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- PDB-3d12: Crystal Structures of Nipah Virus G Attachment Glycoprotein in Co... -

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Basic information

Entry
Database: PDB / ID: 3d12
TitleCrystal Structures of Nipah Virus G Attachment Glycoprotein in Complex with its Receptor Ephrin-B3
Components
  • Ephrin-B3
  • Hemagglutinin-neuraminidase
KeywordsHYDROLASE/MEMBRANE PROTEIN / Beta propeller / Protein-Receptor complex / Envelope protein / Glycoprotein / Hemagglutinin / Hydrolase / Membrane / Signal-anchor / Transmembrane / Virion / Developmental protein / Differentiation / Neurogenesis / HYDROLASE-MEMBRANE PROTEIN COMPLEX
Function / homology
Function and homology information


axon choice point recognition / trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission / Ephrin signaling / : / EPH-Ephrin signaling / : / EPH-ephrin mediated repulsion of cells / EPHB-mediated forward signaling / membrane fusion involved in viral entry into host cell / negative regulation of axonogenesis ...axon choice point recognition / trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission / Ephrin signaling / : / EPH-Ephrin signaling / : / EPH-ephrin mediated repulsion of cells / EPHB-mediated forward signaling / membrane fusion involved in viral entry into host cell / negative regulation of axonogenesis / exo-alpha-sialidase activity / adult walking behavior / ephrin receptor signaling pathway / T cell costimulation / hippocampal mossy fiber to CA3 synapse / ephrin receptor binding / axon guidance / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / viral envelope / glutamatergic synapse / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane / identical protein binding / plasma membrane
Similarity search - Function
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 ...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
Ephrin-B3 / Glycoprotein G
Similarity search - Component
Biological speciesNipah virus
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.005 Å
AuthorsXu, K. / Rajashankar, K.R. / Chan, Y.P. / Himanen, P. / Broder, C.C. / Nikolov, D.B.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2008
Title: Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3.
Authors: Xu, K. / Rajashankar, K.R. / Chan, Y.P. / Himanen, J.P. / Broder, C.C. / Nikolov, D.B.
History
DepositionMay 2, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 19, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Feb 12, 2014Group: Atomic model
Revision 1.3Oct 25, 2017Group: Refinement description / Category: software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / 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 / struct_asym / struct_conn / struct_ref_seq_dif / 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 / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_atom_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_chiral.details / _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_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hemagglutinin-neuraminidase
B: Ephrin-B3
D: Hemagglutinin-neuraminidase
E: Ephrin-B3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,76034
Polymers128,0634
Non-polymers7,69630
Water2,018112
1
A: Hemagglutinin-neuraminidase
B: Ephrin-B3
hetero molecules

D: Hemagglutinin-neuraminidase
E: Ephrin-B3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,76034
Polymers128,0634
Non-polymers7,69630
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_544y,x-1,-z-1/31
Buried area18000 Å2
ΔGint-241 kcal/mol
Surface area47460 Å2
MethodPISA
2
D: Hemagglutinin-neuraminidase
E: Ephrin-B3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,88017
Polymers64,0322
Non-polymers3,84815
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7840 Å2
ΔGint-123 kcal/mol
Surface area25200 Å2
MethodPISA
3
A: Hemagglutinin-neuraminidase
B: Ephrin-B3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,88017
Polymers64,0322
Non-polymers3,84815
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7600 Å2
ΔGint-98 kcal/mol
Surface area24830 Å2
MethodPISA
Unit cell
Length a, b, c (Å)189.492, 189.492, 277.052
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522

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Components

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Protein , 2 types, 4 molecules ADBE

#1: Protein Hemagglutinin-neuraminidase /


Mass: 47966.520 Da / Num. of mol.: 2 / Fragment: UNP residues 176-602
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Nipah virus / Gene: HN / Plasmid: pAcGP67 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Hi5 / References: UniProt: Q9IH62, exo-alpha-sialidase
#2: Protein Ephrin-B3


Mass: 16065.159 Da / Num. of mol.: 2 / Fragment: UNP residues 29-169
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Efnb3 / Plasmid: pAcGP67 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O35393

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Sugars , 6 types, 8 molecules

