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- PDB-5gaq: Cryo-EM structure of the Lysenin Pore -

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Basic information

Entry
Database: PDB / ID: 5gaq
TitleCryo-EM structure of the Lysenin Pore
ComponentsLysenin
KeywordsTOXIN / Pore forming protein / aerolysin
Function / homology
Function and homology information


other organism cell membrane / monoatomic ion transport / toxin activity / killing of cells of another organism / defense response to bacterium / extracellular region / membrane
Similarity search - Function
Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Mainly Beta
Similarity search - Domain/homology
Biological speciesEisenia fetida (common brandling worm)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsSavva, C.G. / Bokori-Brown, M. / Martin, T.G. / Titball, R.W. / Naylor, C.E. / Basak, A.K.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)MC-A021-53019 United Kingdom
Wellcome TrustWT089618MA United Kingdom
CitationJournal: Nat Commun / Year: 2016
Title: Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.
Authors: Monika Bokori-Brown / Thomas G Martin / Claire E Naylor / Ajit K Basak / Richard W Titball / Christos G Savva /
Abstract: Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small β-pore-forming toxins (β-PFTs), some members of which are pathogenic to humans and animals. ...Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small β-pore-forming toxins (β-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive and therefore the mechanism of activation and membrane insertion remains unclear. Here we determine the pore structure of lysenin by single particle cryo-EM, to 3.1 Å resolution. The nonameric assembly reveals a long β-barrel channel spanning the length of the complex that, unexpectedly, includes the two pre-insertion strands flanking the hypothetical membrane-insertion loop. Examination of other members of the aerolysin family reveals high structural preservation in this region, indicating that the membrane-insertion pathway in this family is conserved. For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre-insertion strands, allowing them to form the β-barrel of the channel.
History
DepositionJan 5, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Apr 6, 2016Provider: repository / Type: Initial release
Revision 1.1May 18, 2016Group: Database references
Revision 1.2May 25, 2016Group: Database references
Revision 1.3Jun 28, 2017Group: Database references / Category: citation / Item: _citation.title
Revision 1.4Jul 5, 2017Group: Derived calculations
Category: struct_sheet / struct_sheet_order / struct_sheet_range
Revision 1.5Jul 19, 2017Group: Derived calculations
Category: struct_sheet / struct_sheet_order / struct_sheet_range
Revision 1.6Aug 30, 2017Group: Author supporting evidence / Data collection
Category: em_imaging_optics / em_software / pdbx_audit_support
Item: _em_imaging_optics.energyfilter_name / _em_software.name / _pdbx_audit_support.funding_organization
Revision 1.7Oct 23, 2019Group: Data collection / Other / Category: atom_sites / cell
Item: _atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[2][1] ..._atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[2][1] / _atom_sites.fract_transf_matrix[2][2] / _atom_sites.fract_transf_matrix[3][2] / _atom_sites.fract_transf_matrix[3][3] / _cell.Z_PDB
Revision 1.8May 15, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_initial_refinement_model / refine / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _refine.ls_d_res_high / _refine.ls_d_res_low / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
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  • Superimposition on EM map
  • EMDB-8015
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Lysenin
B: Lysenin
C: Lysenin
D: Lysenin
E: Lysenin
F: Lysenin
G: Lysenin
H: Lysenin
I: Lysenin


Theoretical massNumber of molelcules
Total (without water)314,7959
Polymers314,7959
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_5551
MethodPISA
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18A
28I
19B
29C
110B
210D
111B
211E
112B
212F
113B
213G
114B
214H
115B
215I
116C
216D
117C
217E
118C
218F
119C
219G
120C
220H
121C
221I
122D
222E
123D
223F
124D
224G
125D
225H
126D
226I
127E
227F
128E
228G
129E
229H
130E
230I
131F
231G
132F
232H
133F
233I
134G
234H
135G
235I
136H
236I

NCS domain segments:

Component-ID: 1 / Beg auth comp-ID: GLU / Beg label comp-ID: GLU / End auth comp-ID: GLY / End label comp-ID: GLY / Refine code: 1 / Auth seq-ID: 10 - 297 / Label seq-ID: 10 - 297

