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- PDB-6pdl: Crystal Structure of Hendra Virus Attachment G Glycoprotein in Co... -

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Basic information

Entry
Database: PDB / ID: 6pdl
TitleCrystal Structure of Hendra Virus Attachment G Glycoprotein in Complex with Receptor Ephrin-B2
Components
  • Attachment glycoprotein
  • Ephrin-B2Ephrin B2
KeywordsVIRAL PROTEIN/SIGNALING PROTEIN / attachment / glycoprotein / G protein / VIRAL PROTEIN / receptor / VIRAL PROTEIN-SIGNALING PROTEIN complex
Function / homology
Function and homology information


venous blood vessel morphogenesis / nephric duct morphogenesis / positive regulation of aorta morphogenesis / positive regulation of cardiac muscle cell differentiation / exo-alpha-sialidase activity / lymph vessel development / regulation of chemotaxis / cell migration involved in sprouting angiogenesis / regulation of postsynaptic neurotransmitter receptor internalization / adherens junction organization ...venous blood vessel morphogenesis / nephric duct morphogenesis / positive regulation of aorta morphogenesis / positive regulation of cardiac muscle cell differentiation / exo-alpha-sialidase activity / lymph vessel development / regulation of chemotaxis / cell migration involved in sprouting angiogenesis / regulation of postsynaptic neurotransmitter receptor internalization / adherens junction organization / EPH-Ephrin signaling / Ephrin signaling / blood vessel morphogenesis / regulation of postsynaptic membrane neurotransmitter receptor levels / keratinocyte proliferation / EPH-ephrin mediated repulsion of cells / anatomical structure morphogenesis / ephrin receptor signaling pathway / negative regulation of keratinocyte proliferation / EPHB-mediated forward signaling / T cell costimulation / ephrin receptor binding / axon guidance / postsynaptic density membrane / animal organ morphogenesis / adherens junction / Schaffer collateral - CA1 synapse / negative regulation of neuron projection development / virus receptor activity / cell-cell signaling / host cell surface / host cell surface receptor binding / cell adhesion / symbiont entry into host cell / focal adhesion / viral envelope / glutamatergic synapse / positive regulation of cell population proliferation / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane / plasma membrane
Similarity search - Function
Ephrin-B ectodomain / Ephrin receptor-binding domain / Ephrin, conserved site / Ephrin / Ephrin / Ephrin receptor-binding (ephrin RBD) domain signature. / Ephrin receptor-binding (ephrin RBD) domain profile. / Haemagglutinin-neuraminidase / Haemagglutinin/haemagglutinin-neuraminidase, paramyxovirus / Haemagglutinin-neuraminidase ...Ephrin-B ectodomain / Ephrin receptor-binding domain / Ephrin, conserved site / Ephrin / Ephrin / Ephrin receptor-binding (ephrin RBD) domain signature. / Ephrin receptor-binding (ephrin RBD) domain profile. / Haemagglutinin-neuraminidase / Haemagglutinin/haemagglutinin-neuraminidase, paramyxovirus / Haemagglutinin-neuraminidase / Neuraminidase - #10 / Sialidase superfamily / 6 Propeller / Neuraminidase / Cupredoxins - blue copper proteins / Cupredoxin / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Glycoprotein / Glycoprotein G / Ephrin-B2
Similarity search - Component
Biological speciesHendra henipavirus
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsXu, K. / Nikolov, D.B.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)NS38486 United States
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)AI057168 United States
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)AI054715 United States
Citation
Journal: PLoS ONE / Year: 2012
Title: New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2.
Authors: Xu, K. / Chan, Y.P. / Rajashankar, K.R. / Khetawat, D. / Yan, L. / Kolev, M.V. / Broder, C.C. / Nikolov, D.B.
#1: Journal: Glycobiology / Year: 2012
Title: Site occupancy and glycan compositional analysis of two soluble recombinant forms of the attachment glycoprotein of Hendra virus.
Authors: Colgrave, M.L. / Snelling, H.J. / Shiell, B.J. / Feng, Y.R. / Chan, Y.P. / Bossart, K.N. / Xu, K. / Nikolov, D.B. / Broder, C.C. / Michalski, W.P.
History
DepositionJun 19, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 27, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_chiral / pdbx_validate_close_contact / pdbx_validate_symm_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _database_PDB_caveat.text / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _pdbx_validate_symm_contact.auth_asym_id_2 / _pdbx_validate_symm_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Attachment glycoprotein
B: Ephrin-B2
C: Attachment glycoprotein
D: Ephrin-B2
E: Attachment glycoprotein
F: Ephrin-B2
G: Attachment glycoprotein
H: Ephrin-B2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)273,22133
Polymers262,1388
Non-polymers11,08325
Water7,656425
1
A: Attachment glycoprotein
B: Ephrin-B2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,2508
Polymers65,5342
Non-polymers2,7166
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5600 Å2
ΔGint33 kcal/mol
Surface area24800 Å2
MethodPISA
2
C: Attachment glycoprotein
D: Ephrin-B2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,2508
Polymers65,5342
Non-polymers2,7166
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5520 Å2
ΔGint37 kcal/mol
Surface area24780 Å2
MethodPISA
3
E: Attachment glycoprotein
F: Ephrin-B2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,0888
Polymers65,5342
Non-polymers2,5536
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5380 Å2
ΔGint32 kcal/mol
Surface area24600 Å2
MethodPISA
4
G: Attachment glycoprotein
H: Ephrin-B2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,6339
Polymers65,5342
Non-polymers3,0997
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5920 Å2
ΔGint43 kcal/mol
Surface area24940 Å2
MethodPISA
Unit cell
Length a, b, c (Å)75.764, 94.642, 102.522
Angle α, β, γ (deg.)112.860, 97.440, 97.560
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 177 through 4172 or resid 4812 through 5292))
21(chain C and (resid 177 through 4172 or resid 4812 through 5292))
31(chain E and (resid 177 through 4172 or resid 4811 through 5291))
41(chain G and (resid 177 through 4172 or resid 4811 through 5291))
12chain B
22(chain D and (resid 27 through 65 or resid 72 through 1391))
32chain F
42(chain H and (resid 27 through 65 or resid 72 through 1391))

