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- PDB-4wdz: JC Polyomavirus VP1 five-fold pore mutant N221W -

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Basic information

Entry
Database: PDB / ID: 4wdz
TitleJC Polyomavirus VP1 five-fold pore mutant N221W
ComponentsMajor capsid protein VP1
KeywordsVIRAL PROTEIN / beta-sandwich / jelly-roll / viral major capsid protein / five-fold pore
Function / homology
Function and homology information


T=7 icosahedral viral capsid / clathrin-dependent endocytosis of virus by host cell / host cell nucleus / virion attachment to host cell / structural molecule activity
Similarity search - Function
Capsid protein VP1,Polyomavirus / Polyomavirus Vp1; Chain A / Capsid protein VP1,Polyomavirus / Polyomavirus capsid protein VP1 superfamily / Polyomavirus coat protein / Double-stranded DNA virus, group I, capsid / Sandwich / Mainly Beta
Similarity search - Domain/homology
Major capsid protein VP1
Similarity search - Component
Biological speciesJC polyomavirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsStroh, L.J. / Stehle, T.
CitationJournal: J.Virol. / Year: 2015
Title: Modulation of a Pore in the Capsid of JC Polyomavirus Reduces Infectivity and Prevents Exposure of the Minor Capsid Proteins.
Authors: Nelson, C.D. / Stroh, L.J. / Gee, G.V. / O'Hara, B.A. / Stehle, T. / Atwood, W.J.
History
DepositionSep 9, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Feb 18, 2015Provider: repository / Type: Initial release
Revision 1.1Mar 18, 2015Group: Database references
Revision 1.2Jan 10, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Major capsid protein VP1
B: Major capsid protein VP1
C: Major capsid protein VP1
D: Major capsid protein VP1
E: Major capsid protein VP1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,46426
Polymers150,7405
Non-polymers1,72421
Water15,727873
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area29150 Å2
ΔGint-117 kcal/mol
Surface area44170 Å2
MethodPISA
Unit cell
Length a, b, c (Å)149.340, 95.980, 128.510
Angle α, β, γ (deg.)90.00, 110.48, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E

NCS domain segments:

Ens-ID: 1 / Refine code: 4

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11VALVALVALVALAA26 - 299 - 12
21VALVALVALVALBB26 - 299 - 12
31VALVALVALVALCC26 - 299 - 12
41VALVALVALVALDD26 - 299 - 12
51VALVALVALVALEE26 - 299 - 12
12THRTHRASPASPAA31 - 5114 - 34
22THRTHRASPASPBB31 - 5114 - 34
32THRTHRASPASPCC31 - 5114 - 34
42THRTHRASPASPDD31 - 5114 - 34
52THRTHRASPASPEE31 - 5114 - 34
13HISHISPHEPHEAA53 - 5736 - 40
23HISHISPHEPHEBB53 - 5736 - 40
33HISHISPHEPHECC53 - 5736 - 40
43HISHISPHEPHEDD53 - 5736 - 40
53HISHISPHEPHEEE53 - 5736 - 40
14PROPROILEILEAA78 - 8561 - 68
24PROPROILEILEBB78 - 8561 - 68
34PROPROILEILECC78 - 8561 - 68
44PROPROILEILEDD78 - 8561 - 68
54PROPROILEILEEE78 - 8561 - 68
15METMETVALVALAA101 - 11184 - 94
25METMETVALVALBB101 - 11184 - 94
35METMETVALVALCC101 - 11184 - 94
45METMETVALVALDD101 - 11184 - 94
55METMETVALVALEE101 - 11184 - 94
16ALAALATHRTHRAA126 - 162109 - 145
26ALAALATHRTHRBB126 - 162109 - 145
36ALAALATHRTHRCC126 - 162109 - 145
46ALAALATHRTHRDD126 - 162109 - 145
56ALAALATHRTHREE126 - 162109 - 145
17ASNASNLEULEUAA173 - 189156 - 172
27ASNASNLEULEUBB173 - 189156 - 172
37ASNASNLEULEUCC173 - 189156 - 172
47ASNASNLEULEUDD173 - 189156 - 172
57ASNASNLEULEUEE173 - 189156 - 172
18ALAALATHRTHRAA194 - 205177 - 188
28ALAALATHRTHRBB194 - 205177 - 188
38ALAALATHRTHRCC194 - 205177 - 188
48ALAALATHRTHRDD194 - 205177 - 188
58ALAALATHRTHREE194 - 205177 - 188
19PHEPHEVALVALAA240 - 287223 - 270
29PHEPHEVALVALBB240 - 287223 - 270
39PHEPHEVALVALCC240 - 287223 - 270
49PHEPHEVALVALDD240 - 287223 - 270
59PHEPHEVALVALEE240 - 287223 - 270
110ILEILESERSERAA112 - 12295 - 105
210ILEILESERSERBB112 - 12295 - 105
310ILEILESERSERCC112 - 12295 - 105
410ILEILESERSERDD112 - 12295 - 105
510ILEILESERSEREE112 - 12295 - 105

