[English] 日本語
Yorodumi
- PDB-2xgk: Virus like particle of L172W mutant of Minute Virus of Mice - the... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2xgk
TitleVirus like particle of L172W mutant of Minute Virus of Mice - the immunosuppressive strain
ComponentsCOAT PROTEIN VP2
KeywordsVIRUS / VLP / PARVOVIRUS
Function / homology
Function and homology information


permeabilization of host organelle membrane involved in viral entry into host cell / symbiont entry into host cell via permeabilization of inner membrane / microtubule-dependent intracellular transport of viral material towards nucleus / T=1 icosahedral viral capsid / viral penetration into host nucleus / clathrin-dependent endocytosis of virus by host cell / host cell nucleus / virion attachment to host cell / structural molecule activity / metal ion binding
Similarity search - Function
Phospholipase A2-like domain / Phospholipase A2-like domain / Parvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Parvovirus coat protein VP2 / Capsid/spike protein, ssDNA virus
Similarity search - Domain/homology
Biological speciesMURINE MINUTE VIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.2 Å
AuthorsPlevka, P. / Hafenstein, S. / Tattersall, P. / Cotmore, S. / Farr, G. / D'Abramo, A. / Rossmann, M.G.
CitationJournal: J.Virol. / Year: 2011
Title: Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome is Packaged Via a Pore at a 5-Fold Axis.
Authors: Plevka, P. / Hafenstein, S. / Li, L. / D'Abrgamo, A. / Cotmore, S.F. / Rossmann, M.G. / Tattersall, P.
History
DepositionJun 4, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 20, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 16, 2011Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Other / Structure summary
Revision 1.2Jan 30, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: COAT PROTEIN VP2


Theoretical massNumber of molelcules
Total (without water)64,8191
Polymers64,8191
Non-polymers00
Water0
1
A: COAT PROTEIN VP2
x 60


Theoretical massNumber of molelcules
Total (without water)3,889,11960
Polymers3,889,11960
Non-polymers00
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
A: COAT PROTEIN VP2
x 5


  • icosahedral pentamer
  • 324 kDa, 5 polymers
Theoretical massNumber of molelcules
Total (without water)324,0935
Polymers324,0935
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
A: COAT PROTEIN VP2
x 6


  • icosahedral 23 hexamer
  • 389 kDa, 6 polymers
Theoretical massNumber of molelcules
Total (without water)388,9126
Polymers388,9126
Non-polymers00
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
A: COAT PROTEIN VP2
x 60
A: COAT PROTEIN VP2
x 60