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 177 through 4172 or resid 4812 through 5292))A177 - 4172
121(chain A and (resid 177 through 4172 or resid 4812 through 5292))A4812 - 5292
211(chain C and (resid 177 through 4172 or resid 4812 through 5292))C177 - 4172
221(chain C and (resid 177 through 4172 or resid 4812 through 5292))C4812 - 5292
311(chain E and (resid 177 through 4172 or resid 4811 through 5291))E177 - 4172
321(chain E and (resid 177 through 4172 or resid 4811 through 5291))E4811 - 5291
411(chain G and (resid 177 through 4172 or resid 4811 through 5291))G177 - 4172
421(chain G and (resid 177 through 4172 or resid 4811 through 5291))G4811 - 5291
112chain BB27 - 1391
212(chain D and (resid 27 through 65 or resid 72 through 1391))D27 - 65
222(chain D and (resid 27 through 65 or resid 72 through 1391))D72 - 1391
312chain FF27 - 1391
412(chain H and (resid 27 through 65 or resid 72 through 1391))H27 - 65
422(chain H and (resid 27 through 65 or resid 72 through 1391))H72 - 1391

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 8 molecules ACEGBDFH

#1: Protein
Attachment glycoprotein / Glycoprotein


Mass: 49431.121 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hendra henipavirus
Production host: Insect cell expression vector pTIE1 (others)
References: UniProt: F4YH71, UniProt: O89343*PLUS
#2: Protein
Ephrin-B2 / Ephrin B2 / EPH-related receptor tyrosine kinase ligand 5 / LERK-5 / HTK ligand / HTK-L


Mass: 16103.368 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EFNB2, EPLG5, HTKL, LERK5
Production host: Insect cell expression vector pTIE1 (others)
References: UniProt: P52799