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.439988, 0.854047, 0.277514), (-0.856603, 0.306408, 0.415144), (0.26952, -0.420378, 0.866396)11.23434, 20.21885, -5.60386
3given(-0.451411, 0.514804, 0.728838), (-0.527757, -0.812649, 0.247132), (0.719514, -0.273091, 0.63853)31.4349, 14.57475, -15.56504
4given(-0.443877, -0.535489, 0.718488), (0.520866, -0.806623, -0.279389), (0.729159, 0.250221, 0.636959)32.80703, -8.64556, -16.63044
5given(0.447828, -0.852525, 0.269539), (0.849033, 0.310943, -0.42715), (0.280345, 0.420137, 0.863071)13.51019, -17.83764, -6.85143

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Components

#1: Protein
Major capsid protein VP1 / Major structural protein VP1 / Mad-1 VP1


Mass: 30147.967 Da / Num. of mol.: 5 / Fragment: UNP residues 23-290 / Mutation: N221W
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) JC polyomavirus / Plasmid: 15b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P03089
#2: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C3H8O3
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 873 / 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 Matthews: 2.86 Å3/Da / Density % sol: 57.02 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 0.1 M HEPES pH 7.5, 0.2 M KSCN, 12% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 18, 2010
RadiationMonochromator: Bartels Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.8→50 Å / Num. obs: 155280 / % possible obs: 98.8 % / Redundancy: 4.1 % / Biso Wilson estimate: 30.7 Å2 / Net I/σ(I): 11.7
Reflection shellResolution: 1.8→1.85 Å / Mean I/σ(I) obs: 1.5 / % possible all: 88.5

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Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
Cootmodel building
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3NXG
Resolution: 1.8→50 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.961 / SU B: 4.773 / SU ML: 0.072 / Cross valid method: THROUGHOUT / ESU R: 0.096 / ESU R Free: 0.094 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.18584 7790 5 %RANDOM
Rwork0.15979 ---
obs0.16109 147490 98.82 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 26.921 Å2
Baniso -1Baniso -2Baniso -3
1-0.16 Å2-0 Å2-0.03 Å2
2--0.51 Å20 Å2
3----0.51 Å2
Refinement stepCycle: 1 / Resolution: 1.8→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10033 0 112 873 11018
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01910433
X-RAY DIFFRACTIONr_bond_other_d0.0010.029736
X-RAY DIFFRACTIONr_angle_refined_deg1.2691.95714162
X-RAY DIFFRACTIONr_angle_other_deg0.729322422
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.76351302
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.09724.085470
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.973151677
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.9221564
X-RAY DIFFRACTIONr_chiral_restr0.0730.21588
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02111812
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022408
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.7065.1095172
X-RAY DIFFRACTIONr_mcbond_other1.7055.1085171
X-RAY DIFFRACTIONr_mcangle_it2.1936.8586453
X-RAY DIFFRACTIONr_mcangle_other2.1936.8596454
X-RAY DIFFRACTIONr_scbond_it3.0796.1625261
X-RAY DIFFRACTIONr_scbond_other3.086.1625261
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.1627.9217699
X-RAY DIFFRACTIONr_long_range_B_refined6.31414.52212062
X-RAY DIFFRACTIONr_long_range_B_other6.31414.52512063
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Ens-ID: 1 / Number: 2598 / Refine-ID: X-RAY DIFFRACTION

