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- PDB-1vbd: POLIOVIRUS (TYPE 1, MAHONEY STRAIN) COMPLEXED WITH R78206 -

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Basic information

Entry
Database: PDB / ID: 1vbd
TitlePOLIOVIRUS (TYPE 1, MAHONEY STRAIN) COMPLEXED WITH R78206
Components(POLIOVIRUS TYPE 1 ...) x 5
KeywordsVIRUS / VIRUS COAT PROTEIN / HYDROLASE / THIOL PROTEASE / Icosahedral virus
Function / homology
Function and homology information


symbiont-mediated suppression of host translation initiation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid ...symbiont-mediated suppression of host translation initiation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding
Similarity search - Function
Picornavirus coat protein VP4 / Rhinovirus 14, subunit 4 / Jelly Rolls - #20 / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A ...Picornavirus coat protein VP4 / Rhinovirus 14, subunit 4 / Jelly Rolls - #20 / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / Few Secondary Structures / Irregular / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Reverse transcriptase/Diguanylate cyclase domain / Jelly Rolls / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Chem-J78 / MYRISTIC ACID / Genome polyprotein
Similarity search - Component
Biological speciesHuman poliovirus 1
MethodX-RAY DIFFRACTION / Resolution: 2.9 Å
AuthorsGrant, R.A. / Hiremath, C.N. / Filman, D.J. / Syed, R. / Andries, K. / Hogle, J.M.
Citation
Journal: Curr.Biol. / Year: 1994
Title: Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design.
Authors: Grant, R.A. / Hiremath, C.N. / Filman, D.J. / Syed, R. / Andries, K. / Hogle, J.M.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1995
Title: Binding of the Antiviral Drug Win51711 to the Sabin Strain of Type 3 Poliovirus: Structural Comparison with Drug Binding in Rhinovirus 14
Authors: Hiremath, C.N. / Grant, R.A. / Filman, D.J. / Hogle, J.M.
#2: Journal: New Aspects of Positive-Strand RNA Viruses / Year: 1990
Title: Role of Conformational Transitions in Poliovirus Assembly and Cell Entry
Authors: Hogle, J.M. / Syed, R. / Fricks, C.E. / Icenogle, J.P. / Flore, O. / Filman, D.J.
#3: Journal: Embo J. / Year: 1989
Title: Structural Factors that Control Conformational Transitions and Serotype Specificity in Type 3 Poliovirus
Authors: Filman, D.J. / Syed, R. / Chow, M. / Macadam, A.J. / Minor, P.D. / Hogle, J.M.
#4: Journal: Nature / Year: 1987
Title: Myristylation of Picornavirus Capsid Protein Vp4 and its Structural Significance
Authors: Chow, M. / Newman, J.F. / Filman, D. / Hogle, J.M. / Rowlands, D.J. / Brown, F.
#5: Journal: Science / Year: 1985
Title: Three-Dimensional Structure of Poliovirus at 2.9 A Resolution
Authors: Hogle, J.M. / Chow, M. / Filman, D.J.
#6: Journal: Nucleic Acids Res. / Year: 1983
