[English] 日本語
Yorodumi
- PDB-4lo8: HA70(D3)-HA17 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4lo8
TitleHA70(D3)-HA17
Components
  • HA-17
  • HA-70
KeywordsPROTEIN TRANSPORT / progenitor toxin complex / botulinum neurotoxin / botulism / neurotoxin associated protein / hemagglutinin / carbohydrate/sugar binding / secreted protein
Function / homology
Function and homology information


Toxicity of botulinum toxin type A (botA) / Toxicity of botulinum toxin type B (botB) / extracellular region
Similarity search - Function
Hemagglutinin component HA-17 / Jelly Rolls - #1090 / Hemagglutinin component HA-70, C-terminal / Haemagglutinin 70 C-terminal domain / Clostridium botulinum HA-17 domain / Clostridium enterotoxin / Clostridium enterotoxin / Ricin B-like lectins / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) ...Hemagglutinin component HA-17 / Jelly Rolls - #1090 / Hemagglutinin component HA-70, C-terminal / Haemagglutinin 70 C-terminal domain / Clostridium botulinum HA-17 domain / Clostridium enterotoxin / Clostridium enterotoxin / Ricin B-like lectins / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesClostridium botulinum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsLee, K. / Gu, S. / Jin, L. / Le, T.T. / Cheng, L.W. / Strotmeier, J. / Kruel, A.M. / Yao, G. / Perry, K. / Rummel, A. / Jin, R.
CitationJournal: PLoS Pathog / Year: 2013
Title: Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity.
Authors: Kwangkook Lee / Shenyan Gu / Lei Jin / Thi Tuc Nghi Le / Luisa W Cheng / Jasmin Strotmeier / Anna Magdalena Kruel / Guorui Yao / Kay Perry / Andreas Rummel / Rongsheng Jin /
Abstract: Botulinum neurotoxins (BoNTs) are produced by Clostridium botulinum and cause the fatal disease botulism, a flaccid paralysis of the muscle. BoNTs are released together with several auxiliary ...Botulinum neurotoxins (BoNTs) are produced by Clostridium botulinum and cause the fatal disease botulism, a flaccid paralysis of the muscle. BoNTs are released together with several auxiliary proteins as progenitor toxin complexes (PTCs) to become highly potent oral poisons. Here, we report the structure of a ∼760 kDa 14-subunit large PTC of serotype A (L-PTC/A) and reveal insight into its absorption mechanism. Using a combination of X-ray crystallography, electron microscopy, and functional studies, we found that L-PTC/A consists of two structurally and functionally independent sub-complexes. A hetero-dimeric 290 kDa complex protects BoNT, while a hetero-dodecameric 470 kDa complex facilitates its absorption in the harsh environment of the gastrointestinal tract. BoNT absorption is mediated by nine glycan-binding sites on the dodecameric sub-complex that forms multivalent interactions with carbohydrate receptors on intestinal epithelial cells. We identified monosaccharides that blocked oral BoNT intoxication in mice, which suggests a new strategy for the development of preventive countermeasures for BoNTs based on carbohydrate receptor mimicry.
History
DepositionJul 12, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 30, 2013Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Advisory / Refinement description / Category: pdbx_unobs_or_zero_occ_atoms / software / Item: _software.name
Revision 1.2Feb 28, 2024Group: Advisory / Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_unobs_or_zero_occ_atoms / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HA-70
B: HA-17
C: HA-70
D: HA-17
E: HA-70
F: HA-17
G: HA-70
H: HA-17


Theoretical massNumber of molelcules
Total (without water)183,6648
Polymers183,6648
Non-polymers00
Water7,440413
1
A: HA-70
B: HA-17


Theoretical massNumber of molelcules
Total (without water)45,9162
Polymers45,9162
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1550 Å2
ΔGint-6 kcal/mol
Surface area17780 Å2
MethodPISA
2
C: HA-70
D: HA-17


Theoretical massNumber of molelcules
Total (without water)45,9162
Polymers45,9162
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1650 Å2
ΔGint-5 kcal/mol
Surface area17810 Å2
MethodPISA
3
E: HA-70
F: HA-17


Theoretical massNumber of molelcules
Total (without water)45,9162
Polymers45,9162
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1560 Å2
ΔGint-6 kcal/mol
Surface area17670 Å2
MethodPISA
4
G: HA-70
H: HA-17


Theoretical massNumber of molelcules
Total (without water)45,9162
Polymers45,9162
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1610 Å2
ΔGint-5 kcal/mol
Surface area17790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)45.810, 228.859, 78.718
Angle α, β, γ (deg.)90.00, 92.05, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
HA-70 / HA70 / Non-toxin haemagglutinin HA70


