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- PDB-1eah: PV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973 -

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Basic information

Entry
Database: PDB / ID: 1eah
TitlePV2L COMPLEXED WITH ANTIVIRAL AGENT SCH48973
Components(POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO ...) x 4
KeywordsVIRUS / TYPE 2 / LANSING / ANTIVIRAL / PICORNAVIRUS / MOUSE NEUROVIRULENCE / COAT PROTEIN / Icosahedral virus
Function / homology
Function and homology information


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 ...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 / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / receptor-mediated endocytosis of virus by host cell / DNA replication / 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 / structural molecule activity / virion attachment to host cell / 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
MYRISTIC ACID / Chem-SC4 / Genome polyprotein
Similarity search - Component
Biological speciesHuman poliovirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.9 Å
AuthorsLentz, K. / Arnold, E.
Citation
Journal: Structure / Year: 1997
Title: Structure of poliovirus type 2 Lansing complexed with antiviral agent SCH48973: comparison of the structural and biological properties of three poliovirus serotypes.
Authors: Lentz, K.N. / Smith, A.D. / Geisler, S.C. / Cox, S. / Buontempo, P. / Skelton, A. / DeMartino, J. / Rozhon, E. / Schwartz, J. / Girijavallabhan, V. / O'Connell, J. / Arnold, E.
#1: 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.
#2: Journal: Semin.Virol. / Year: 1992
Title: Three Dimensional Structure-Activity Relationships for Antiviral Agents that Interact with Picornavirus Capsids
Authors: Zhang, A. / Nanni, R. / Oren, D.A. / Rozhon, E.J. / Arnold, E.
#3: Journal: Embo J. / Year: 1991
Title: Three-Dimensional Structure of a Mouse-Adapted Type 2/Type 1 Poliovirus Chimera
Authors: Yeates, T.O. / Jacobson, D.H. / Martin, A. / Wychowski, C. / Girard, M. / Filman, D.J. / Hogle, J.M.
#4: 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.
#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.
History
DepositionJul 22, 1997Processing site: BNL
Revision 1.0Sep 16, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
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_database_status / pdbx_struct_oper_list / pdbx_validate_symm_contact / 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][3] / _database_PDB_matrix.origx[3][1] / _database_PDB_matrix.origx[3][3] / _database_PDB_matrix.origx_vector[1] / _database_PDB_matrix.origx_vector[2] / _database_PDB_matrix.origx_vector[3] / _pdbx_database_status.process_site / _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.matrix[3][3] / _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_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

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Assembly

Deposited unit
1: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
2: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
3: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
4: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,4916
Polymers96,8394
Non-polymers6522
Water4,882271
1
1: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
2: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
3: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
4: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
hetero molecules
x 60


Theoretical massNumber of molelcules
Total (without water)5,849,478360
Polymers5,810,353240
Non-polymers39,125120
Water4,324240
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
1: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
2: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
3: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
4: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
hetero molecules
x 5


  • icosahedral pentamer
  • 487 kDa, 20 polymers
Theoretical massNumber of molelcules
Total (without water)487,45730
Polymers484,19620
Non-polymers3,26010
Water36020
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
1: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
2: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
3: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
4: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
hetero molecules
x 6


  • icosahedral 23 hexamer
  • 585 kDa, 24 polymers
Theoretical massNumber of molelcules
Total (without water)584,94836
Polymers581,03524
Non-polymers3,91312
Water43224
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
1: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
2: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
3: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
4: POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4
hetero molecules
x 30


