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- PDB-5o05: GII.10 Vietnam 026 norovirus protruding domain in complex with Na... -

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Basic information

Entry
Database: PDB / ID: 5o05
TitleGII.10 Vietnam 026 norovirus protruding domain in complex with Nanobody Nano-42
Components
  • Capsid protein
  • Nanobody (VHH) Nano-42
KeywordsVIRAL PROTEIN / Norovirus / Protruding domain / capsid protein / Nanobody / VHH
Function / homology
Function and homology information


Positive stranded ssRNA viruses / Nucleoplasmin-like/VP (viral coat and capsid proteins) / Positive stranded ssRNA viruses / Calicivirus coat protein C-terminal / Calicivirus coat protein C-terminal / Calicivirus coat protein / Calicivirus coat protein / Elongation Factor Tu (Ef-tu); domain 3 / Picornavirus/Calicivirus coat protein / Viral coat protein subunit ...Positive stranded ssRNA viruses / Nucleoplasmin-like/VP (viral coat and capsid proteins) / Positive stranded ssRNA viruses / Calicivirus coat protein C-terminal / Calicivirus coat protein C-terminal / Calicivirus coat protein / Calicivirus coat protein / Elongation Factor Tu (Ef-tu); domain 3 / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / Immunoglobulins / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesVicugna pacos (alpaca)
Norwalk virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsKoromyslova, A.D. / Hansman, G.S.
CitationJournal: PLoS Pathog. / Year: 2017
Title: Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization.
Authors: Koromyslova, A.D. / Hansman, G.S.
History
DepositionMay 16, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 4, 2017Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Apr 10, 2019Group: Data collection / Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_variant
Revision 1.3Jan 17, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Nanobody (VHH) Nano-42
D: Nanobody (VHH) Nano-42
A: Capsid protein
B: Capsid protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,81343
Polymers95,3934
Non-polymers2,42139
Water7,458414
1


  • Idetical with deposited unit
  • defined by software
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15030 Å2
ΔGint91 kcal/mol
Surface area32150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)87.930, 105.360, 107.750
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Antibody Nanobody (VHH) Nano-42


Mass: 13189.652 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vicugna pacos (alpaca) / Plasmid: pHEN6C / Production host: Escherichia coli (E. coli) / Variant (production host): WK6
#2: Protein Capsid protein


Mass: 34506.660 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Norwalk virus / Variant: Vietnam 026 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5F4T5
#3: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 39 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 414 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.62 Å3/Da / Density % sol: 52.98 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / Details: 0.2 M potassium iodide, 20% (w/v) PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8729 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Jun 9, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8729 Å / Relative weight: 1
ReflectionResolution: 2→47.327 Å / Num. obs: 68217 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 4.497 % / Biso Wilson estimate: 28.38 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.09 / Rrim(I) all: 0.102 / Χ2: 1.051 / Net I/σ(I): 13.08
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2-2.124.6460.7422.15107750.7490.83898.8
2.12-2.274.6230.4993.16102760.8530.56499.9
2.27-2.454.5010.324.6496030.9230.36399.9
2.45-2.684.3320.2046.8688000.9670.23299.5
2.68-2.994.4070.12210.9380130.9880.13999.9
2.99-3.464.6580.07318.971080.9960.08299.9
3.46-4.234.5110.0431.3760920.9980.046100
4.23-5.954.1380.02939.8147550.9990.03399.5
5.95-47.3274.3920.02545.9827950.9990.02899.1

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation7.33 Å48.01 Å
Translation7.33 Å48.01 Å