Title: The Nucleotide Sequence of Poliovirus Type 3 Leon 12 A1B: Comparison with Poliovirus Type 1
Authors: Stanway, G. / Cann, A.J. / Hauptmann, R. / Hughes, P. / Clarke, L.D. / Mountford, R.C. / Minor, P.D. / Schild, G.C. / Almond, J.W.
History
DepositionJan 2, 1996Processing site: BNL
Revision 1.0Jul 11, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 2.0Apr 19, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other / Refinement description
Category: atom_site / cell ...atom_site / cell / database_2 / database_PDB_matrix / pdbx_database_remark / pdbx_struct_oper_list / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_torsion / struct_conn / struct_ncs_oper / struct_ref_seq_dif / struct_site
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _cell.Z_PDB / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _database_PDB_matrix.origx[1][1] / _database_PDB_matrix.origx[1][2] / _database_PDB_matrix.origx[2][1] / _database_PDB_matrix.origx[2][2] / _database_PDB_matrix.origx_vector[3] / _pdbx_struct_oper_list.id / _pdbx_struct_oper_list.matrix[1][1] / _pdbx_struct_oper_list.matrix[1][2] / _pdbx_struct_oper_list.matrix[1][3] / _pdbx_struct_oper_list.matrix[2][1] / _pdbx_struct_oper_list.matrix[2][2] / _pdbx_struct_oper_list.matrix[2][3] / _pdbx_struct_oper_list.matrix[3][1] / _pdbx_struct_oper_list.matrix[3][2] / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type / _pdbx_struct_oper_list.vector[1] / _pdbx_struct_oper_list.vector[2] / _pdbx_struct_oper_list.vector[3] / _pdbx_validate_rmsd_angle.angle_deviation / _pdbx_validate_rmsd_angle.angle_standard_deviation / _pdbx_validate_rmsd_angle.angle_target_value / _pdbx_validate_rmsd_angle.angle_value / _pdbx_validate_rmsd_angle.auth_asym_id_1 / _pdbx_validate_rmsd_angle.auth_asym_id_2 / _pdbx_validate_rmsd_angle.auth_asym_id_3 / _pdbx_validate_rmsd_angle.auth_atom_id_1 / _pdbx_validate_rmsd_angle.auth_atom_id_2 / _pdbx_validate_rmsd_angle.auth_atom_id_3 / _pdbx_validate_rmsd_angle.auth_comp_id_1 / _pdbx_validate_rmsd_angle.auth_comp_id_2 / _pdbx_validate_rmsd_angle.auth_comp_id_3 / _pdbx_validate_rmsd_angle.auth_seq_id_1 / _pdbx_validate_rmsd_angle.auth_seq_id_2 / _pdbx_validate_rmsd_angle.auth_seq_id_3 / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Details: Coordinates and associated matrices have been transformed from the icosahedral point symmetry frame to the crystallographic frame
Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: POLIOVIRUS TYPE 1 MAHONEY
1: POLIOVIRUS TYPE 1 MAHONEY
2: POLIOVIRUS TYPE 1 MAHONEY
3: POLIOVIRUS TYPE 1 MAHONEY
4: POLIOVIRUS TYPE 1 MAHONEY
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,5547
Polymers97,9425
Non-polymers6122
Water0
1
0: POLIOVIRUS TYPE 1 MAHONEY
1: POLIOVIRUS TYPE 1 MAHONEY
2: POLIOVIRUS TYPE 1 MAHONEY
3: POLIOVIRUS TYPE 1 MAHONEY
4: POLIOVIRUS TYPE 1 MAHONEY
hetero molecules
x 60


