALUE / σ(F): 0.02 / Phase error: 19.37 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.198 3726 4.95 %
Rwork0.1703 --
obs0.1717 39555 99.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.9→33.708 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3031 0 538 157 3726
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.013863
X-RAY DIFFRACTIONf_angle_d0.8115186
X-RAY DIFFRACTIONf_dihedral_angle_d15.8652142
X-RAY DIFFRACTIONf_chiral_restr0.05585
X-RAY DIFFRACTIONf_plane_restr0.005622
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9001-1.92410.31461110.29732694X-RAY DIFFRACTION100
1.9241-1.94940.34061340.28892681X-RAY DIFFRACTION100
1.9494-1.97610.3641260.2772686X-RAY DIFFRACTION100
1.9761-2.00440.28541510.26422637X-RAY DIFFRACTION100
2.0044-2.03430.2951460.2412646X-RAY DIFFRACTION100
2.0343-2.06610.24871700.23482658X-RAY DIFFRACTION100
2.0661-2.09990.26531330.22482644X-RAY DIFFRACTION99
2.0999-2.13610.23661550.21042633X-RAY DIFFRACTION100
2.1361-2.1750.22951160.20582678X-RAY DIFFRACTION99
2.175-2.21680.20911600.19662586X-RAY DIFFRACTION99
2.2168-2.2620.18311410.17962653X-RAY DIFFRACTION99
2.262-2.31120.22531210.17522697X-RAY DIFFRACTION100
2.3112-2.3650.25231460.16882610X-RAY DIFFRACTION99
2.365-2.42410.2141200.15862689X-RAY DIFFRACTION99
2.4241-2.48960.20761880.15842587X-RAY DIFFRACTION99
2.4896-2.56280.17811270.15062660X-RAY DIFFRACTION100
2.5628-2.64550.15471290.14842676X-RAY DIFFRACTION100
2.6455-2.740.15671430.13892617X-RAY DIFFRACTION100
2.74-2.84970.16411690.14032666X-RAY DIFFRACTION100
2.8497-2.97930.17291670.13782615X-RAY DIFFRACTION99
2.9793-3.13630.15351150.14782643X-RAY DIFFRACTION100
3.1363-3.33260.17581250.14512705X-RAY DIFFRACTION100
3.3326-3.58970.17441330.14862669X-RAY DIFFRACTION100
3.5897-3.95040.15841330.14542624X-RAY DIFFRACTION99
3.9504-4.52090.18991300.14542630X-RAY DIFFRACTION99
4.5209-5.69140.1881270.16932650X-RAY DIFFRACTION98
5.6914-33.7130.1921100.18272611X-RAY DIFFRACTION97
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)
11.5243-0.11570.06627.6265-2.31183.29970.1092-0.0257-0.0073-0.303-0.05740.4231-0.0378-0.1848-0.01870.1752-0.015-0.01190.2006-0.00980.0878-11.3183-4.70357.1391
29.01534.21680.63991.98460.32090.08530.005-0.0696-1.4862-0.11910.14390.55031.2678-0.5444-0.0690.6412-0.1529-0.07050.27590.07770.4597-10.8679-30.040615.1594
31.7059-1.26350.54277.4395-0.02261.18030.0646-0.0525-0.0584-0.0428-0.04060.17780.0912-0.1787-0.03990.1085-0.02110.01530.17230.010.0572-10.199-4.320217.1719
43.3533-4.0424-0.21197.93380.78850.921-0.0662-0.1164-0.0410.19580.0531-0.07530.1594-0.07880.0230.1447-0.0175-0.0210.18250.01080.0748-2.4406-9.362124.0002
54.934-5.6801-0.88749.52164.0414.0907-0.6799-1.0615-1.41591.21830.14550.28580.90620.67840.68610.7043-0.04020.03590.41190.14730.51350.1727-32.204928.661
62.38861.3334-0.53367.7017-2.12762.27680.0693-0.1589-0.23610.3158-0.11010.04810.5035-0.20820.06190.2388-0.0365-0.00040.21420.02860.1066-7.5946-12.353529.6952
73.0385-1.82651.86372.1817-2.98724.847-0.105-0.14290.60130.2489-0.0686-0.0445-0.7239-0.08970.09390.28530.0527-0.03180.215-0.03350.2596-7.973716.713227.1974