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XSCALEdata scaling
PHASER2.5.6phasing
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3ONU and 4X4C
Resolution: 2→47.327 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 22.26
RfactorNum. reflection% reflection
Rfree0.2215 3409 5 %
Rwork0.1799 --
obs0.182 68128 99.68 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2→47.327 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6399 0 156 414 6969
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0096720
X-RAY DIFFRACTIONf_angle_d1.0829124
X-RAY DIFFRACTIONf_dihedral_angle_d12.3862350
X-RAY DIFFRACTIONf_chiral_restr0.0531019
X-RAY DIFFRACTIONf_plane_restr0.0061186
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9989-2.02750.32441360.27642589X-RAY DIFFRACTION97
2.0275-2.05770.33761390.26672653X-RAY DIFFRACTION100
2.0577-2.08990.28111410.25372669X-RAY DIFFRACTION100
2.0899-2.12420.29151400.23862677X-RAY DIFFRACTION100
2.1242-2.16080.26351400.23512656X-RAY DIFFRACTION100
2.1608-2.20010.27031420.22572689X-RAY DIFFRACTION100
2.2001-2.24240.26591420.22752683X-RAY DIFFRACTION100
2.2424-2.28820.26271400.21572670X-RAY DIFFRACTION100
2.2882-2.33790.23961390.20412648X-RAY DIFFRACTION100
2.3379-2.39230.21591430.20342714X-RAY DIFFRACTION100
2.3923-2.45210.24331420.19752677X-RAY DIFFRACTION100
2.4521-2.51840.2431390.19082653X-RAY DIFFRACTION99
2.5184-2.59250.22231410.18722667X-RAY DIFFRACTION100
2.5925-2.67620.21521410.18142690X-RAY DIFFRACTION100
2.6762-2.77180.22091430.18222703X-RAY DIFFRACTION100
2.7718-2.88280.21761410.18752677X-RAY DIFFRACTION100
2.8828-3.0140.2251430.1772725X-RAY DIFFRACTION100
3.014-3.17290.23531430.1762701X-RAY DIFFRACTION100
3.1729-3.37160.22971420.17482709X-RAY DIFFRACTION100
3.3716-3.63180.18961440.16742727X-RAY DIFFRACTION100
3.6318-3.99710.18411440.15172737X-RAY DIFFRACTION100
3.9971-4.57510.18471450.1372743X-RAY DIFFRACTION100
4.5751-5.76260.18941460.14652767X-RAY DIFFRACTION100
5.7626-47.33970.22631530.18132895X-RAY DIFFRACTION99
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)
15.6208-1.59570.70859.694-6.9365.00560.4468-0.8178-0.7017-0.3805-0.5387-0.27361.34010.05570.06930.4089-0.05560.09790.62410.49050.8564-32.0704-51.178842.6879
20.43280.5475-0.46381.1774-0.58430.52530.3382-1.1252-0.46340.4874-0.7665-0.3910.2291-0.01970.36250.5329-0.2429-0.07720.87290.21290.4209-32.2801-41.131650.2772
31.098-1.30870.6021.5671-0.77753.59110.6964-0.52771.35170.9007-0.4117-0.4327-0.3080.3613-0.25950.796-0.481-0.02911.6020.24680.8022-32.3748-31.544259.1887
40.08390.29960.72131.44041.91987.6060.3868-1.0628-0.95460.2034-0.3747-0.48520.44250.5557-0.03030.3715-0.1236-0.14581.24070.39370.7239-24.922-42.280551.6715
52.87921.0888-0.92032.225-2.23286.80160.1755-1.0609-0.33360.1469-0.2135-0.19510.0568-0.17870.01470.3429-0.09770.02180.56230.19030.4481-35.4603-43.030147.5241
63.9499-1.86382.6954.9147-3.70173.31030.59560.5696-1.1845-0.87160.11220.19312.49380.0211-0.64270.7396-0.0537-0.07020.6648-0.35910.9286-23.64-51.8103-18.5158
72.9565-4.4187-2.41998.73590.16877.66321.17880.90450.0805-1.5427-1.466-0.26071.8521.03770.2510.94310.0867-0.05811.20820.06940.4557-21.1463-45.5601-41.2891
85.7736-2.60351.14556.6397-1.12618.49161.25391.1651-0.8134-0.3911-0.17011.17580.6871-1.2209-1.13270.37950.0326-0.11370.7154-0.20950.8414-26.7346-46.9083-25.9029
95.8169-3.40170.74176.26620.92820.53640.32221.1202-0.54810.1932-0.65480.91640.4019-0.15640.2930.3242-0.0273-0.05160.5131-0.19660.5395-21.4887-42.1502-18.8656
