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- PDB-5lkc: Protruding domain of GII.17 norovirus Kawasaki308 in complex with... -

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Basic information

Entry
Database: PDB / ID: 5lkc
TitleProtruding domain of GII.17 norovirus Kawasaki308 in complex with HBGA type A (triglycan)
ComponentsMajor capsid protein
KeywordsVIRAL PROTEIN / Norovirus / Virus capsid / HBGA / Protruding domain / P domain
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 / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Capsid protein VP1 / VP1
Similarity search - Component
Biological speciesNorovirus GII
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.81 Å
AuthorsSingh, B.K. / Morozov, V. / Hansman, G.S.
CitationJournal: Virology / Year: 2017
Title: Human norovirus inhibition by a human milk oligosaccharide.
Authors: Koromyslova, A. / Tripathi, S. / Morozov, V. / Schroten, H. / Hansman, G.S.
History
DepositionJul 22, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 24, 2017Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _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
B: Major capsid protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,98610
Polymers68,6302
Non-polymers1,3568
Water9,530529
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6400 Å2
ΔGint9 kcal/mol
Surface area23790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)75.870, 86.730, 97.440
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / End auth comp-ID: MET / End label comp-ID: MET

Dom-IDBeg auth comp-IDBeg label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1SERSERchain AAA224 - 5302 - 308
2GLYGLYchain BBB223 - 5301 - 308

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Components

#1: Protein Major capsid protein / Major viral capsid protein


Mass: 34315.203 Da / Num. of mol.: 2 / Fragment: P DOMAIN (UNP residues 225-530)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Norovirus GII / Gene: VP1 / Plasmid: MBP-HTSHP / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A0A0S1Z370, UniProt: A0A0E4B1P1*PLUS
#2: Polysaccharide alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]alpha-D-galactopyranose


Type: oligosaccharide / Mass: 529.490 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-2[DGalpNAca1-3]DGalpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,3,2/[a2112h-1a_1-5][a1221m-1a_1-5][a2112h-1a_1-5_2*NCC/3=O]/1-2-3/a2-b1_a3-c1WURCSPDB2Glycan 1.1.0
[][a-D-Galp]{[(2+1)][a-L-Fucp]{}[(3+1)][a-D-GalpNAc]{}}LINUCSPDB-CARE
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 529 / Source method: isolated from a natural source / Formula: H2O

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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: 2.35 Å3/Da / Density % sol: 47.6 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 / Details: Magnesium Chloride, PEG8000, Tris-HCl

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.9677 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 29, 2016
RadiationMonochromator: Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9677 Å / Relative weight: 1
ReflectionResolution: 1.76→48.72 Å / Num. obs: 64128 / % possible obs: 99.1 % / Observed criterion σ(I): -3 / Redundancy: 13.2 % / Biso Wilson estimate: 18.95 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.136 / Net I/σ(I): 15.27
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsCC1/2Diffraction-ID% possible all
1.76-1.81.1282.920.761194.2
1.8-1.850.9473.940.8821100
1.85-1.910.7675.160.9441100
1.91-1.960.6046.720.9691100
1.96-2.030.518.360.9821100
2.03-2.10.449.610.986199.5
2.1-2.180.34911.290.988199.5
2.18-2.270.27413.130.993199.2
2.27-2.370.23114.230.993198.6
2.37-2.490.19715.220.994196
2.49-2.620.18218.070.996199.6
2.62-2.780.14921.120.9971100
2.78-2.970.12123.910.9971100
2.97-3.210.09926.720.9981100
3.21-3.510.08529.480.9981100
3.51-3.930.07431.740.9981100
3.93-4.540.06933.460.9991100
4.54-5.560.06933.760.9981100
5.56-7.860.06932.780.9981100
7.860.07332.180.991199.2

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation7.34 Å48.72 Å
Translation7.34 Å48.72 Å