#3: Polysaccharide beta-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...beta-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-2-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#4: Polysaccharide beta-D-glucopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]beta-D-gulopyranose-(1-4)-2-acetamido-2- ...beta-D-glucopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]beta-D-gulopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[beta-D-glucopyranose-(1-3)][alpha-D-glucopyranose-(1-6)]2-acetamido-2-deoxy-alpha-D-idopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpb1-3[DGlcpa1-6]DGulpb1-4DGalpNAcb1-4[DGlcpb1-3][DGlcpa1-6]DIdopNAca1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/5,7,6/[a1212h-1a_1-5_2*NCC/3=O][a2122h-1b_1-5][a2112h-1b_1-5_2*NCC/3=O][a2212h-1b_1-5][a2122h-1a_1-5]/1-2-3-4-2-5-5/a3-b1_a4-c1_a6-g1_c4-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-IdopNAc]{[(3+1)][a-L-Idop]{}[(4+1)][b-L-GalpNAc]{[(4+1)][a-D-Gulp]{[(3+1)][b-D-Glcp]{}[(6+1)][a-L-Glcp]{}}}[(6+1)][a-L-Glcp]{}}LINUCSPDB-CARE
#5: 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.: 2
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)][a-D-GlcpNAc]{}}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-glucopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...beta-D-glucopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpb1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a2122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-4/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Glcp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#7: Polysaccharide beta-D-glucopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]beta-D-gulopyranose-(1-4)-2-acetamido-2- ...beta-D-glucopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]beta-D-gulopyranose-(1-4)-2-acetamido-2-deoxy-alpha-L-glucopyranose-(1-4)-[beta-D-glucopyranose-(1-3)][alpha-L-galactopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-gulopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpb1-3[DGlcpa1-6]DGulpb1-4LGlcpNAca1-4[DGlcpb1-3][LGalpa1-6]DGulpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/6,7,6/[a2212h-1b_1-5_2*NCC/3=O][a2122h-1b_1-5][a1211h-1a_1-5_2*NCC/3=O][a2212h-1b_1-5][a2122h-1a_1-5][a1221h-1a_1-5]/1-2-3-4-2-5-6/a3-b1_a4-c1_a6-g1_c4-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GulpNAc]{[(3+1)][a-L-Idop]{}[(4+1)][b-L-GlcpNAc]{[(4+1)][a-D-Gulp]{[(3+1)][b-D-Glcp]{}[(6+1)][a-L-Glcp]{}}}[(6+1)][a-L-Glcp]{}}LINUCSPDB-CARE
#8: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
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 , 2 types, 134 molecules

#9: Chemical...
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 22 / Source method: obtained synthetically / Formula: SO4
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 112 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsTHE STEREOCHEMISTRIES OF BGC 1466D AND GLC 1465D LIGANDS ARE AMBIGUOUS

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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: 5.61 Å3/Da / Density % sol: 78.06 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 1.5M Li2SO4 and 100mM Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9192 Å
DetectorDate: Oct 30, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9192 Å / Relative weight: 1
ReflectionResolution: 3→40 Å / Num. obs: 58204 / % possible obs: 98.9 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.086 / Χ2: 1.196 / Net I/σ(I): 8.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
3-3.113.50.46956390.793198.1
3.11-3.233.70.33257000.826198.8
3.23-3.383.70.24957410.894198.8
3.38-3.563.70.17857311.028199
3.56-3.783.70.1357721.254199
3.78-4.073.60.10557711.405199.1
4.07-4.483.60.07858271.713199.2
4.48-5.133.60.06758621.763199.2
5.13-6.463.50.05759471.332199.4
6.46-403.40.02962140.921198.6