104.57092.5541-6.42231.9311-3.60039.0455-0.17960.71081.0173-0.29130.44130.29040.2207-1.3861-0.24430.48120.19910.00180.86380.04420.4881-6.0869-43.5699-28.1216
112.538-2.55531.74765.97993.16538.34360.33551.5062-0.0213-0.9855-0.81690.1806-0.02990.07560.43910.44270.2-0.03080.7103-0.05120.3208-22.0309-34.9095-26.0802
122.9325-0.84542.29215.5977-1.1821.85070.3741.61950.5058-0.6245-0.37710.4123-0.3685-0.84510.08120.59620.2784-0.11651.1214-0.12880.4779-21.6634-40.9554-34.3074
133.3856-1.33952.2714.54770.15371.8044-0.04071.3714-0.72760.201-0.44430.57391.02170.2290.54340.41390.0420.01260.6237-0.26860.4437-18.3765-45.1295-21.1236
149.5809-3.2438-5.83572.39344.80289.7119-0.3625-0.2524-1.191-0.20070.1107-0.412.01820.23760.25310.587-0.00130.06660.2098-0.03170.439-20.5109-40.1086-4.2357
153.1808-0.18932.25454.6949-0.20838.60080.30621.1193-0.39480.0587-0.3070.30521.23070.3278-0.02240.38040.0974-0.01650.6314-0.26770.6027-16.7539-48.5113-24.05
161.8392-0.57910.23621.84080.56032.33640.01130.1378-0.1079-0.0975-0.0299-0.00720.24380.06180.02420.1854-0.01470.01920.1706-0.00770.183-18.3152-16.65681.4568
176.37541.74421.56795.31262.69411.8724-0.03560.13650.4113-0.17740.1574-0.6135-0.35050.6152-0.06750.2946-0.0927-0.00840.37340.00620.2789-5.85354.549813.552
181.8099-0.4809-0.6061.36480.5192.6853-0.024-0.09330.21550.05160.1278-0.3455-0.4010.5606-0.10060.2107-0.1083-0.03830.2843-0.01620.2653-7.24161.053513.8891
191.2326-0.06940.40251.92230.19442.28290.0610.18840.0483-0.26380.0071-0.3461-0.13240.3517-0.06150.1985-0.04720.06370.25060.00550.2095-12.3825-5.1444-1.6428
201.96570.23260.26044.33891.42224.3762-0.03760.176-0.1122-0.1112-0.06920.31830.2391-0.11010.09120.2151-0.02550.02260.1632-0.02590.1927-23.6173-24.257-3.8972
211.2662-0.1418-0.21521.6447-0.72142.4234-0.03750.07940.035-0.0230.03880.0848-0.0898-0.26110.00430.1515-0.01240.01780.165-0.01350.1546-32.8906-7.269718.5312
221.00510.0779-0.17381.21-0.54612.5030.0220.00010.13470.17590.02590.1035-0.335-0.1557-0.04990.22610.01350.00280.1718-0.0110.2086-31.72162.185519.8456
231.97470.77270.05524.0822-0.58853.75720.0344-0.2155-0.2190.0785-0.1381-0.3020.2890.13680.08490.20940.0010.01960.17390.03370.2232-25.03-24.114629.6514
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'C' and (resid 1 through 7 )
2X-RAY DIFFRACTION2chain 'C' and (resid 8 through 59 )
3X-RAY DIFFRACTION3chain 'C' and (resid 60 through 66 )
4X-RAY DIFFRACTION4chain 'C' and (resid 67 through 82 )
5X-RAY DIFFRACTION5chain 'C' and (resid 83 through 118 )
6X-RAY DIFFRACTION6chain 'D' and (resid 1 through 7 )
7X-RAY DIFFRACTION7chain 'D' and (resid 8 through 17 )
8X-RAY DIFFRACTION8chain 'D' and (resid 18 through 26 )
9X-RAY DIFFRACTION9chain 'D' and (resid 27 through 39 )
10X-RAY DIFFRACTION10chain 'D' and (resid 40 through 45 )
11X-RAY DIFFRACTION11chain 'D' and (resid 46 through 76 )
12X-RAY DIFFRACTION12chain 'D' and (resid 77 through 90 )
13X-RAY DIFFRACTION13chain 'D' and (resid 91 through 99 )
14X-RAY DIFFRACTION14chain 'D' and (resid 100 through 106 )
15X-RAY DIFFRACTION15chain 'D' and (resid 107 through 118 )
16X-RAY DIFFRACTION16chain 'A' and (resid 224 through 279 )
17X-RAY DIFFRACTION17chain 'A' and (resid 280 through 307 )
18X-RAY DIFFRACTION18chain 'A' and (resid 308 through 390 )
19X-RAY DIFFRACTION19chain 'A' and (resid 391 through 455 )
20X-RAY DIFFRACTION20chain 'A' and (resid 456 through 538 )
21X-RAY DIFFRACTION21chain 'B' and (resid 224 through 327 )
22X-RAY DIFFRACTION22chain 'B' and (resid 328 through 455 )
23X-RAY DIFFRACTION23chain 'B' and (resid 456 through 538 )

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