Theoretical massNumber of molelcules
Total (without water)5,913,251420
Polymers5,876,540300
Non-polymers36,711120
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
2


  • Idetical with deposited unit
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
0: POLIOVIRUS TYPE 1 MAHONEY
1: POLIOVIRUS TYPE 1 MAHONEY
2: POLIOVIRUS TYPE 1 MAHONEY
3: POLIOVIRUS TYPE 1 MAHONEY
4: POLIOVIRUS TYPE 1 MAHONEY
hetero molecules
x 5


  • icosahedral pentamer
  • 493 kDa, 25 polymers
Theoretical massNumber of molelcules
Total (without water)492,77135
Polymers489,71225
Non-polymers3,05910
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
0: POLIOVIRUS TYPE 1 MAHONEY
1: POLIOVIRUS TYPE 1 MAHONEY
2: POLIOVIRUS TYPE 1 MAHONEY
3: POLIOVIRUS TYPE 1 MAHONEY
4: POLIOVIRUS TYPE 1 MAHONEY
hetero molecules
x 6


  • icosahedral 23 hexamer
  • 591 kDa, 30 polymers
Theoretical massNumber of molelcules
Total (without water)591,32542
Polymers587,65430
Non-polymers3,67112
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
6
0: POLIOVIRUS TYPE 1 MAHONEY
1: POLIOVIRUS TYPE 1 MAHONEY
2: POLIOVIRUS TYPE 1 MAHONEY
3: POLIOVIRUS TYPE 1 MAHONEY
4: POLIOVIRUS TYPE 1 MAHONEY
hetero molecules
x 30


  • crystal asymmetric unit, crystal frame
  • 2.96 MDa, 150 polymers
Theoretical massNumber of molelcules
Total (without water)2,956,626210
Polymers2,938,270150
Non-polymers18,35660
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z2
point symmetry operation29
Unit cell
Length a, b, c (Å)322.940, 358.040, 380.150
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
SymmetryPoint symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral))
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2generate(0.30928879, -0.8162167, 0.48798633), (0.80181729, 0.4997282, 0.32765947), (-0.51130183, 0.28993456, 0.80901699)46.32068, 31.10212, -18.1285
3generate(-0.80830541, -0.51884908, 0.2782768), (0.48115092, -0.30972858, 0.82009864), (-0.33931724, 0.79678356, 0.5)26.41461, 77.84547, -47.46104
4generate(-0.8083054, 0.48115093, -0.33931714), (-0.51884908, -0.30972858, 0.7967833), (0.27827689, 0.8200989, 0.5)-32.20869, 75.63233, -47.46104
5generate(0.30928879, 0.80181729, -0.51130167), (-0.8162167, 0.4997282, 0.28993447), (0.48798649, 0.32765957, 0.80901699)-48.53382, 27.52118, -18.1285
6generate(-0.99715365, -0.0753963), (-0.0753963, 0.99715365), (-1)-189.84416
7generate(-0.36886251, 0.7762158, -0.51130167), (0.7762158, 0.55984552, 0.28993447), (0.51130183, -0.28993456, -0.80901699)-48.53382, 27.52118, -171.71566
8generate(0.76972768, 0.54072464, -0.33931714), (0.54072464, -0.26972768, 0.7967833), (0.33931724, -0.79678356, -0.5)-32.20869, 75.63233, -142.38312
9generate(0.84512398, -0.45642901, 0.2782768), (-0.45642901, -0.34512398, 0.82009864), (-0.27827689, -0.8200989, -0.5)26.41461, 77.84547, -142.38312
10generate(-0.24686873, -0.83721269, 0.48798633), (-0.83721269, 0.43785174, 0.32765947), (-0.48798649, -0.32765957, -0.80901699)46.32068, 31.10212, -171.71566