Dom-IDEns-IDAuth asym-IDLabel asym-ID
11AA
21BB
12AA
22CC
13AA
23DD
14AA
24EE
15AA
25FF
16AA
26GG
17AA
27HH
18AA
28II
19BB
29CC
110BB
210DD
111BB
211EE
112BB
212FF
113BB
213GG
114BB
214HH
115BB
215II
116CC
216DD
117CC
217EE
118CC
218FF
119CC
219GG
120CC
220HH
121CC
221II
122DD
222EE
123DD
223FF
124DD
224GG
125DD
225HH
126DD
226II
127EE
227FF
128EE
228GG
129EE
229HH
130EE
230II
131FF
231GG
132FF
232HH
133FF
233II
134GG
234HH
135GG
235II
136HH
236II

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.766015, -0.642823, -1.5E-5), (0.642823, 0.766015, -6.0E-6), (1.6E-5, -5.0E-6, 1)58.596279, -26.55695, 0.00034
3given(1), (1), (1)
4given(0.173652, -0.984807, -6.0E-6), (0.984807, 0.173652, -1.4E-5), (1.5E-5, -3.0E-6, 1)120.54493, -9.24101, -0.00081
5given(1), (1), (1)
6given(-0.500007, -0.866021, -6.0E-6), (0.866021, -0.500007, -6.0E-6), (2.0E-6, -8.0E-6, 1)156.874313, 43.849121, 0.00024
7given(1), (1), (1)
8given(-0.939698, -0.342005, -1.0E-6), (0.342005, -0.939698, 4.0E-6), (-2.0E-6, 3.0E-6, 1)150.578247, 107.869347, -0.00029
9given(1), (1), (1)
10given(-0.93969, 0.342027), (-0.342027, -0.93969, 1.5E-5), (6.0E-6, 1.4E-5, 1)104.603523, 152.863831, -0.00117
11given(1), (1), (1)
12given(-0.5, 0.866025, -2.5E-5), (-0.866025, -0.5, 6.0E-6), (-8.0E-6, 2.5E-5, 1)40.464989, 157.781006, -0.00053
13given(1), (1), (1)
14given(0.173634, 0.98481, -5.0E-6), (-0.98481, 0.173634, -1.8E-5), (-1.7E-5, 8.0E-6, 1)-11.83016, 120.320953, 0.00019
15given(1), (1), (1)
16given(0.766031, 0.642804, -1.2E-5), (-0.642804, 0.766031, -2.9E-5), (-9.0E-6, 3.0E-5, 1)-27.81168, 58.009949, -0.00137
17given(1), (1), (1)
18given(0.766077, -0.642749, 2.0E-6), (0.642749, 0.766077, -1.2E-5), (6.0E-6, 1.1E-5, 1)58.584671, -26.557739, -0.00222
19given(1), (1), (1)
20given(0.173685, -0.984801, 8.0E-6), (0.984801, 0.173685, -6.0E-6), (4.0E-6, 8.0E-6, 1)120.541061, -9.24328, -0.00207
21given(1), (1), (1)
22given(-0.499974, -0.866041, 1.7E-5), (0.866041, -0.499974, -1.0E-6), (1.0E-5, 1.4E-5, 1)156.871857, 43.844421, -0.00291
23given(1), (1), (1)
24given(-0.93968, -0.342056, 2.6E-5), (0.342056, -0.93968, 6.0E-6), (2.2E-5, 1.5E-5, 1)150.578003, 107.864471, -0.00337
25given(1), (1), (1)
26given(-0.939708, 0.341977), (-0.341977, -0.939708, 1.6E-5), (5.0E-6, 1.5E-5, 1)104.607819, 152.860825, -0.00178
27given(1), (1), (1)
28given(-0.500052, 0.865995), (-0.865995, -0.500052, -1.5E-5), (-1.3E-5, -8.0E-6, 1)40.468761, 157.782364, -2.0E-5
29given(1), (1), (1)
30given(0.173582, 0.984819, -1.2E-5), (-0.98482, 0.173582, -1.9E-5), (-1.7E-5, 1.5E-5, 1)-11.82824, 120.324509, -0.00094
31given(1), (1), (1)
32given(0.766036, -0.642797, 8.0E-6), (0.642797, 0.766036, 1.0E-6), (-7.0E-6, 4.0E-6, 1)58.592209, -26.55821, 9.0E-5
33given(1), (1), (1)
