[English] 日本語
Yorodumi
- PDB-4eoz: Crystal structure of the SPOP BTB domain complexed with the Cul3 ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4eoz
TitleCrystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain
Components
  • Cullin-3
  • Speckle-type POZ protein
KeywordsPROTEIN BINDING / E3 Ubiquitin Ligase / Nucleus
Function / homology
Function and homology information


positive regulation of mitotic cell cycle phase transition / trophectodermal cellular morphogenesis / liver morphogenesis / POZ domain binding / nuclear protein quality control by the ubiquitin-proteasome system / polar microtubule / COPII vesicle coating / anaphase-promoting complex-dependent catabolic process / regulation protein catabolic process at postsynapse / RHOBTB3 ATPase cycle ...positive regulation of mitotic cell cycle phase transition / trophectodermal cellular morphogenesis / liver morphogenesis / POZ domain binding / nuclear protein quality control by the ubiquitin-proteasome system / polar microtubule / COPII vesicle coating / anaphase-promoting complex-dependent catabolic process / regulation protein catabolic process at postsynapse / RHOBTB3 ATPase cycle / cell projection organization / positive regulation of mitotic metaphase/anaphase transition / embryonic cleavage / stem cell division / Notch binding / fibroblast apoptotic process / RHOBTB1 GTPase cycle / negative regulation of type I interferon production / molecular function inhibitor activity / Cul3-RING ubiquitin ligase complex / mitotic metaphase chromosome alignment / ubiquitin ligase complex scaffold activity / negative regulation of Rho protein signal transduction / stress fiber assembly / positive regulation of cytokinesis / regulation of proteolysis / sperm flagellum / protein monoubiquitination / endoplasmic reticulum to Golgi vesicle-mediated transport / protein K48-linked ubiquitination / RHOBTB2 GTPase cycle / protein autoubiquitination / gastrulation / regulation of cellular response to insulin stimulus / positive regulation of TORC1 signaling / intrinsic apoptotic signaling pathway / cyclin binding / positive regulation of protein ubiquitination / kidney development / integrin-mediated signaling pathway / cellular response to amino acid stimulus / Degradation of DVL / Hedgehog 'on' state / protein destabilization / Wnt signaling pathway / G1/S transition of mitotic cell cycle / Regulation of RAS by GAPs / protein polyubiquitination / spindle pole / mitotic spindle / KEAP1-NFE2L2 pathway / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / cell migration / Neddylation / cellular response to oxidative stress / ubiquitin-dependent protein catabolic process / gene expression / proteasome-mediated ubiquitin-dependent protein catabolic process / Potential therapeutics for SARS / postsynapse / nuclear speck / protein ubiquitination / inflammatory response / positive regulation of cell population proliferation / centrosome / ubiquitin protein ligase binding / glutamatergic synapse / negative regulation of transcription by RNA polymerase II / Golgi apparatus / extracellular exosome / nucleoplasm / identical protein binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #240 / Cullin Repeats / SPOP, C-terminal BACK domain / : / BPM/SPOP, BACK domain / 5 helical Cullin repeat like / MATH domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / MATH/TRAF domain / MATH/TRAF domain profile. ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #240 / Cullin Repeats / SPOP, C-terminal BACK domain / : / BPM/SPOP, BACK domain / 5 helical Cullin repeat like / MATH domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / MATH/TRAF domain / MATH/TRAF domain profile. / meprin and TRAF homology / TRAF-like / Cullin protein neddylation domain / Cullin, conserved site / Cullin family signature. / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / Cullin / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin family / Cullin family profile. / BTB/POZ domain / BTB domain profile. / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / SKP1/BTB/POZ domain superfamily / Helix non-globular / Special / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Speckle-type POZ protein / Cullin-3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.4 Å
AuthorsPrive, G.G. / Errington, W.J.
CitationJournal: Structure / Year: 2012
Title: Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.
Authors: Errington, W.J. / Khan, M.Q. / Bueler, S.A. / Rubinstein, J.L. / Chakrabartty, A. / Prive, G.G.
History
DepositionApr 16, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 30, 2012Provider: repository / Type: Initial release
Revision 1.1Jan 9, 2013Group: Database references
Revision 1.2Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Speckle-type POZ protein
C: Speckle-type POZ protein
B: Cullin-3
D: Cullin-3