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHASER2.5.6phasing
PHENIXrefinement
PDB_EXTRACT3.2data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5F4O
Resolution: 1.81→48.72 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 18.01
RfactorNum. reflection% reflection
Rfree0.1829 2949 5 %
Rwork0.1526 --
obs0.1541 58952 99.49 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 100.21 Å2 / Biso mean: 26.3423 Å2 / Biso min: 9.8 Å2
Refinement stepCycle: final / Resolution: 1.81→48.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4757 0 90 529 5376
Biso mean--45.11 30.95 -
Num. residues----611
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0055059
X-RAY DIFFRACTIONf_angle_d1.0076921
X-RAY DIFFRACTIONf_chiral_restr0.04758
X-RAY DIFFRACTIONf_plane_restr0.005924
X-RAY DIFFRACTIONf_dihedral_angle_d12.2441836
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3500X-RAY DIFFRACTION5.7TORSIONAL
12B3500X-RAY DIFFRACTION5.7TORSIONAL
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.81-1.83970.33151400.3022652X-RAY DIFFRACTION100
1.8397-1.87140.28721380.23632632X-RAY DIFFRACTION100
1.8714-1.90540.21221380.21022611X-RAY DIFFRACTION100
1.9054-1.94210.19871410.17672678X-RAY DIFFRACTION100
1.9421-1.98170.21721390.16122646X-RAY DIFFRACTION100
1.9817-2.02480.20541390.15582643X-RAY DIFFRACTION100
2.0248-2.07190.19741390.15532647X-RAY DIFFRACTION100
2.0719-2.12370.18071390.15032628X-RAY DIFFRACTION99
2.1237-2.18120.20021390.14852642X-RAY DIFFRACTION100
2.1812-2.24530.18151390.14132651X-RAY DIFFRACTION99
2.2453-2.31780.16431390.14092630X-RAY DIFFRACTION99
2.3178-2.40070.15081370.14092611X-RAY DIFFRACTION98
2.4007-2.49680.1771340.14342543X-RAY DIFFRACTION96
2.4968-2.61040.18551410.15092673X-RAY DIFFRACTION100
2.6104-2.7480.19931410.1532683X-RAY DIFFRACTION100
2.748-2.92020.18911410.15092678X-RAY DIFFRACTION100
2.9202-3.14560.1781420.14942703X-RAY DIFFRACTION100
3.1456-3.46210.18241420.14612697X-RAY DIFFRACTION100
3.4621-3.96280.181440.13752740X-RAY DIFFRACTION100
3.9628-4.9920.13621450.12332747X-RAY DIFFRACTION100
4.992-48.720.18061520.16962868X-RAY DIFFRACTION100
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)
12.1858-0.26840.20881.56590.49312.22420.0421-0.09480.12920.0135-0.082-0.0629-0.0596-0.04860.02970.1119-0.03420.03420.0994-0.03040.1466-38.597512.57693.5655
22.23550.53531.23321.56731.1723.50160.0486-0.0042-0.00240.0069-0.11960.20780.0608-0.19390.03940.1057-0.00350.01660.1241-0.02310.1781-52.78261.2502-9.8837
31.467-0.0468-0.53653.74480.87951.5674-0.00360.0506-0.0305-0.2143-0.10750.0627-0.0153-0.09830.11070.05770.0122-0.01950.1094-0.00970.0556-47.4929-2.5114-16.1357
41.2927-0.1022-0.03612.19940.83621.20180.05710.1020.1681-0.2019-0.11280.0782-0.1317-0.14340.04540.1130.02250.00040.13090.00090.1175-49.74667.8957-16.3996
50.59690.1428-0.28421.05220.0062.37510.0298-0.08780.2020.0829-0.10240.1023-0.054-0.03560.05360.0912-0.02270.01610.1374-0.0330.1931-38.460714.98860.5695
65.27170.5642-1.88462.7390.53063.06850.0457-0.48010.1590.18240.0912-0.44660.08470.1599-0.10080.1889-0.022-0.02550.2094-0.0850.2096-34.235114.856516.6791