84.511-3.92681.1797.3394-1.46182.74790.01110.00650.23420.0412-0.1046-0.1238-0.16910.02230.06710.1123-0.00980.00970.15240.00590.08810.41297.608625.1851
92.9899-1.5878-1.46411.53911.94972.685-0.0856-0.1488-0.41360.28690.2162-0.32410.40880.1867-0.20040.19830.0368-0.04180.18890.00950.290412.6758-20.602221.6939
100.9278-0.01930.36296.80010.42291.39020.07320.0257-0.287-0.35780.0301-0.29970.30170.1776-0.0720.17160.05530.0160.17040.0210.18137.3215-13.39914.9511
114.9063-2.35513.07458.59431.44733.0717-0.52080.49440.6104-0.21610.3497-0.3791-0.63120.93010.12940.2586-0.05760.03730.31040.06620.260611.149416.30516.4813
121.60962.15760.5497.3567-0.26041.5022-0.03630.12050.014-0.38240.01080.16750.11230.0729-0.00680.16150.01020.00940.18820.01040.0804-0.6061-4.62348.3494
137.27310.25312.90997.42710.66557.3775-0.03610.782-0.6891-1.21750.31810.39920.695-0.3446-0.32420.6845-0.1421-0.03660.3298-0.05090.3122-11.309-25.03133.212
146.0261-6.75860.3789.23892.62595.6785-0.0836-0.03080.6351-1.0692-0.3671-1.0822-0.03660.07290.43810.48570.12460.14980.38040.09021.07925.4454-49.156616.691
154.2111-3.3254-4.11273.37891.51158.0352-0.3866-1.2921.190.19640.0229-0.8864-0.49790.63990.40180.43770.0234-0.11570.4567-0.1490.938423.6603-53.14325.8393
163.7448-0.93412.39536.19221.1572.5897-0.2112-1.27810.05110.41310.65440.84360.165-0.4437-0.47150.49080.04190.02610.42490.13790.673615.1798-58.558323.7831
173.4269-3.34512.71835.5764-3.23352.7925-0.1459-0.2154-0.1017-0.34960.05220.14850.65210.34260.22930.74840.21930.19110.42080.10840.882925.8411-65.412518.7479
186.37282.67343.13213.7939-0.92426.91880.66190.6689-0.6906-1.5815-0.1070.72270.97390.2691-0.47830.84430.1671-0.06960.35090.06070.827715.0829-55.521412.9657
196.69581.40182.38979.6403-3.15397.8340.05720.1088-0.6455-0.9851-0.3012-0.5631-0.2014-0.05310.20940.82380.2289-0.05730.3593-0.03920.578311.8705-46.997413.6956
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' (resid -1 through 34)
2X-RAY DIFFRACTION2chain 'A' (resid 35 through 38)
3X-RAY DIFFRACTION3chain 'A' (resid 39 through 73)
4X-RAY DIFFRACTION4chain 'A' (resid 74 through 108)
5X-RAY DIFFRACTION5chain 'A' (resid 109 through 117)
6X-RAY DIFFRACTION6chain 'A' (resid 118 through 137)
7X-RAY DIFFRACTION7chain 'A' (resid 138 through 161)
8X-RAY DIFFRACTION8chain 'A' (resid 162 through 186)
9X-RAY DIFFRACTION9chain 'A' (resid 187 through 208)
10X-RAY DIFFRACTION10chain 'A' (resid 219 through 259)
11X-RAY DIFFRACTION11chain 'A' (resid 260 through 265)
12X-RAY DIFFRACTION12chain 'A' (resid 266 through 292)
13X-RAY DIFFRACTION13chain 'A' (resid 293 through 307)
14X-RAY DIFFRACTION14chain 'A' (resid 1001 through 1021)
15X-RAY DIFFRACTION15chain 'A' (resid 1022 through 1042)
16X-RAY DIFFRACTION16chain 'A' (resid 1059 through 1081)
17X-RAY DIFFRACTION17chain 'A' (resid 1082 through 1093)
18X-RAY DIFFRACTION18chain 'A' (resid 1094 through 1101)
19X-RAY DIFFRACTION19chain 'A' (resid 1102 through 1106)

+
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