Theoretical massNumber of molelcules
Total (without water)119,2584
Polymers119,2584
Non-polymers00
Water82946
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5950 Å2
ΔGint-40 kcal/mol
Surface area40740 Å2
MethodPISA
2
A: Speckle-type POZ protein
B: Cullin-3


Theoretical massNumber of molelcules
Total (without water)59,6292
Polymers59,6292
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1640 Å2
ΔGint-10 kcal/mol
Surface area21660 Å2
MethodPISA
3
C: Speckle-type POZ protein
D: Cullin-3


Theoretical massNumber of molelcules
Total (without water)59,6292
Polymers59,6292
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1660 Å2
ΔGint-10 kcal/mol
Surface area21730 Å2
MethodPISA
Unit cell
Length a, b, c (Å)213.166, 76.944, 85.834
Angle α, β, γ (deg.)90.00, 108.34, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein Speckle-type POZ protein / HIB homolog 1 / Roadkill homolog 1


Mass: 16167.548 Da / Num. of mol.: 2 / Fragment: BTB domain from SPOP, unp residues 177-319
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SPOP / Plasmid: pET32a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: O43791
#2: Protein Cullin-3 / CUL-3


Mass: 43461.695 Da / Num. of mol.: 2 / Fragment: N-terminal domain from Cul3, unp residue 20-381 / Mutation: I342R, L346D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CUL3, KIAA0617 / Plasmid: pET32a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q13618
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 46 / 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: 2.8 Å3/Da / Density % sol: 56.13 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.025M Hepes pH 6.5, 0.1M MgCl2, 13% PEG 2000, 11% 2,4-Methyl-2-Pentanediol, VAPOR DIFFUSION, HANGING DROP, temperature 298K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9794 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 17, 2007 / Details: mirrors
RadiationMonochromator: Double-crystal monochromator Si-111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionResolution: 2.4→19.61 Å / Num. all: 51676 / Num. obs: 49937 / % possible obs: 95.6 % / Observed criterion σ(F): 1.34 / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rsym value: 0.052 / Net I/σ(I): 20.4
Reflection shellResolution: 2.4→2.4856 Å / Mean I/σ(I) obs: 2.2 / Rsym value: 0.495 / % possible all: 74