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIXrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data reduction
HKL-2000data scaling
PHASESphasing
RefinementResolution: 3.005→39.337 Å / FOM work R set: 0.795 / Stereochemistry target values: ml
RfactorNum. reflection% reflection
Rfree0.265 2676 4.97 %
Rwork0.221 --
obs-53799 91.31 %
Solvent computationBsol: 29.077 Å2 / ksol: 0.323 e/Å3
Displacement parametersBiso max: 132.01 Å2 / Biso mean: 69.13 Å2 / Biso min: 35.21 Å2
Baniso -1Baniso -2Baniso -3
1-9.962 Å20 Å2-0 Å2
2--9.962 Å20 Å2
3----19.924 Å2
Refinement stepCycle: LAST / Resolution: 3.005→39.337 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9004 0 482 112 9598
Refine LS restraints
Refine-IDTypeDev idealWeight
X-RAY DIFFRACTIONf_angle_d0.9271
X-RAY DIFFRACTIONf_bond_d0.0071
X-RAY DIFFRACTIONf_chiral_restr0.0711
X-RAY DIFFRACTIONf_dihedral_angle_d15.3661
X-RAY DIFFRACTIONf_plane_restr0.0031
X-RAY DIFFRACTIONf_nbd_refined4.0961
LS refinement shell
Resolution (Å)Rfactor RworkNum. reflection RworkRefine-IDTotal num. of bins used% reflection obs (%)
3.005-3.0150.331290X-RAY DIFFRACTION10253
3.015-3.0250.326432X-RAY DIFFRACTION10275
3.025-3.0350.33396X-RAY DIFFRACTION10274
3.035-3.0450.338450X-RAY DIFFRACTION10276
3.045-3.0560.327443X-RAY DIFFRACTION10278
3.056-3.0660.306424X-RAY DIFFRACTION10277
3.066-3.0770.308431X-RAY DIFFRACTION10277
3.077-3.0880.303466X-RAY DIFFRACTION10282
3.088-3.0990.318451X-RAY DIFFRACTION10277
3.099-3.110.28445X-RAY DIFFRACTION10278
3.11-3.1210.316418X-RAY DIFFRACTION10277
3.121-3.1330.28454X-RAY DIFFRACTION10280
3.133-3.1450.307466X-RAY DIFFRACTION10283
3.145-3.1560.301490X-RAY DIFFRACTION10282
3.156-3.1680.284448X-RAY DIFFRACTION10281
3.168-3.1810.283432X-RAY DIFFRACTION10276
3.181-3.1930.291469X-RAY DIFFRACTION10281
3.193-3.2060.286445X-RAY DIFFRACTION10280
3.206-3.2180.306482X-RAY DIFFRACTION10283
3.218-3.2310.269465X-RAY DIFFRACTION10284
3.231-3.2450.275477X-RAY DIFFRACTION10285
3.245-3.2580.273488X-RAY DIFFRACTION10282
3.258-3.2720.294462X-RAY DIFFRACTION10283
3.272-3.2860.268455X-RAY DIFFRACTION10281
3.286-3.30.267479X-RAY DIFFRACTION10284
3.3-3.3140.282480X-RAY DIFFRACTION10283
3.314-3.3290.278492X-RAY DIFFRACTION10284
3.329-3.3440.28472X-RAY DIFFRACTION10288
3.344-3.3590.283488X-RAY DIFFRACTION10284
3.359-3.3750.255470X-RAY DIFFRACTION10283
3.375-3.390.263502X-RAY DIFFRACTION10286
3.39-3.4060.257458X-RAY DIFFRACTION10283
3.406-3.4230.272484X-RAY DIFFRACTION10286
3.423-3.440.284479X-RAY DIFFRACTION10284
3.44-3.4570.261492X-RAY DIFFRACTION10284
3.457-3.4740.253466X-RAY DIFFRACTION10285
3.474-3.4910.244518X-RAY DIFFRACTION10286
3.491-3.510.258468X-RAY DIFFRACTION10284
3.51-3.5280.25503X-RAY DIFFRACTION10287
3.528-3.5470.249481X-RAY DIFFRACTION10287
3.547-3.5660.257493X-RAY DIFFRACTION10286
3.566-3.5860.238501X-RAY DIFFRACTION10288
3.586-3.6060.23479X-RAY DIFFRACTION10284
3.606-3.6270.236503X-RAY DIFFRACTION10289
3.627-3.6480.223518X-RAY DIFFRACTION10285
3.648-3.6690.208475X-RAY DIFFRACTION10288
3.669-3.6910.226508X-RAY DIFFRACTION10288
3.691-3.7140.211497X-RAY DIFFRACTION10289
3.714-3.7370.208501X-RAY DIFFRACTION10287
3.737-3.7610.206505X-RAY DIFFRACTION10290
3.761-3.7850.193509X-RAY DIFFRACTION10288
3.785-3.810.211509X-RAY DIFFRACTION10288
3.81-3.8360.199491X-RAY DIFFRACTION10287
3.836-3.8620.213513X-RAY DIFFRACTION10288
3.862-3.890.22490X-RAY DIFFRACTION10288
3.89-3.9180.212498X-RAY DIFFRACTION10288
3.918-3.9460.205551X-RAY DIFFRACTION10290
3.946-3.9760.221488X-RAY DIFFRACTION10289
3.976-4.0070.188513X-RAY DIFFRACTION10289
4.007-4.0380.203501X-RAY DIFFRACTION10288
4.038-4.0710.194509X-RAY DIFFRACTION10289
4.071-4.1040.204511X-RAY DIFFRACTION10289
4.104-4.1390.176512X-RAY DIFFRACTION10288
4.139-4.1750.193512X-RAY DIFFRACTION10290
4.175-4.2120.182538X-RAY DIFFRACTION10290
4.212-4.2510.166505X-RAY DIFFRACTION10291
4.251-4.2910.177523X-RAY DIFFRACTION10291
4.291-4.3320.169507X-RAY DIFFRACTION10289
4.332-4.3760.169534X-RAY DIFFRACTION10292
4.376-4.4210.178531X-RAY DIFFRACTION10291
4.421-4.4680.172532X-RAY DIFFRACTION10292
4.468-4.5170.158532X-RAY DIFFRACTION10291
4.517-4.5680.162516X-RAY DIFFRACTION10292
4.568-4.6220.174541X-RAY DIFFRACTION10291
4.622-4.6780.153511X-RAY DIFFRACTION10291
4.678-4.7370.185546X-RAY DIFFRACTION10291
4.737-4.7990.162506X-RAY DIFFRACTION10291
4.799-4.8650.16536X-RAY DIFFRACTION10291
4.865-4.9340.17524X-RAY DIFFRACTION10291
4.934-5.0080.164544X-RAY DIFFRACTION10292
5.008-5.0860.169526X-RAY DIFFRACTION10291
5.086-5.1690.167538X-RAY DIFFRACTION10291
5.169-5.2580.186542X-RAY DIFFRACTION10293
5.258-5.3530.174528X-RAY DIFFRACTION10292
5.353-5.4560.186544X-RAY DIFFRACTION10292
5.456-5.5670.182550X-RAY DIFFRACTION10293
5.567-5.6880.219524X-RAY DIFFRACTION10291
5.688-5.820.186532X-RAY DIFFRACTION10292
5.82-5.9650.198554X-RAY DIFFRACTION10292
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