34given(0.173629, -0.984811, 1.8E-5), (0.984811, 0.173629, -1.0E-6), (-2.0E-6, 1.8E-5, 1)120.546463, -9.24054, -0.00131
35given(1), (1), (1)
36given(-0.50001, -0.866019, 3.0E-5), (0.866019, -0.50001, -1.0E-6), (1.6E-5, 2.5E-5, 1)156.873718, 43.849091, -0.00256
37given(1), (1), (1)
38given(-0.939694, -0.342016, 1.6E-5), (0.342016, -0.939694, 2.3E-5), (7.0E-6, 2.7E-5, 1)150.578384, 107.867043, -0.00162
39given(1), (1), (1)
40given(-0.939696, 0.342011, -4.0E-6), (-0.342011, -0.939696, -1.0E-6), (-4.0E-6, 1)104.606277, 152.862656, -7.0E-5
41given(1), (1), (1)
42given(-0.500015, 0.866017, -1.6E-5), (-0.866017, -0.500015, 4.0E-6), (-4.0E-6, 1.5E-5, 1)40.466751, 157.780914, -0.00065
43given(1), (1), (1)
44given(0.76604, -0.642793, 6.0E-6), (0.642793, 0.76604, -9.0E-6), (1.0E-6, 1.1E-5, 1)58.590961, -26.558041, -0.00088
45given(1), (1), (1)
46given(0.173649, -0.984808, 1.5E-5), (0.984808, 0.173649, -1.6E-5), (1.3E-5, 1.8E-5, 1)120.54483, -9.24052, -0.00176
47given(1), (1), (1)
48given(-0.499993, -0.86603, 2.0E-5), (0.86603, -0.499993, 1.1E-5), (2.3E-5, 1)156.87294, 43.846191, -0.00078
49given(1), (1), (1)
50given(-0.939685, -0.342041, -1.1E-5), (0.342041, -0.939685, 6.0E-6), (-1.2E-5, 2.0E-6, 1)150.579681, 107.865211, 0.00047
51given(1), (1), (1)
52given(-0.939703, 0.341992, -1.7E-5), (-0.341992, -0.939703, 1.7E-5), (-1.0E-5, 2.2E-5, 1)104.60791, 152.861481, -0.00062
53given(1), (1), (1)
54given(0.76605, -0.642781, 2.0E-6), (0.642781, 0.76605, -1.1E-5), (5.0E-6, 1.0E-5, 1)58.590721, -26.557619, -0.00066
55given(1), (1), (1)
56given(0.173664, -0.984805, 2.3E-5), (0.984805, 0.173664, 7.0E-6), (-1.0E-5, 2.2E-5, 1)120.543266, -9.24257, 8.0E-5
57given(1), (1), (1)
58given(-0.499974, -0.86604, -4.0E-6), (0.86604, -0.499974, 2.2E-5), (-2.1E-5, 8.0E-6, 1)156.873383, 43.843811, 0.00072
59given(1), (1), (1)
60given(-0.93968, -0.342055, -1.0E-6), (0.342055, -0.93968, 3.4E-5), (-1.2E-5, 3.2E-5, 1)150.580475, 107.863083, -0.00106
61given(1), (1), (1)
62given(0.76605, -0.642782, 2.7E-5), (0.642782, 0.76605), (-2.1E-5, 1.8E-5, 1)58.58852, -26.55776, 0.00069
63given(1), (1), (1)
64given(0.173669, -0.984804, 1.7E-5), (0.984804, 0.17367, 2.9E-5), (-3.2E-5, 1.2E-5, 1)120.54213, -9.24329, 0.00082
65given(1), (1), (1)
66given(-0.499975, -0.86604, 2.7E-5), (0.86604, -0.499975, 3.7E-5), (-1.9E-5, 4.2E-5, 1)156.871857, 43.843609, -0.00169
67given(1), (1), (1)
68given(0.766053, -0.642777, 1.1E-5), (0.642777, 0.766053, 2.9E-5), (-2.7E-5, -1.5E-5, 1)58.588951, -26.558889, 0.00183
69given(1), (1), (1)
70given(0.173669, -0.984804, 2.3E-5), (0.984804, 0.173669, 2.9E-5), (-3.2E-5, 1.8E-5, 1)120.542603, -9.24379, 0.00032
71given(1), (1), (1)
72given(0.766049, -0.642782, 9.0E-6), (0.642782, 0.766049, -9.0E-6), (-2.0E-6, 1.2E-5, 1)58.58955, -26.55809, -0.00034