  • crystal asymmetric unit, crystal frame
  • 2.92 MDa, 120 polymers
Theoretical massNumber of molelcules
Total (without water)2,924,739180
Polymers2,905,177120
Non-polymers19,56360
Water2,162120
TypeNameSymmetry operationNumber
identity operation1_555x,y,z2
point symmetry operation29
Unit cell
Length a, b, c (Å)345.700, 497.200, 485.900
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
SymmetryPoint symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral))
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2generate(0.64288003, -0.71885497, 0.26448569), (0.21383163, 0.5, 0.83921163), (-0.73551431, -0.48295691, 0.47515394)36.13781, -54.46063, 109.61977
3generate(0.0650478, -0.94930019, -0.30756748), (-0.37286826, -0.30901699, 0.87491595), (-0.92560145, 0.05777078, -0.37406479)127.51224, 18.03064, 161.42831
4generate(0.0650478, -0.37286819, -0.92560145), (-0.94930037, -0.30901699, 0.05777079), (-0.30756747, 0.87491578, -0.37406479)147.84694, 117.29335, 83.82797
5generate(0.64288003, 0.21383159, -0.73551431), (-0.71885511, 0.5, -0.482957), (0.26448569, 0.83921147, 0.47515395)69.04004, 106.1498, -15.94021
6generate(-0.72193856, -0.23044522, -0.65245666), (-0.23044526, -0.80901699, 0.54072779), (-0.65245666, 0.54072769, 0.53095555)101.14145, 106.10875, 5.62686
7generate(-0.03350516, 0.71885497, -0.69435208), (-0.71885511, -0.5, -0.482957), (-0.69435208, 0.48295691, 0.53350516)16.08021, 201.115, 10.80336
8generate(0.64288003, 0.71885497, 0.26448569), (-0.21383163, 0.5, -0.83921163), (-0.73551431, 0.48295691, 0.47515394)-100.39461, 149.42583, 17.89157
9generate(0.37247566, -0.23044522, 0.89897545), (0.5866999, 0.80901699, -0.03570432), (-0.71905852, 0.54072769, 0.43654132)-87.31877, 22.47392, 17.09583
10generate(-0.47102862, -0.817145, 0.33227391), (0.57643211, 0.81714516), (-0.66772608, 0.576432, 0.47102862)37.23736, -4.29751, 9.51582
11generate(-0.31156659, 0.94930019, -0.04189543), (0.94930037, 0.30901699, -0.05777079), (-0.04189542, -0.05777078, -0.99745039)-85.06124, 72.63705, 248.1265
12generate(0.03350516, 0.71885497, 0.69435208), (0.71885511, -0.5, 0.482957), (0.69435208, 0.48295691, -0.53350516)-152.61263, 83.7806, 140.41844
13generate(-0.33545217, 0.94205724), (-1), (0.94205724, 0.33545217)-114.4364, 189.9304, 80.72595
14generate(-0.90855208, -0.21383159, 0.35889992), (-0.21383163, -0.5, -0.83921163), (0.35889992, -0.83921147, 0.40855208)-23.29081, 244.39103, 151.54202
15generate(-0.89378997, 0.37286819, -0.24921627), (0.37286826, 0.30901699, -0.87491595), (-0.24921626, -0.87491578, -0.41522701)-5.13596, 171.89976, 255.00125
16generate(-0.37247566, -0.58669978, 0.71905852), (-0.23044526, 0.80901699, 0.54072779), (-0.89897545, 0.03570431, -0.43654133)-31.63157, -47.54817, 171.11319
17generate(-0.89378997, -0.37286819, -0.24921627), (-0.37286826, 0.30901699, 0.87491595), (-0.24921626, 0.87491578, -0.41522701)65.68305, -40.66108, 88.82815
18generate(-0.47102862, 0.576432, -0.66772608), (-0.81714516, 0.57643211), (0.33227391, 0.817145, 0.47102862)26.37105, 24.94311, -13.34354
19generate(0.31156659, 0.94930019, 0.04189543), (-0.94930037, 0.30901699, 0.05777079), (0.04189542, -0.05777078, 0.99745039)-95.23973, 58.60163, 5.79593
20generate(0.37247566, 0.23044522, 0.89897545), (-0.5866999, 0.80901699, 0.03570432), (-0.71905852, -0.54072769, 0.43654132)-131.08732, 13.79956, 119.79646
21generate(-0.47102862, -0.576432, -0.66772608), (0.81714516, -0.57643211), (0.33227391, -0.817145, 0.47102862)135.85301, 164.98729, 141.85714
22generate(0.0650478, 0.37286819, -0.92560145), (0.94930037, -0.30901699, -0.05777079), (-0.30756747, -0.87491578, -0.37406479)77.02793, 131.32877, 250.00107
23generate(0.80234206, 0.58669978, -0.10968365), (0.5866999, -0.80901699, -0.03570432), (-0.10968365, -0.03570431, -0.99332507)-42.39224, 176.13084, 245.52983
24generate(0.72193856, -0.23044522, 0.65245666), (0.23044526, -0.80901699, -0.54072779), (0.65245666, 0.54072769, -0.53095555)-57.3729, 237.47857, 134.62251
25generate(-0.0650478, -0.94930019, 0.30756748), (0.37286826, -0.30901699, -0.87491595), (0.92560145, 0.05777078, 0.37406479)52.78872, 230.59148, 70.54927
26generate(0.90855208, -0.21383159, -0.35889992), (0.21383163, -0.5, 0.83921163), (-0.35889992, -0.83921147, -0.40855208)63.90393, 40.50457, 250.79975
27generate(0.80234206, -0.58669978, -0.10968365), (-0.5866999, -0.80901699, 0.03570432), (-0.10968365, 0.03570431, -0.99332507)69.03988, 167.45648, 238.7485
28generate(0.47102862, -0.817145, -0.33227391), (-0.57643211, -0.81714516), (0.66772608, 0.576432, -0.47102862)117.96331, 194.22791, 123.95222
29generate(0.37247566, -0.58669978, -0.71905852), (0.23044526, 0.80901699, -0.54072779), (0.89897545, 0.03570431, 0.43654133)143.0637, 83.82165, 65.05548
30generate(0.64288003, -0.21383159, -0.73551431), (0.71885511, 0.5, 0.482957), (0.26448569, -0.83921147, 0.47515395)109.65316, -11.1846, 143.45156