-
Processing

Software
NameVersionClassification
HKL-3000data collection
SOLVEphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: SAD / Resolution: 2.4→19.61 Å / SU ML: 0.73 / σ(F): 1.34 / Phase error: 30.48 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2627 2513 5.09 %Random
Rwork0.211 ---
obs0.2137 49397 95.59 %-
all-51676 --
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 62.202 Å2 / ksol: 0.324 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--1.225 Å20 Å2-0.7866 Å2
2--0.356 Å2-0 Å2
3---0.8691 Å2
Refinement stepCycle: LAST / Resolution: 2.4→19.61 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6739 0 0 46 6785
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0136839
X-RAY DIFFRACTIONf_angle_d1.4499186
X-RAY DIFFRACTIONf_dihedral_angle_d17.7312636
X-RAY DIFFRACTIONf_chiral_restr0.11014
X-RAY DIFFRACTIONf_plane_restr0.0051193
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.44610.4281010.32571860X-RAY DIFFRACTION69
2.4461-2.49590.34331270.3092193X-RAY DIFFRACTION81
2.4959-2.55010.34641360.31462498X-RAY DIFFRACTION92
2.5501-2.60930.38311410.30082669X-RAY DIFFRACTION98
2.6093-2.67440.33061470.27742702X-RAY DIFFRACTION100
2.6744-2.74650.31241330.28392729X-RAY DIFFRACTION100
2.7465-2.82710.39771400.27472711X-RAY DIFFRACTION100
2.8271-2.9180.34831270.26252684X-RAY DIFFRACTION100
2.918-3.0220.32861180.2472759X-RAY DIFFRACTION100
3.022-3.14250.3081570.25282692X-RAY DIFFRACTION100
3.1425-3.28490.27641400.23172704X-RAY DIFFRACTION99
3.2849-3.45720.25641400.22072707X-RAY DIFFRACTION99
3.4572-3.67250.27591600.20882688X-RAY DIFFRACTION99
3.6725-3.95390.25271460.18742681X-RAY DIFFRACTION99
3.9539-4.34790.22671640.16832663X-RAY DIFFRACTION98
4.3479-4.96810.20171570.16572682X-RAY DIFFRACTION98
4.9681-6.22580.27151520.20042728X-RAY DIFFRACTION99
6.2258-19.61060.2471270.21662534X-RAY DIFFRACTION90
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)
17.8533-1.86412.93223.5855-1.9052.870.09331.4474-0.15451.9121-0.38541.5989-0.37710.4144-0.14871.3741-0.49180.29891.0608-0.08321.667355.960324.856817.2368
23.15730.9621-0.84016.0905-4.19833.77060.19820.679-0.689-0.12580.49061.82752.166-0.582-0.56220.7078-0.151-0.02330.57230.06230.670868.778226.48715.1072
35.3893-5.5762-5.9235.9416.41437.02280.57031.75820.2605-0.7463-1.04050.09910.0199-1.49330.34470.7782-0.11470.03350.8376-0.03980.505579.239529.3095-2.354
48.3993-0.815-4.6327.2986-4.50396.55560.08680.0349-0.13820.7134-0.1559-0.05080.4646-0.24930.06290.433-0.11560.01610.4251-0.02090.489784.649830.491810.0558
54.211-3.0214.08062.2749-2.94943.9390.5191-0.36270.5591-1.86750.3751-0.2924-1.033-0.3882-0.9320.8502-0.18820.1660.72350.10320.767492.944336.78632.9094
64.231-1.2123-2.08574.3455-2.42875.0545-1.38631.3965-0.2034-2.16151.0591-0.8175-0.54540.35130.01810.8625-0.34040.02570.6773-0.03180.630488.721624.3991-1.6699
79.0837-7.7948-4.84757.64565.54366.5260.27870.7287-1.329-1.32380.18750.68530.5276-0.6953-0.32350.9331-0.1806-0.03810.4529-0.03020.647377.976520.05074.222
86.6738-6.22520.48346.12150.77254.34310.5706-0.5074-1.6746-1.9428-0.02481.24650.3124-0.0837-0.72770.9108-0.2898-0.02630.5440.03141.066574.905911.46456.2145
92.61340.9189-1.80629.2962-0.34984.3181-0.0669-0.528-0.53460.2877-0.10480.27760.13680.34430.07560.7899-0.07460.10380.47020.10260.673383.746913.871911.9932
102.57421.2921-0.28872.1896-1.53221.2256-0.0586-0.2236-0.87171.5699-0.0021-0.92741.1704-0.74740.2250.9761-0.2306-0.07120.73990.16890.619475.322727.198519.5413
118.4088-7.2455-6.32536.67576.11515.6092-0.4124-0.39960.7731-0.75110.6446-0.5149-0.35650.4979-0.05890.5951-0.1097-0.05630.53670.06370.528173.858945.618313.7741
128.2684-3.1250.1493.768-3.84996.47350.05040.87520.6575-1.0721-0.6117-0.1874-0.2280.39540.1720.7374-0.1101-0.07680.57340.05890.444366.039142.78543.4039
138.2777-3.1771-6.30876.26171.25457.15741.7605-0.35841.7859-0.7930.20320.2806-1.94410.3082-1.51581.2345-0.2091-0.0850.68180.10731.038264.46450.81912.706