Auth asym-IDTypeRms dev position (Å)Weight position
Amedium positional0.240.5
Bmedium positional0.290.5
Cmedium positional0.260.5
Dmedium positional0.280.5
Emedium positional0.270.5
Amedium thermal1.382
Bmedium thermal1.22
Cmedium thermal1.172
Dmedium thermal1.192
Emedium thermal1.182
LS refinement shellResolution: 1.8→1.847 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.361 503 -
Rwork0.342 9808 -
obs--88.49 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.8957-0.00630.66650.5002-0.15921.8582-0.06590.02520.06250.06610.0085-0.1066-0.10810.23070.05740.0497-0.003-0.01760.09360.01880.150460.38311.728518.846
20.5794-0.11140.14710.70950.12930.6479-0.01160.0548-0.003-0.0056-0.0056-0.0585-0.00290.08620.01710.0128-0.0202-0.02410.05110.0230.104157.72775.587218.58
34.16980.25523.95020.67590.3775.1614-0.1108-0.00140.08040.0449-0.0041-0.0401-0.16870.10360.11490.0155-0.0124-0.00240.02450.01930.091559.141612.13224.2431
48.38140.09634.45840.99940.55874.77880.0302-0.5582-0.05680.0812-0.0161-0.0388-0.174-0.233-0.0140.21970.0002-0.02750.1270.00540.208943.797230.256752.0065
50.8020.0687-0.12090.2639-0.14140.6354-0.0172-0.00270.10220.01590.0096-0.0001-0.143-0.01740.00760.05770.0074-0.04240.02740.0070.13537.841825.338325.1078
62.29590.87912.33280.99291.11774.1299-0.0239-0.0730.04980.05790.0117-0.024-0.12050.05330.01220.03960.0145-0.0180.03040.00750.129738.008325.888535.3415
73.57032.59944.01513.46752.79218.21910.1491-0.1175-0.09780.347-0.0119-0.09710.2759-0.0893-0.13720.14890.04580.02260.16-0.00270.179821.58795.623662.6403
80.4482-0.03060.15760.897-0.05430.4769-0.0017-0.02480.06380.04770.00830.0724-0.0654-0.133-0.00660.0190.0182-0.01980.0860.00490.121615.372211.428635.6591
90.76710.12010.93830.980.76724.776-0.02-0.07370.02480.11360.009-0.0203-0.1131-0.00650.0110.02440.0042-0.01430.04730.00210.126119.14587.109645.8388
100.7051-0.46321.12662.33451.367410.6172-0.0208-0.0628-0.05470.17220.0065-0.02220.23640.30670.01420.1057-0.0335-0.01580.15370.02540.18734.87-24.416755.8302
110.8336-0.1066-0.07740.38060.17090.62680.0087-0.0297-0.05260.01280.01670.06760.0842-0.0795-0.02530.0217-0.0188-0.03540.0470.01140.121620.6567-16.420833.3775
120.977-0.30040.83310.7313-0.75.4095-0.0347-0.1302-0.01380.0660.04050.0108-0.0109-0.0592-0.00580.0132-0.0046-0.01410.0416-0.00070.118127.9212-19.315540.6172
132.72810.37620.26731.9581-2.540210.865-0.0203-0.0988-0.04030.2292-0.1212-0.1197-0.24330.5620.14150.10470.0528-0.020.0898-0.03180.194365.2589-20.126141.6209
140.53640.21470.10820.4316-0.09510.68750.01040.0514-0.0676-0.0507-0.0073-0.01090.09280.0403-0.00310.02220.0135-0.02520.0393-0.01760.11545.8533-19.684421.0144
151.9185-0.76472.18461.2889-1.35433.76540.0154-0.0336-0.04180.03440.00480.01390.02940.0337-0.02020.00290.0015-0.00260.0257-0.01660.082553.4037-17.624827.2081
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A24 - 68
2X-RAY DIFFRACTION2A69 - 263
3X-RAY DIFFRACTION3A264 - 289
4X-RAY DIFFRACTION4B24 - 42
5X-RAY DIFFRACTION5B43 - 237
6X-RAY DIFFRACTION6B238 - 288
7X-RAY DIFFRACTION7C25 - 42
8X-RAY DIFFRACTION8C43 - 232
9X-RAY DIFFRACTION9C233 - 288
10X-RAY DIFFRACTION10D24 - 42
11X-RAY DIFFRACTION11D43 - 236
12X-RAY DIFFRACTION12D237 - 288
13X-RAY DIFFRACTION13E24 - 42
14X-RAY DIFFRACTION14E43 - 238
15X-RAY DIFFRACTION15E239 - 288

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