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Components

#1: Protein
Lysenin / efL1


Mass: 34977.246 Da / Num. of mol.: 9
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Eisenia fetida (common brandling worm) / Plasmid: pHis-Parallel 1 / Production host: Escherichia coli (E. coli) / Variant (production host): Rosetta 2 / References: UniProt: O18423

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Membrane-inserted form of the nonameric pore forming protein Lysenin
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.315 MDa / Experimental value: NO
Source (natural)Organism: Eisenia foetida (common brandling worm)
Source (recombinant)Organism: Escherichia coli (E. coli) / Plasmid: pHis-Parallel 1
Buffer solutionpH: 7.4
Buffer component
IDConc.NameBuffer-ID
1150 mMSodium Chloride1
250 mMTris1
3500 mMImidazole1
40.02 %Dodecyl Maltoside1
SpecimenConc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: Grids were glow-discharged prior to deposition of Graphene-oxide.No further treatment was performed after graphene-oxide deposition.
Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationCryogen name: ETHANE / Humidity: 90 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Details: Direct alignments: Beam tilt pivot points, Beam shift, Comma Free. C2 aperture centering, C2 lens astigmatism correction. Objective aperture centering and objective lens astigmatism ...Details: Direct alignments: Beam tilt pivot points, Beam shift, Comma Free. C2 aperture centering, C2 lens astigmatism correction. Objective aperture centering and objective lens astigmatism correction. Energy filter Tuning and occasional ZLP centering.
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 81000 X / Calibrated magnification: 34965 X / Nominal defocus max: 4500 nm / Nominal defocus min: 1000 nm / Calibrated defocus min: 700 nm / Calibrated defocus max: 4700 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: BASIC
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 85 K / Temperature (min): 85 K
Image recordingAverage exposure time: 18 sec. / Electron dose: 47 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 280
EM imaging opticsEnergyfilter name: GIF Quantum / Energyfilter upper: 20 eV / Energyfilter lower: 0 eV
Image scansSampling size: 5 µm / Width: 3710 / Height: 3710 / Movie frames/image: 20 / Used frames/image: 0-20

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Processing

SoftwareName: REFMAC / Version: 5.8.0124 / Classification: refinement
EM software
IDNameVersionCategoryDetails
1RELION1.4particle selection
2Titan User Interfaceimage acquisitionManual collection using FEI Low Dose software in EFTEM mode
4GctfCTF correctionThis is a new GPU based software that was just published recently. http://www.ncbi.nlm.nih.gov/pubmed/26592709
7Coot0.8.2model fitting
9RELION1.4initial Euler assignment
10RELION1.4final Euler assignment
11RELION1.4classification
12RELION1.43D reconstruction
13REFMAC5model refinement
Image processingDetails: Super-resolution images were binned by 2 for further processing.
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 53779
Details: Autopicking performed with RELION after manually picking 1000 particles to create 2D Classes (references) for autopicking.
SymmetryPoint symmetry: C9 (9 fold cyclic)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 29329 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL / Space: REAL
Details: Initial docking of C-terminal region of lysenin monomer to EM map was performed using UCSF Chimera followed by model N-terminal extension in COOT.
Atomic model buildingPDB-ID: 3ZXD