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Sugars , 6 types, 25 molecules

#3: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#4: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1203.105 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-3][LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5][a1122h-1b_1-5][a1122h-1a_1-5]/1-2-1-3-4-4-2/a3-b1_a4-c1_a6-g1_c4-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(3+1)][b-L-Fucp]{}[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2- ...beta-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1203.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3[DManpa1-6]DManpa1-4DGlcpNAcb1-4[LFucpa1-3][LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5][a1122h-1a_1-5][a1122h-1b_1-5]/1-2-1-3-4-3-2/a3-b1_a4-c1_a6-g1_c4-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(3+1)][a-L-Fucp]{}[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#7: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 878.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-3][LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5][a1122h-1b_1-5]/1-2-1-3-2/a3-b1_a4-c1_a6-e1_c4-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(3+1)][a-L-Fucp]{}[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#8: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 13
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 1 types, 425 molecules

#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 425 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 51.02 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / Details: 27.5% PEG2000MME and 0.09% MG7

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 10, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.7→40 Å / Num. obs: 65721 / % possible obs: 93.8 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.076 / Χ2: 1.202 / Net I/σ(I): 10.1 / Num. measured all: 241203
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsΧ2Diffraction-ID% possible all
2.7-2.82.90.20751030.598173.3
2.8-2.913.20.17958550.623183.3
2.91-3.043.50.16463490.725190.5
3.04-3.23.70.13467080.838195.8
3.2-3.43.90.1169171.002198.4
3.4-3.663.90.08869531.198199
3.66-4.033.90.0769221.374199.1
4.03-4.623.90.05769451.637199.3
4.62-5.813.80.05169851.625199.4
5.81-403.80.04669841.763199.4

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIX1.15.2_3472refinement
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3D11

3d11


Resolution: 2.7→37.561 Å / SU ML: 0.3 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 24.26
RfactorNum. reflection% reflection
Rfree0.2269 3222 4.91 %
Rwork0.1719 --
obs0.1746 65675 93.45 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 116.71 Å2 / Biso mean: 35.5952 Å2 / Biso min: 2.74 Å2
Refinement stepCycle: final / Resolution: 2.7→37.561 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17552 0 730 425 18707
Biso mean--59.32 31.5 -
Num. residues----2222
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5228X-RAY DIFFRACTION7.046TORSIONAL
12C5228X-RAY DIFFRACTION7.046TORSIONAL
13E5228X-RAY DIFFRACTION7.046TORSIONAL
14G5228X-RAY DIFFRACTION7.046TORSIONAL
21B1592X-RAY DIFFRACTION7.046TORSIONAL
22D1592X-RAY DIFFRACTION7.046TORSIONAL
23F1592X-RAY DIFFRACTION7.046TORSIONAL
24H1592X-RAY DIFFRACTION7.046TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 23

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.7-2.73660.30671070.22561834194165
2.7366-2.77930.28181150.21562211232675
2.7793-2.82490.29261320.20792286241880
2.8249-2.87360.29081220.21072425254783
2.8736-2.92580.3341530.20662515266887
2.9258-2.98210.28291250.20142596272190
2.9821-3.04290.27681330.19932726285992
3.0429-3.10910.25871490.20192719286895
3.1091-3.18130.27581540.19822800295497
3.1813-3.26090.27131430.19382856299998
3.2609-3.3490.24141380.1842877301598
3.349-3.44750.25631440.17352899304399
3.4475-3.55860.20621240.16882880300499
3.5586-3.68570.21181380.16042878301699
3.6857-3.83320.18881350.16432898303399
3.8332-4.00740.20361550.1572889304499
4.0074-4.21840.18971430.14982915305899
4.2184-4.48230.18821660.13472820298699
4.4823-4.82780.19411440.13132901304599
4.8278-5.31240.19011310.145829223053100
5.3124-6.07830.20541560.16612891304799
6.0783-7.64740.2081690.19062847301699
7.6474-37.56480.21841460.18912868301498

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Jul 12, 2017. Major update of PDB

Major update of PDB

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External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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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

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