Mass: 28846.920 Da / Num. of mol.: 4 / Fragment: UNP residues 378-626
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Gene: ha70 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8KHU9
#2: Protein
HA-17 / HA-17 protein / HA17 / Ha17 protein / Non-toxin haemagglutinin HA17


Mass: 17069.195 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Gene: ha17, HA-17 / Production host: Escherichia coli (E. coli) / References: UniProt: Q45878
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 413 / 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: 2.25 Å3/Da / Density % sol: 45.22 %
Crystal growTemperature: 292 K / Method: evaporation / pH: 4.8
Details: 0.1 M sodium acetate, 12% PEG2000 MME, 0.1 M cesium chloride, pH 4.8, EVAPORATION, temperature 292.0K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 3, 2011
RadiationMonochromator: Cryo-Cooled double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. all: 62666 / Num. obs: 62548 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 4.7 % / Rmerge(I) obs: 0.125 / Net I/σ(I): 8.4
Reflection shellResolution: 2.4→2.5 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.689 / Mean I/σ(I) obs: 1.7 / % possible all: 99

-
Processing

Software
NameVersionClassification
JBluIce-EPICSdata collection
PHASESphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→45.781 Å / SU ML: 0.72 / σ(F): 1.36 / Phase error: 28.43 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2489 3176 5.08 %RANDOM
Rwork0.1968 ---
obs0.1995 62548 99.37 %-
all-62666 --
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 31.63 Å2 / ksol: 0.316 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-18.7097 Å2-0 Å2-0.5295 Å2
2---12.2326 Å2-0 Å2
3----6.4771 Å2
Refinement stepCycle: LAST / Resolution: 2.4→45.781 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12267 0 0 413 12680
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00312523
X-RAY DIFFRACTIONf_angle_d0.7617036
X-RAY DIFFRACTIONf_dihedral_angle_d14.0164588
X-RAY DIFFRACTIONf_chiral_restr0.0551907
X-RAY DIFFRACTIONf_plane_restr0.0032214
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.43590.34211330.27972559X-RAY DIFFRACTION98
2.4359-2.47390.35381140.27212557X-RAY DIFFRACTION99
2.4739-2.51450.30551660.26922539X-RAY DIFFRACTION99
2.5145-2.55780.36341390.27012600X-RAY DIFFRACTION99
2.5578-2.60430.38181210.27232531X-RAY DIFFRACTION99
2.6043-2.65440.30991170.26292618X-RAY DIFFRACTION99
2.6544-2.70860.30181300.25222613X-RAY DIFFRACTION99
2.7086-2.76750.29731450.23812525X-RAY DIFFRACTION99
2.7675-2.83180.28551540.22982575X-RAY DIFFRACTION99
2.8318-2.90270.26131310.22212614X-RAY DIFFRACTION99
2.9027-2.98110.291270.21762568X-RAY DIFFRACTION99
2.9811-3.06880.26561190.20882629X-RAY DIFFRACTION99
3.0688-3.16790.27541390.20992547X-RAY DIFFRACTION100
3.1679-3.28110.2541640.19492607X-RAY DIFFRACTION99
3.2811-3.41240.24031380.19862553X-RAY DIFFRACTION99
3.4124-3.56760.24031440.18032594X-RAY DIFFRACTION100
3.5676-3.75560.20571380.18342582X-RAY DIFFRACTION99
3.7556-3.99080.23061310.17322572X-RAY DIFFRACTION100
3.9908-4.29870.21461420.16852599X-RAY DIFFRACTION100
4.2987-4.73090.21071450.14152608X-RAY DIFFRACTION100
4.7309-5.41460.19081570.14952564X-RAY DIFFRACTION100
5.4146-6.81820.25661370.20292615X-RAY DIFFRACTION100
6.8182-45.7890.21981450.18482603X-RAY DIFFRACTION99
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)