3zxd


Pdb chain-ID: A / Accession code: 3ZXD / Pdb chain residue range: 150-297 / Source name: PDB / Type: experimental model
RefinementResolution: 3.1→3.1 Å / Cor.coef. Fo:Fc: 0.975 / SU B: 20.023 / SU ML: 0.34 / ESU R: 0.545
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.3054 --
obs0.3054 145882 100 %
Solvent computationSolvent model: PARAMETERS FOR MASK CACLULATION
Displacement parametersBiso mean: 294.145 Å2
Baniso -1Baniso -2Baniso -3
1--0.62 Å2-0.03 Å20.01 Å2
2---0.73 Å20.02 Å2
3---1.36 Å2
Refinement stepCycle: 1 / Total: 20574
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0050.01921024
ELECTRON MICROSCOPYr_bond_other_d0.0020.0219611
ELECTRON MICROSCOPYr_angle_refined_deg1.0631.93528485
ELECTRON MICROSCOPYr_angle_other_deg0.792345207
ELECTRON MICROSCOPYr_dihedral_angle_1_deg5.56452583
ELECTRON MICROSCOPYr_dihedral_angle_2_deg27.00224945
ELECTRON MICROSCOPYr_dihedral_angle_3_deg11.634153645
ELECTRON MICROSCOPYr_dihedral_angle_4_deg8.95415117
ELECTRON MICROSCOPYr_chiral_restr0.0670.23168
ELECTRON MICROSCOPYr_gen_planes_refined0.0030.0223598
ELECTRON MICROSCOPYr_gen_planes_other0.0010.024833
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it9.12428.66210359
ELECTRON MICROSCOPYr_mcbond_other9.12428.66110358
ELECTRON MICROSCOPYr_mcangle_it13.25243.08812933
ELECTRON MICROSCOPYr_mcangle_other13.25243.08812934
ELECTRON MICROSCOPYr_scbond_it11.68130.510665
ELECTRON MICROSCOPYr_scbond_other11.6830.50110666
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other19.59245.04715553
ELECTRON MICROSCOPYr_long_range_B_refined25.05523446
ELECTRON MICROSCOPYr_long_range_B_other25.05523446
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Number: 2632 / Refine-ID: ELECTRON MICROSCOPY

Ens-IDAuth asym-IDTypeRms dev position (Å)Weight position
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT POSITIONAL00.14
1ATIGHT THERMAL0.591.41
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT POSITIONAL00.14
2ATIGHT THERMAL0.651.41
3ATIGHT POSITIONAL00.14
3ATIGHT POSITIONAL00.14
3ATIGHT POSITIONAL00.14
3ATIGHT POSITIONAL00.14
3ATIGHT POSITIONAL00.14
3ATIGHT POSITIONAL00.14
3ATIGHT POSITIONAL00.14
3ATIGHT THERMAL0.631.41
4ATIGHT THERMAL0.611.41
5ATIGHT THERMAL0.591.41
6ATIGHT THERMAL0.581.41
7ATIGHT THERMAL0.611.41
8ATIGHT THERMAL0.621.41
9BTIGHT THERMAL0.61.41
10BTIGHT THERMAL0.621.41
11BTIGHT THERMAL0.611.41
12BTIGHT THERMAL0.551.41
13BTIGHT THERMAL0.581.41
14BTIGHT THERMAL0.591.41
15BTIGHT THERMAL0.641.41
16CTIGHT THERMAL0.581.41
17CTIGHT THERMAL0.611.41
18CTIGHT THERMAL0.61.41
19CTIGHT THERMAL0.591.41
20CTIGHT THERMAL0.591.41
21CTIGHT THERMAL0.591.41
22DTIGHT THERMAL0.611.41
23DTIGHT THERMAL0.581.41
24DTIGHT THERMAL0.581.41
25DTIGHT THERMAL0.611.41
26DTIGHT THERMAL0.591.41
27ETIGHT THERMAL0.591.41
28ETIGHT THERMAL0.621.41
29ETIGHT THERMAL0.611.41
30ETIGHT THERMAL0.641.41
31FTIGHT THERMAL0.61.41
32FTIGHT THERMAL0.581.41
33FTIGHT THERMAL0.61.41
34GTIGHT THERMAL0.561.41
35GTIGHT THERMAL0.581.41
36HTIGHT THERMAL0.581.41
LS refinement shellResolution: 3.14→3.222 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rwork3.041 10745 -
Rfree-0 -
obs--100 %

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