  • crystal asymmetric unit, crystal frame
  • 7.78 MDa, 120 polymers
Theoretical massNumber of molelcules
Total (without water)7,778,239120
Polymers7,778,239120
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z3
point symmetry operation118
transform to crystal frame1
Unit cell
Length a, b, c (Å)442.900, 411.100, 301.800
Angle α, β, γ (deg.)90.00, 95.88, 90.00
Int Tables number5
Space group name H-MC121
SymmetryPoint symmetry: (Schoenflies symbol: I (icosahedral))
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2generate(0.959943, -0.141521, 0.241827), (0.141521, -0.5, -0.854384), (0.241827, 0.854384, -0.459943)
3generate(0.959943, 0.141521, 0.241827), (-0.141521, -0.5, 0.854384), (0.241827, -0.854384, -0.459943)
4generate(0.920505, -0.390731), (-1), (-0.390731, -0.920505)
5generate(0.789143, -0.464105, 0.402317), (-0.141521, 0.5, 0.854384), (-0.597683, -0.731168, 0.328891)
6generate(0.789143, 0.464105, 0.402317), (0.141521, 0.5, -0.854384), (-0.597683, 0.731168, 0.328891)
7generate(0.39154, -0.89246, -0.22408), (0.89246, 0.309017, 0.32867), (-0.22408, -0.32867, 0.917477)
8generate(0.195366, 0.199368, 0.960252), (0.979925, -0.199368), (-0.039748, 0.979925, -0.195366)
9generate(0.44797, 0.693092, -0.564754), (0.89246, -0.309017, 0.32867), (0.05328, -0.651254, -0.756987)
10generate(0.44797, 0.89246, 0.05328), (0.693092, -0.309017, -0.651254), (-0.564754, 0.32867, -0.756987)
11generate(0.569212, -0.464105, -0.678678), (0.464105, -0.5, 0.731168), (-0.678678, -0.731168, -0.069212)
12generate(0.316608, -0.428354, 0.846328), (0.55157, 0.809017, 0.203129), (-0.771706, 0.402497, 0.492409)
13generate(-0.592969, -0.55157, -0.58665), (0.55157, -0.809017, 0.203129), (-0.58665, -0.203129, 0.783952)
14generate(-0.789143, -0.141521, 0.597683), (0.464105, 0.5, 0.731168), (-0.402317, 0.854384, -0.328891)
15generate(-0.633025, 0.693092, -0.344823), (0.693092, 0.309017, -0.651254), (-0.344823, -0.651254, -0.675992)
16generate(-0.316608, 0.55157, 0.771706), (0.428354, 0.809017, -0.402497), (-0.846328, 0.203129, -0.492409)
17generate(-0.039248, 0.428354, -0.902758), (0.428354, -0.809017, -0.402497), (-0.902758, -0.402497, -0.151735)
18generate(-0.195366, -0.979925, 0.039748), (0.199368, 0.979925), (-0.960252, 0.199368, 0.195366)
19generate(-0.592969, 0.55157, -0.58665), (-0.55157, -0.809017, -0.203129), (-0.58665, 0.203129, 0.783952)
20generate(-0.633025, -0.693092, -0.344823), (-0.693092, 0.309017, 0.651254), (-0.344823, 0.651254, -0.675992)
21generate(-0.789143, 0.141521, 0.597683), (-0.464105, 0.5, -0.731168), (-0.402317, -0.854384, -0.328891)
22generate(-0.316608, -0.55157, 0.771706), (-0.428354, 0.809017, 0.402497), (-0.846328, -0.203129, -0.492409)
23generate(-0.195366, 0.979925, 0.039748), (-0.199368, -0.979925), (-0.960252, -0.199368, 0.195366)
24generate(-0.039248, -0.428354, -0.902758), (-0.428354, -0.809017, 0.402497), (-0.902758, 0.402497, -0.151735)
25generate(0.39154, 0.89246, -0.22408), (-0.89246, 0.309017, -0.32867), (-0.22408, 0.32867, 0.917477)
26generate(0.44797, -0.693092, -0.564754), (-0.89246, -0.309017, -0.32867), (0.05328, 0.651254, -0.756987)
27generate(0.195366, -0.199368, 0.960252), (-0.979925, 0.199368), (-0.039748, -0.979925, -0.195366)
28generate(0.44797, -0.89246, 0.05328), (-0.693092, -0.309017, 0.651254), (-0.564754, -0.32867, -0.756987)
29generate(0.316608, 0.428354, 0.846328), (-0.55157, 0.809017, -0.203129), (-0.771706, -0.402497, 0.492409)
30generate(0.569212, 0.464105, -0.678678), (-0.464105, -0.5, -0.731168), (-0.678678, 0.731168, -0.069212)
31generate(0.745476, 0.666533), (1), (-0.666533, 0.745476)205.98199, 150.08099
32generate(0.8768, 0.463974, -0.126291), (0.141521, -0.5, -0.854384), (-0.459557, 0.731251, -0.504062)205.98199, 150.08099
33generate(0.8768, -0.463974, -0.126291), (-0.141521, -0.5, 0.854384), (-0.459557, -0.731251, -0.504062)205.98199, 150.08099
34generate(0.425779, -0.904827), (-1), (-0.904827, -0.425779)205.98199, 150.08099
35generate(0.189912, -0.833327, 0.519134), (-0.141521, 0.5, 0.854384), (-0.971548, -0.235727, -0.022977)205.98199, 150.08099
36generate(0.189912, 0.833327, 0.519134), (0.141521, 0.5, -0.854384), (-0.971548, 0.235727, -0.022977)205.98199, 150.08099
37generate(0.142527, -0.884377, 0.444482), (0.89246, 0.309017, 0.32867), (-0.428021, 0.349838, 0.833314)205.98199, 150.08099
38generate(0.119147, 0.801776, 0.585628), (0.979925, -0.199368), (-0.159848, 0.597625, -0.78568)205.98199, 150.08099
39generate(0.369464, 0.082601, -0.925567), (0.89246, -0.309017, 0.32867), (-0.258867, -0.947463, -0.187889)205.98199, 150.08099
40generate(-0.042476, 0.884377, -0.464837), (0.693092, -0.309017, -0.651254), (-0.719597, -0.349838, -0.599828)205.98199, 150.08099
41generate(-0.028027, -0.833327, -0.55207), (0.464105, -0.5, 0.731168), (-0.885337, -0.235727, 0.400765)205.98199, 150.08099
42generate(-0.278343, -0.05105, 0.959124), (0.55157, 0.809017, 0.203129), (-0.786318, 0.585564, -0.197026)205.98199, 150.08099
43generate(-0.833065, -0.546575, 0.085196), (0.55157, -0.809017, 0.203129), (-0.042101, 0.216211, 0.975438)205.98199, 150.08099
44generate(-0.856445, 0.463974, 0.226342), (0.464105, 0.5, 0.731168), (0.226072, 0.731251, -0.643555)205.98199, 150.08099
45generate(-0.701741, 0.082601, -0.707628), (0.693092, 0.309017, -0.651254), (0.164875, -0.947463, -0.2741)205.98199, 150.08099
46generate(-0.800129, 0.546575, 0.247081), (0.428354, 0.809017, -0.402497), (-0.419888, -0.216211, -0.881446)205.98199, 150.08099
47generate(-0.630976, 0.05105, -0.774121), (0.428354, -0.809017, -0.402497), (-0.646825, -0.585564, 0.488602)205.98199, 150.08099
48generate(-0.78568, -0.597625, 0.159848), (0.199368, 0.979925), (-0.585628, 0.801776, 0.119147)205.98199, 150.08099
49generate(-0.833065, 0.546575, 0.085196), (-0.55157, -0.809017, -0.203129), (-0.042101, -0.216211, 0.975438)205.98199, 150.08099
50generate(-0.701741, -0.082601, -0.707628), (-0.693092, 0.309017, 0.651254), (0.164875, 0.947463, -0.2741)205.98199, 150.08099
51generate(-0.856445, -0.463974, 0.226342), (-0.464105, 0.5, -0.731168), (0.226072, -0.731251, -0.643555)205.98199, 150.08099
52generate(-0.800129, -0.546575, 0.247081), (-0.428354, 0.809017, 0.402497), (-0.419888, 0.216211, -0.881446)205.98199, 150.08099
53generate(-0.78568, 0.597625, 0.159848), (-0.199368, -0.979925), (-0.585628, -0.801776, 0.119147)205.98199, 150.08099
54generate(-0.630976, -0.05105, -0.774121), (-0.428354, -0.809017, 0.402497), (-0.646825, 0.585564, 0.488602)205.98199, 150.08099
55generate(0.142527, 0.884377, 0.444482), (-0.89246, 0.309017, -0.32867), (-0.428021, -0.349838, 0.833314)205.98199, 150.08099
56generate(0.369464, -0.082601, -0.925567), (-0.89246, -0.309017, -0.32867), (-0.258867, 0.947463, -0.187889)205.98199, 150.08099
57generate(0.119147, -0.801776, 0.585628), (-0.979925, 0.199368), (-0.159848, -0.597625, -0.78568)205.98199, 150.08099
58generate(-0.042476, -0.884377, -0.464837), (-0.693092, -0.309017, 0.651254), (-0.719597, 0.349838, -0.599828)205.98199, 150.08099
59generate(-0.278343, 0.05105, 0.959124), (-0.55157, 0.809017, -0.203129), (-0.786318, -0.585564, -0.197026)205.98199, 150.08099
60generate(-0.028027, 0.833327, -0.55207), (-0.464105, -0.5, -0.731168), (-0.885337, 0.235727, 0.400765)205.98199, 150.08099