14.40860.01990.23114.70670.08223.5944-0.17040.3371-0.4665-0.2511-0.1339-0.64890.35270.59590.22940.28010.04830.07770.32950.07140.371815.6906-58.40529.0647
22.80310.43390.60334.0130.51581.8049-0.14580.04840.089-0.0998-0.01430.2144-0.1284-0.13720.12160.1014-0.0011-0.02820.2348-0.00120.1684-2.932-43.286129.8059
33.9545-1.2153-0.47696.7629-0.80931.14670.25130.1829-0.0778-0.3053-0.0677-0.866-0.03250.1591-0.19930.4774-0.0287-0.09150.2217-0.07990.328821.7065-21.157632.2547
43.1642-0.1887-0.38223.75030.97731.77550.2286-0.0738-0.25920.1542-0.0868-0.14060.00380.18-0.1220.4467-0.0466-0.15310.18850.00150.288816.874-20.866241.3934
52.85360.93091.58885.10623.51942.7304-0.68340.1585-0.8747-0.8280.64860.07150.8339-0.76470.22051.9487-0.52670.15491.0873-0.03840.7059-16.5036-81.670752.8153
62.9115-0.87580.25778.32811.01552.1751-0.14590.4736-0.8746-1.66150.1060.17010.3531-0.29470.01291.1822-0.09610.06420.2743-0.03270.5721-12.5695-81.247663.6834
70.753-1.32941.06093.4642-1.28312.1087-0.08090.6657-0.2901-0.04520.2055-0.00030.0767-1.5835-0.01011.81860.3387-0.262-0.6757-0.53020.9162-16.5938-82.004959.1292
83.63410.3884-0.5584.87441.86225.4984-0.00740.3751-0.4999-0.6787-0.1961-0.12590.1575-0.26850.15570.5635-0.03340.08980.22470.04510.3872-14.1871-69.866670.9906
92.44971.0927-0.09362.3616-0.82732.38430.2-0.4833-0.36120.8353-0.1954-0.01140.1695-0.217-0.00140.6639-0.04930.08630.33750.07170.2731-12.7367-66.692781.3466
102.6692-1.0484-0.45073.22490.36924.5092-0.02010.2087-0.0216-0.1777-0.00710.1861-0.3665-0.39140.03160.55770.01210.06040.23380.02380.2043-11.5008-43.155958.3312
111.35140.35770.06522.00160.48614.11990.03760.06270.0220.17780.0821-0.1322-0.40070.0603-0.13380.581-0.00050.04260.1989-0.00660.1967-2.4214-42.659463.3392
124.72310.63470.44928.48247.05919.11120.0814-0.74540.3397-0.33370.0699-0.6217-0.11560.4553-0.20430.712-0.14870.0880.88960.09791.118720.41068.777887.5123
130.5236-0.4906-1.1570.46421.07952.48660.1234-0.88390.35310.7093-0.85480.0401-0.2854-0.05830.61970.9825-0.2894-0.36081.0331-0.09311.18420.82833.396196.3443
142.6811.0424-1.35955.77730.22222.46790.10580.0140.51710.2546-0.1886-0.7192-1.14320.7320.08890.55-0.1138-0.08310.29980.03840.594510.79466.965487.9204
153.23460.4207-0.28931.29271.18371.199-0.0362-0.70391.02120.8633-0.0976-0.4369-0.85640.98490.17940.7275-0.1611-0.20220.41030.06030.741210.89093.316793.0116
168.74415.0305-1.66375.64782.21924.0371-0.25910.7454-0.2442-1.13090.1615-0.4059-0.01180.38110.18350.59190.01750.05070.24290.09330.34219.7169-4.28981.9143
172.64040.3004-0.14894.9154-0.26572.9455-0.002-0.13410.34580.15670.15770.3692-0.0643-0.1389-0.10750.25130.0480.04030.250.01580.2133-4.8387-10.200792.5907
186.2085-2.0509-2.48514.12061.21313.6878-0.46950.44060.0403-0.86990.22110.71630.3722-0.49490.19250.7166-0.04-0.18510.26460.07430.4448-7.6886-10.556484.9579
193.7167-1.5762-1.1392.430.12882.8508-0.032-0.03460.28360.25480.36640.7385-0.243-0.508-0.18170.05410.05020.12010.30840.07210.4807-8.8564-8.644993.4054
203.99831.6836-0.73043.9206-2.13783.30160.0372-0.362-0.01970.4507-0.059-0.54710.03890.37760.01790.50760.09250.02370.3235-0.03950.141516.9832-32.374986.4187
213.14811.23741.03751.26550.43166.2365-0.16680.2837-0.4118-0.40420.3492-0.38860.4180.7845-0.11180.66310.18920.04180.3943-0.01370.310121.7742-36.912676.6423