72.6263-0.79930.48662.127-0.1282.5880.00190.10980.0712-0.05810.0298-0.4863-0.21190.2049-0.01610.1528-0.06190.02690.1643-0.08770.2938-33.798921.49148.1668
83.0845-1.0401-1.15125.86532.12093.3906-0.1032-0.31930.46310.16840.1583-0.2251-0.0667-0.018-0.01790.1406-0.0325-0.0360.2593-0.09270.2249-36.475620.972417.2474
91.5533-0.5718-0.1441.5826-0.69342.12750.1378-0.25720.08420.1883-0.05130.0377-0.1025-0.0438-0.05070.17-0.0580.00390.14610.00110.1179-38.4712-8.32285.3247
103.58782.76430.3353.0103-0.09350.7825-0.06510.1851-0.2498-0.0082-0.0341-0.31840.37680.09420.07950.26670.01350.04150.16690.04580.1726-30.5021-19.5870.577
112.23680.2838-1.06721.7353-0.80782.84720.06630.08420.0769-0.0707-0.1525-0.32610.09180.23510.05950.1170.02590.02930.14940.05690.2373-20.5132-0.8906-9.9862
120.96710.14660.3221.5505-0.16641.16660.0270.06340.0977-0.0323-0.1295-0.04530.02840.14720.10630.0860.01230.05450.15070.04780.1355-25.84382.85-15.3501
131.2372-0.25750.09891.6786-0.44581.02240.05150.11-0.0742-0.1683-0.173-0.21550.19520.20640.11680.15980.0390.06310.16010.03790.1523-23.4823-7.1442-16.1871
141.09680.24540.33121.38010.06311.75480.0926-0.0945-0.15230.1667-0.1353-0.12440.29480.05120.01260.1843-0.02530.02830.12240.02830.1385-35.2661-14.8927-0.1573
152.8709-0.21721.16692.9421-0.57962.59430.2211-0.4135-0.27350.3855-0.03960.27110.0218-0.1517-0.1750.2705-0.10170.02770.26460.06130.1386-40.0725-15.701516.1387
162.7631-0.4178-0.38922.8009-0.78822.27320.06790.0081-0.21970.0625-0.06360.13480.3752-0.19340.01240.2696-0.10460.0020.16470.02490.1968-39.9585-21.82467.3431
172.5572-0.96351.55395.0521-2.58483.45420.1081-0.301-0.37120.2003-0.15650.09740.4165-0.00750.04820.3905-0.12530.03550.2980.09080.1927-37.7689-21.146916.4113
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 224 through 268 )A224 - 268
2X-RAY DIFFRACTION2chain 'A' and (resid 269 through 319 )A269 - 319
3X-RAY DIFFRACTION3chain 'A' and (resid 320 through 347 )A320 - 347
4X-RAY DIFFRACTION4chain 'A' and (resid 348 through 422 )A348 - 422
5X-RAY DIFFRACTION5chain 'A' and (resid 423 through 464 )A423 - 464
6X-RAY DIFFRACTION6chain 'A' and (resid 465 through 484 )A465 - 484
7X-RAY DIFFRACTION7chain 'A' and (resid 485 through 513 )A485 - 513
8X-RAY DIFFRACTION8chain 'A' and (resid 514 through 530 )A514 - 530
9X-RAY DIFFRACTION9chain 'B' and (resid 223 through 247 )B223 - 247
10X-RAY DIFFRACTION10chain 'B' and (resid 248 through 268 )B248 - 268
11X-RAY DIFFRACTION11chain 'B' and (resid 269 through 319 )B269 - 319
12X-RAY DIFFRACTION12chain 'B' and (resid 320 through 347 )B320 - 347
13X-RAY DIFFRACTION13chain 'B' and (resid 348 through 422 )B348 - 422
14X-RAY DIFFRACTION14chain 'B' and (resid 423 through 464 )B423 - 464
15X-RAY DIFFRACTION15chain 'B' and (resid 465 through 484 )B465 - 484
16X-RAY DIFFRACTION16chain 'B' and (resid 485 through 513 )B485 - 513
17X-RAY DIFFRACTION17chain 'B' and (resid 514 through 530 )B514 - 530

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