148.3746-1.3843-0.50146.1764-0.11856.1871-0.196-0.9043-0.16110.9302-0.00290.8860.1455-0.34040.24260.684-0.10520.08540.7049-0.00720.622158.894237.360720.8014
157.2295-1.287-0.06476.42481.19997.57540.00720.5722-0.4131-0.8011-0.0088-0.17930.50480.59980.06860.6633-0.0160.0970.53490.01740.4003104.026223.84236.1081
164.80683.42981.04979.07153.7465.2499-0.24060.18980.0327-0.2310.31820.14380.1440.3157-0.11070.40810.07090.01130.52650.03720.3553107.480834.118819.8665
175.1185-1.29660.58733.24644.37576.9152-0.38310.3508-0.0945-0.13170.09110.1974-0.05460.07230.20070.459-0.08480.00990.49540.00690.5261108.763348.593334.3185
185.85953.79663.36032.63231.7672.8028-0.432-0.26950.5523-0.66940.1644-0.4752-1.11030.3237-0.41420.7380.001-0.05290.58350.040.7278112.635255.969350.8182
193.6152-1.18211.34235.13872.98559.835-0.4031-0.08050.45290.2973-0.13130.4723-0.4808-0.39820.66860.43020.0404-0.01460.3898-0.02890.6081102.276754.966850.2254
206.3028-0.3734-0.66796.8161-0.10856.9818-0.3061-0.93131.14991.1572-0.04990.9049-0.9953-0.39880.24560.75110.1283-0.04540.6079-0.11980.7555101.852459.649667.7208
212.2464-0.1980.85191.4968-1.65484.65350.4631-1.29260.23891.0645-2.35442.4356-1.0568-1.13080.94851.3963-0.20390.61291.2585-0.08411.0812100.960355.372778.4239
225.8764-5.5009-5.7455.03215.30045.5550.2648-0.34571.1408-0.66280.47790.5257-0.7237-0.1865-0.61770.98430.012-0.13290.6958-0.14821.059447.356956.54191.8775
232.6951-0.1165-0.61953.09081.72727.4179-0.30090.25040.3284-0.32130.06770.1077-0.89330.05870.14930.6637-0.0375-0.19450.64070.00870.777949.587245.0803-8.7175
245.8724-1.4507-2.38415.96824.71546.1276-0.50180.6175-0.0385-0.8040.3044-0.4074-0.5330.6930.00660.879-0.244-0.0841.08220.0880.614652.702233.7424-31.6449
252.0285-0.9772-0.84377.77786.55745.2155-0.09690.2240.091-1.0836-0.23520.4682-1.151-0.16120.57160.6937-0.18350.04431.09-0.07550.592346.619523.7936-35.3756
262.1613-0.8703-3.65324.61021.14458.1505-0.26031.0527-0.0397-0.2050.1255-0.2444-0.5211.22020.41830.51440.03140.04731.477-0.110.815954.78816.6401-37.8097
273.1844-1.072-2.83475.34971.11773.2308-0.27721.04020.01610.19050.2071-0.41431.29090.3144-0.04990.73720.16360.0421.3378-0.05310.880853.56192.5967-48.4118
284.8494-0.5283-0.20117.88366.19674.8228-0.3211.42620.2145-0.9866-0.54780.8558-1.76460.26031.43691.12240.45440.0051.31150.12051.225349.6401-7.6435-48.9687
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 179:185)
2X-RAY DIFFRACTION2chain 'A' and (resseq 186:196)
3X-RAY DIFFRACTION3chain 'A' and (resseq 197:214)
4X-RAY DIFFRACTION4chain 'A' and (resseq 215:230)
5X-RAY DIFFRACTION5chain 'A' and (resseq 231:238)
6X-RAY DIFFRACTION6chain 'A' and (resseq 239:247)
7X-RAY DIFFRACTION7chain 'A' and (resseq 248:260)
8X-RAY DIFFRACTION8chain 'A' and (resseq 261:269)
9X-RAY DIFFRACTION9chain 'A' and (resseq 270:292)
10X-RAY DIFFRACTION10chain 'C' and (resseq 180:196)
11X-RAY DIFFRACTION11chain 'C' and (resseq 197:214)
12X-RAY DIFFRACTION12chain 'C' and (resseq 215:238)
13X-RAY DIFFRACTION13chain 'C' and (resseq 239:247)
14X-RAY DIFFRACTION14chain 'C' and (resseq 248:295)
15X-RAY DIFFRACTION15chain 'B' and (resseq 24:69)
16X-RAY DIFFRACTION16chain 'B' and (resseq 70:154)
17X-RAY DIFFRACTION17chain 'B' and (resseq 155:205)
18X-RAY DIFFRACTION18chain 'B' and (resseq 206:227)
19X-RAY DIFFRACTION19chain 'B' and (resseq 228:268)
20X-RAY DIFFRACTION20chain 'B' and (resseq 269:308)
21X-RAY DIFFRACTION21chain 'B' and (resseq 309:325)
22X-RAY DIFFRACTION22chain 'D' and (resseq 24:45)
23X-RAY DIFFRACTION23chain 'D' and (resseq 46:154)
24X-RAY DIFFRACTION24chain 'D' and (resseq 155:194)
25X-RAY DIFFRACTION25chain 'D' and (resseq 195:226)
26X-RAY DIFFRACTION26chain 'D' and (resseq 227:268)
27X-RAY DIFFRACTION27chain 'D' and (resseq 269:308)
28X-RAY DIFFRACTION28chain 'D' and (resseq 309:324)

+
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