11generate(-0.03769815, -0.00142318, 0.999288), (0.99857683, 0.03769815, 0.037725), (-0.03772501, 0.99928832)94.8545, 3.58094, -94.92208
12generate(-0.52373853, 0.31978679, 0.78957847), (0.31978679, -0.78527847, 0.53016417), (0.78957872, 0.53016433, 0.30901699)74.94843, 50.32429, -65.58954
13generate(-0.30928879, 0.8162167, 0.48798633), (-0.80181729, -0.4997282, 0.32765947), (0.51130183, -0.28993456, 0.80901699)46.32068, 31.10212, -18.1285
14generate(0.30928879, 0.80181729, 0.51130167), (-0.8162167, 0.4997282, -0.28993447), (-0.48798649, -0.32765957, 0.80901699)48.53382, -27.52118, -18.1285
15generate(0.47714105, 0.29648805, 0.82730347), (0.29648805, 0.83187594, -0.46912383), (-0.82730373, 0.46912399, 0.30901699)78.52937, -44.53021, -65.58954
16generate(0.03769815, 0.00142318, 0.999288), (-0.99857683, -0.03769815, 0.037725), (0.03772501, -0.99928832)94.8545, 3.58094, -94.92208
17generate(-0.49813704, 0.25966947, 0.82730347), (-0.35836451, 0.80715403, -0.46912383), (-0.78957872, -0.53016433, -0.30901699)78.52937, -44.53021, -124.25462
18generate(-0.36886251, 0.7762158, 0.51130167), (0.7762158, 0.55984552, -0.28993447), (-0.51130183, 0.28993456, -0.80901699)48.53382, -27.52118, -171.71566
19generate(0.24686873, 0.83721269, 0.48798633), (0.83721269, -0.43785174, 0.32765947), (0.48798649, 0.32765957, -0.80901699)46.32068, 31.10212, -171.71566
20generate(0.49813704, 0.35836451, 0.78957847), (-0.25966947, -0.80715403, 0.53016417), (0.82730373, -0.46912399, -0.30901699)74.94843, 50.32429, -124.25462
21generate(-0.03769815, 0.99857683, -0.037725), (-0.00142318, 0.03769815, 0.999288), (0.99928832, 0.03772501)-3.58094, 94.8545, -94.92208
22generate(0.80830541, 0.51884908, 0.2782768), (-0.48115092, 0.30972858, 0.82009864), (0.33931724, -0.79678356, 0.5)26.41461, 77.84547, -47.46104
23generate(0.52373853, -0.31978679, 0.78957847), (-0.31978679, 0.78527847, 0.53016417), (-0.78957872, -0.53016433, 0.30901699)74.94843, 50.32429, -65.58954
24generate(-0.49813704, -0.35836451, 0.78957847), (0.25966947, 0.80715403, 0.53016417), (-0.82730373, 0.46912399, -0.30901699)74.94843, 50.32429, -124.25462
25generate(-0.84512398, 0.45642901, 0.2782768), (0.45642901, 0.34512398, 0.82009864), (0.27827689, 0.8200989, -0.5)26.41461, 77.84547, -142.38312
26generate(0.03769815, -0.99857683, -0.037725), (0.00142318, -0.03769815, 0.999288), (-0.99928832, -0.03772501)-3.58094, 94.8545, -94.92208
27generate(-0.76972768, -0.54072464, -0.33931714), (-0.54072464, 0.26972768, 0.7967833), (-0.33931724, 0.79678356, -0.5)-32.20869, 75.63233, -142.38312
28generate(-0.49813704, 0.25966947, -0.82730347), (-0.35836451, 0.80715403, 0.46912383), (0.78957872, 0.53016433, -0.30901699)-78.52937, 44.53021, -124.25462
29generate(0.47714105, 0.29648805, -0.82730347), (0.29648805, 0.83187594, 0.46912383), (0.82730373, -0.46912399, 0.30901699)-78.52937, 44.53021, -65.58954
30generate(0.8083054, -0.48115093, -0.33931714), (0.51884908, 0.30972858, 0.7967833), (-0.27827689, -0.8200989, 0.5)-32.20869, 75.63233, -47.46104