222.3901-0.80640.19611.75360.36511.2623-0.0211-0.10170.1024-0.0898-0.0188-0.3947-0.09940.47260.02460.53890.05110.09850.26950.0080.25215.3166-28.006578.6334
232.9209-0.44740.43942.58010.88272.4007-0.09170.03410.0321-0.808-0.12910.07350.33620.21410.10210.82440.03410.05910.15030.01170.12516.6189-33.119277.4456
242.4647-4.1021-3.28587.30875.56514.36-0.8836-0.76360.11251.20280.81160.7022-0.2708-0.76270.42371.80140.06030.03350.9177-0.07580.7007-13.212328.857264.0767
255.3035-1.3562-0.46066.26873.34083.5052-0.1352-0.99550.6831.40410.1819-0.01190.3281-0.0047-0.0181.7639-0.09050.0433-0.4811-0.31580.4495-8.367125.056557.2088
262.6373-0.47641.55562.10810.37031.605-0.5432-0.25360.76210.6025-0.11340.8574-0.273-0.18470.42041.04670.0554-0.09310.0212-0.11150.7906-10.578530.120150.0887
270.43670.0944-1.21544.6628-0.35783.5906-0.3624-0.71310.39280.57140.16080.8076-0.2265-0.9820.1121.33730.03790.1568-0.0506-0.30181.0073-13.531528.783257.6811
282.849-0.94380.36074.03850.87473.70610.10610.0367-0.13110.67060.0266-0.1493-0.0403-0.0679-0.18030.88920.0422-0.12210.23790.03620.5156-7.583816.089549.233
292.0979-0.85410.11935.4074-1.13451.28460.20760.20320.1446-1.0306-0.21121.2046-0.4525-0.2231-0.01170.79540.0168-0.23130.28840.01840.3112-13.119312.249736.9778
301.9687-0.5760.58553.008-1.82912.63-0.10830.36390.2773-1.06240.05460.1326-0.6038-0.27430.03060.9050.0365-0.19030.24690.05650.269-8.094812.815936.3422
313.14720.97530.21414.92181.33424.57220.0641-0.512-0.14920.51050.06820.06350.1869-0.2088-0.09540.5688-0.0577-0.05120.30890.0560.2294-6.2497-9.493560.8847
322.9045-0.9851-0.15961.65180.60383.13930.0006-0.2352-0.33720.17110.1516-0.04440.09650.0897-0.14360.5261-0.0762-0.10440.21390.02340.23992.8034-10.01955.7677
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 380:507)
2X-RAY DIFFRACTION2chain 'A' and (resseq 508:626)
3X-RAY DIFFRACTION3chain 'B' and (resseq 4:60)
4X-RAY DIFFRACTION4chain 'B' and (resseq 61:146)
5X-RAY DIFFRACTION5chain 'C' and (resseq 380:405)
6X-RAY DIFFRACTION6chain 'C' and (resseq 406:474)
7X-RAY DIFFRACTION7chain 'C' and (resseq 475:493)
8X-RAY DIFFRACTION8chain 'C' and (resseq 494:529)
9X-RAY DIFFRACTION9chain 'C' and (resseq 530:626)
10X-RAY DIFFRACTION10chain 'D' and (resseq 4:60)
11X-RAY DIFFRACTION11chain 'D' and (resseq 61:146)
12X-RAY DIFFRACTION12chain 'E' and (resseq 380:391)
13X-RAY DIFFRACTION13chain 'E' and (resseq 392:405)
14X-RAY DIFFRACTION14chain 'E' and (resseq 406:460)
15X-RAY DIFFRACTION15chain 'E' and (resseq 461:493)
16X-RAY DIFFRACTION16chain 'E' and (resseq 494:507)
17X-RAY DIFFRACTION17chain 'E' and (resseq 508:574)
18X-RAY DIFFRACTION18chain 'E' and (resseq 575:594)
19X-RAY DIFFRACTION19chain 'E' and (resseq 595:626)
20X-RAY DIFFRACTION20chain 'F' and (resseq 5:60)
21X-RAY DIFFRACTION21chain 'F' and (resseq 61:75)
22X-RAY DIFFRACTION22chain 'F' and (resseq 76:101)
23X-RAY DIFFRACTION23chain 'F' and (resseq 102:146)
24X-RAY DIFFRACTION24chain 'G' and (resseq 380:405)
25X-RAY DIFFRACTION25chain 'G' and (resseq 406:428)
26X-RAY DIFFRACTION26chain 'G' and (resseq 429:474)
27X-RAY DIFFRACTION27chain 'G' and (resseq 475:493)
28X-RAY DIFFRACTION28chain 'G' and (resseq 494:521)
29X-RAY DIFFRACTION29chain 'G' and (resseq 522:562)
30X-RAY DIFFRACTION30chain 'G' and (resseq 563:626)
31X-RAY DIFFRACTION31chain 'H' and (resseq 4:60)
32X-RAY DIFFRACTION32chain 'H' and (resseq 61:146)

+
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