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Components

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POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO ... , 4 types, 4 molecules 1234

#1: Protein POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4


Mass: 33039.145 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 2 / Genus: Enterovirus / Species: Poliovirus / Strain: LANSING / Cell line: HELA CELLS / Cell line (production host): HELA CELLS / Production host: Homo sapiens (human) / References: UniProt: P06210
#2: Protein POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4


Mass: 29980.822 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 2 / Genus: Enterovirus / Species: Poliovirus / Strain: LANSING / Cell line: HELA CELLS / Cell line (production host): HELA CELLS / Production host: Homo sapiens (human) / References: UniProt: P06210
#3: Protein POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4


Mass: 26472.293 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 2 / Genus: Enterovirus / Species: Poliovirus / Strain: LANSING / Cell line: HELA CELLS / Cell line (production host): HELA CELLS / Production host: Homo sapiens (human) / References: UniProt: P06210
#4: Protein POLIOVIRUS TYPE 2 COAT PROTEINS VP1 TO VP4


Mass: 7346.957 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 2 / Genus: Enterovirus / Species: Poliovirus / Strain: LANSING / Cell line: HELA CELLS / Cell line (production host): HELA CELLS / Production host: Homo sapiens (human) / References: UniProt: P06210

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Non-polymers , 3 types, 273 molecules

#5: Chemical ChemComp-SC4 / 1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE


Mass: 423.717 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H17Cl3O3
#6: Chemical ChemComp-MYR / MYRISTIC ACID / Myristic acid


Mass: 228.371 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H28O2
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 271 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity % sol: 50 %
Crystal
*PLUS
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
10.9-1.4 %PEG80001reservoir
2100-250 mM1reservoirLi2SO4
35 mg/mlvirus1drop

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918
DetectorType: FUJI / Detector: IMAGE PLATE / Date: Mar 1, 1996
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918 Å / Relative weight: 1
ReflectionRedundancy: 2.79 % / Biso Wilson estimate: 21.2 Å2 / Rmerge(I) obs: 0.11
Reflection
*PLUS
Highest resolution: 2.9 Å / Lowest resolution: 30 Å / Num. obs: 444639 / % possible obs: 48.9 % / Num. measured all: 1242301 / Rmerge(I) obs: 0.11
Reflection shell
*PLUS
Highest resolution: 2.9 Å / Lowest resolution: 3 Å / % possible obs: 34.9 % / Rmerge(I) obs: 0.227

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
X-PLORphasing
RefinementHighest resolution: 2.9 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED
RfactorNum. reflection% reflection
Rwork0.185 --
obs0.185 402860 45.4 %
Displacement parametersBiso mean: 14.1 Å2
Refine analyzeLuzzati coordinate error obs: 0.27 Å / Luzzati d res low obs: 10 Å
Refinement stepCycle: LAST / Highest resolution: 2.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6516 0 38 271 6825
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.5
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d26.7
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.35
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it1.5
X-RAY DIFFRACTIONx_mcangle_it2
X-RAY DIFFRACTIONx_scbond_it2
X-RAY DIFFRACTIONx_scangle_it2.5
Refine LS restraints NCSNCS model details: STRICT (THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS 30 PROTOMERS RELATED BY ICOSAHEDRAL SYMMETRY)
LS refinement shellResolution: 2.9→3.03 Å / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rwork0.231 32694 -
obs--29.6 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2ADDITIONAL.PARADDITIONAL.TOP
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Lowest resolution: 10 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg26.7
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.35

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