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Components

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POLIOVIRUS TYPE 1 ... , 5 types, 5 molecules 01234

#1: Protein/peptide POLIOVIRUS TYPE 1 MAHONEY


Mass: 437.404 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: P1/MAHONEY PREPARED FROM A LOW-PASSAGE STOCK, PROVIDED BY M. CHOW, OF A PLAQUE ISOLATED FROM HELA CELLS TRANSFECTED WITH AN INFECTIOUS CDNA CLONE OF THE VIRAL GENOME
Source: (natural) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Strain: Mahoney
#2: Protein POLIOVIRUS TYPE 1 MAHONEY


Mass: 33488.613 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: P1/MAHONEY PREPARED FROM A LOW-PASSAGE STOCK, PROVIDED BY M. CHOW, OF A PLAQUE ISOLATED FROM HELA CELLS TRANSFECTED WITH AN INFECTIOUS CDNA CLONE OF THE VIRAL GENOME
Source: (natural) Human poliovirus 1 / Genus: Enterovirus / Cell line: HELA / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300
#3: Protein POLIOVIRUS TYPE 1 MAHONEY


Mass: 30075.783 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: P1/MAHONEY PREPARED FROM A LOW-PASSAGE STOCK, PROVIDED BY M. CHOW, OF A PLAQUE ISOLATED FROM HELA CELLS TRANSFECTED WITH AN INFECTIOUS CDNA CLONE OF THE VIRAL GENOME
Source: (natural) Human poliovirus 1 / Genus: Enterovirus / Cell line: HELA / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300
#4: Protein POLIOVIRUS TYPE 1 MAHONEY


Mass: 26547.482 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: P1/MAHONEY PREPARED FROM A LOW-PASSAGE STOCK, PROVIDED BY M. CHOW, OF A PLAQUE ISOLATED FROM HELA CELLS TRANSFECTED WITH AN INFECTIOUS CDNA CLONE OF THE VIRAL GENOME
Source: (natural) Human poliovirus 1 / Genus: Enterovirus / Cell line: HELA / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300
#5: Protein POLIOVIRUS TYPE 1 MAHONEY


Mass: 7393.050 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: P1/MAHONEY PREPARED FROM A LOW-PASSAGE STOCK, PROVIDED BY M. CHOW, OF A PLAQUE ISOLATED FROM HELA CELLS TRANSFECTED WITH AN INFECTIOUS CDNA CLONE OF THE VIRAL GENOME
Source: (natural) Human poliovirus 1 / Genus: Enterovirus / Cell line: HELA / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300*PLUS

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Non-polymers , 2 types, 2 molecules

#6: Chemical ChemComp-J78 / (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE / R78206


Mass: 383.484 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H29N3O3
#7: Chemical ChemComp-MYR / MYRISTIC ACID / Myristic acid


Mass: 228.371 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H28O2

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.59 Å3/Da / Density % sol: 30 %
Crystal grow
*PLUS
Method: other / Details: Hogle, J.M., (1985) Science, 229, 1358.

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 2.9→30 Å / Num. obs: 298390 / % possible obs: 30 % / Observed criterion σ(I): 0
Reflection
*PLUS
Num. measured all: 737276

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Processing

Software
NameVersionClassification
X-PLORmodel building
X-PLOR2.1refinement
X-PLORphasing
RefinementRfactor Rwork: 0.287 / Highest resolution: 2.9 Å
Refinement stepCycle: LAST / Highest resolution: 2.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6632 0 43 0 6675
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.011
X-RAY DIFFRACTIONo_bond_d_na
X-RAY DIFFRACTIONo_bond_d_prot
X-RAY DIFFRACTIONo_angle_d
X-RAY DIFFRACTIONo_angle_d_na
X-RAY DIFFRACTIONo_angle_d_prot
X-RAY DIFFRACTIONo_angle_deg2.526
X-RAY DIFFRACTIONo_angle_deg_na
X-RAY DIFFRACTIONo_angle_deg_prot
X-RAY DIFFRACTIONo_dihedral_angle_d
X-RAY DIFFRACTIONo_dihedral_angle_d_na
X-RAY DIFFRACTIONo_dihedral_angle_d_prot
X-RAY DIFFRACTIONo_improper_angle_d
X-RAY DIFFRACTIONo_improper_angle_d_na
X-RAY DIFFRACTIONo_improper_angle_d_prot
X-RAY DIFFRACTIONo_mcbond_it
X-RAY DIFFRACTIONo_mcangle_it
X-RAY DIFFRACTIONo_scbond_it
X-RAY DIFFRACTIONo_scangle_it
Software
*PLUS
Name: 'PSEUDO-REAL SPACE PROCEDURE' / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.287
Solvent computation
*PLUS
Displacement parameters
*PLUS

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