-
Components

#1: Protein COAT PROTEIN VP2


Mass: 64818.656 Da / Num. of mol.: 1 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MURINE MINUTE VIRUS / Strain: IMMUNOSUPRESSIVE STRAIN MVMI / Plasmid: PFASTBAC / Cell line (production host): SF1 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: P07302
Compound detailsENGINEERED RESIDUE IN CHAIN A, LEU 303 TO TRP ENGINEERED RESIDUE IN CHAIN B, LEU 303 TO TRP

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 8 Å3/Da / Density % sol: 67 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop / pH: 7.5
Details: 10 MM TRIS-HCL, 8 MM CACL2, PEG 8000, VIRUS CONCENTRATION 10 MG/ML, PH 7.5, VAPOR DIFFUSION, HANGING DROP.

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 1.033
DetectorType: ADSC CCD / Detector: CCD / Date: Dec 10, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 4.2→35 Å / Num. obs: 214730 / % possible obs: 55.3 % / Observed criterion σ(I): 0 / Redundancy: 1.5 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 5.52
Reflection shellResolution: 4.2→4.39 Å / Redundancy: 1.2 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 1.86 / % possible all: 29.4

-
Processing

Software
NameVersionClassification
HKL-2000data reduction
HKL-2000data scaling
GLRFphasing
CNSphasing
CNS1.21refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1MVM
Resolution: 4.2→35 Å / Data cutoff high absF: 10000 / Data cutoff low absF: 0 / Cross valid method: NONE / σ(F): 0 / Stereochemistry target values: CRYSTALLOGRAPHIC RESIDUAL
RfactorNum. reflection% reflection
Rwork0.3029 --
obs0.3029 214730 55.3 %
Solvent computationSolvent model: DENSITY MODIFICATION / Bsol: 63.3752 Å2 / ksol: 0.65 e/Å3
Displacement parametersBiso mean: 108.5 Å2
Baniso -1Baniso -2Baniso -3
1-40.649 Å20 Å2-25.515 Å2
2---24.397 Å20 Å2
3----16.252 Å2
Refine analyzeLuzzati coordinate error obs: 0.96 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 1.31 Å
Refinement stepCycle: LAST / Resolution: 4.2→35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4295 0 0 0 4295
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.01
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d24.1
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.71
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
Refine LS restraints NCSNCS model details: CONSTRAINED
LS refinement shellResolution: 4.2→4.39 Å / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rwork0.4324 13533 -
obs--29.4 %
Xplor fileSerial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

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

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

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

Read more