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- PDB-4v5t: X-ray structure of the Grapevine Fanleaf virus -

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Basic information

Entry
Database: PDB / ID: 4v5t
TitleX-ray structure of the Grapevine Fanleaf virus
ComponentsCOAT PROTEIN
KeywordsVIRUS / FANLEAF DISEASE
Function / homology
Function and homology information


transport of virus in host, cell to cell / host cell plasmodesma / viral capsid / host cell cytoplasm / host cell nucleus / structural molecule activity
Similarity search - Function
Nepovirus subgroup A, RNA2 polyprotein, Protein 2A / Nepovirus subgroup A polyprotein / Nepovirus coat protein / Nepovirus coat protein, C-terminal / Nepovirus coat protein, N-terminal / Nepovirus coat protein, central domain / Nepovirus coat protein, C-terminal domain / Nepovirus coat protein, N-terminal domain / Viral coat protein subunit
Similarity search - Domain/homology
Biological speciesGRAPEVINE FANLEAF VIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsSchellenberger, P. / Sauter, C. / Lorber, B. / Bron, P. / Trapani, S. / Bergdoll, M. / Marmonier, A. / Schmitt-Keichinger, C. / Lemaire, O. / Demangeat, G. / Ritzenthaler, C.
Citation
Journal: Plos Pathog. / Year: 2011
Title: Structural Insights Into Viral Determinants of Nematode Mediated Grapevine Fanleaf Virus Transmission.
Authors: Schellenberger, P. / Sauter, C. / Lorber, B. / Bron, P. / Trapani, S. / Bergdoll, M. / Marmonier, A. / Schmitt-Keichinger, C. / Lemaire, O. / Demangeat, G. / Ritzenthaler, C.
#1: Journal: J.Struct.Biol. / Year: 2011
Title: Strategies for the Crystallization of Viruses: Using Phase Diagrams and Gels to Produce 3D Crystals of Grapevine Fanleaf Virus.
Authors: Schellenberger, P. / Demangeat, G. / Lemaire, O. / Ritzenthaler, C. / Bergdoll, M. / Olieric, V. / Sauter, C. / Lorber, B.
History
DepositionFeb 1, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 9, 2014Provider: repository / Type: Initial release
SupersessionDec 10, 2014ID: 2Y7T, 2Y7U, 2Y7V
Revision 1.1Dec 10, 2014Group: Other
Revision 1.2Mar 6, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.temp / _pdbx_database_status.date_author_approval / _pdbx_database_status.recvd_author_approval
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.4Jan 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
AA: COAT PROTEIN
AB: COAT PROTEIN
AC: COAT PROTEIN
AD: COAT PROTEIN
AE: COAT PROTEIN
AF: COAT PROTEIN
AG: COAT PROTEIN
AH: COAT PROTEIN
AI: COAT PROTEIN
AJ: COAT PROTEIN
AK: COAT PROTEIN
AL: COAT PROTEIN
AM: COAT PROTEIN
AN: COAT PROTEIN
AO: COAT PROTEIN
AP: COAT PROTEIN
AQ: COAT PROTEIN
AR: COAT PROTEIN
AS: COAT PROTEIN
AT: COAT PROTEIN
BA: COAT PROTEIN
BB: COAT PROTEIN
BC: COAT PROTEIN
BD: COAT PROTEIN
BE: COAT PROTEIN
BF: COAT PROTEIN
BG: COAT PROTEIN
BH: COAT PROTEIN
BI: COAT PROTEIN
BJ: COAT PROTEIN
BK: COAT PROTEIN
BL: COAT PROTEIN
BM: COAT PROTEIN
BN: COAT PROTEIN
BO: COAT PROTEIN
BP: COAT PROTEIN
BQ: COAT PROTEIN
BR: COAT PROTEIN
BS: COAT PROTEIN
BT: COAT PROTEIN
CA: COAT PROTEIN
CB: COAT PROTEIN
CC: COAT PROTEIN
CD: COAT PROTEIN
CE: COAT PROTEIN
CF: COAT PROTEIN
CG: COAT PROTEIN
CH: COAT PROTEIN
CI: COAT PROTEIN
CJ: COAT PROTEIN
CK: COAT PROTEIN
CL: COAT PROTEIN
CM: COAT PROTEIN
CN: COAT PROTEIN
CO: COAT PROTEIN
CP: COAT PROTEIN
CQ: COAT PROTEIN
CR: COAT PROTEIN
CS: COAT PROTEIN
CT: COAT PROTEIN


Theoretical massNumber of molelcules
Total (without water)3,364,38860
Polymers3,364,38860
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)279.400, 279.600, 293.300
Angle α, β, γ (deg.)102.40, 116.40, 108.20
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101
111
121
131
141
151
161
171
181
191
201
211
221
231
241
251
261
271
281
291
301
311
321
331
341
351
361
371
381
391
401
411
421
431
441
451
461
471
481
491
501
511
521
531
541
551
561
571
581
591
601

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN AA
211CHAIN AB
311CHAIN AC
411CHAIN AD
511CHAIN AE
611CHAIN AF
711CHAIN AG
811CHAIN AH
911CHAIN AI
1011CHAIN AJ
1111CHAIN AK
1211CHAIN AL
1311CHAIN AM
1411CHAIN AN
1511CHAIN AO
1611CHAIN AP
1711CHAIN AQ
1811CHAIN AR
1911CHAIN AS
2011CHAIN AT
2111CHAIN BA
2211CHAIN BB
2311CHAIN BC
2411CHAIN BD
2511CHAIN BE
2611CHAIN BF
2711CHAIN BG
2811CHAIN BH
2911CHAIN BI
3011CHAIN BJ
3111CHAIN BK
3211CHAIN BL
3311CHAIN BM
3411CHAIN BN
3511CHAIN BO
3611CHAIN BP
3711CHAIN BQ
3811CHAIN BR
3911CHAIN BS
4011CHAIN BT
4111CHAIN CA
4211CHAIN CB
4311CHAIN CC
4411CHAIN CD
4511CHAIN CE
4611CHAIN CF
4711CHAIN CG
4811CHAIN CH
4911CHAIN CI
5011CHAIN CJ
5111CHAIN CK
5211CHAIN CL
5311CHAIN CM
5411CHAIN CN
5511CHAIN CO
5611CHAIN CP
5711CHAIN CQ
5811CHAIN CR
5911CHAIN CS
6011CHAIN CT

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Components

#1: Protein ...
COAT PROTEIN / 2C-CP


Mass: 56073.141 Da / Num. of mol.: 60 / Source method: isolated from a natural source / Source: (natural) GRAPEVINE FANLEAF VIRUS / Strain: GFLV-F13 / References: UniProt: P18474

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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: 5.27 Å3/Da / Density % sol: 76.66 % / Description: NONE
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: CRYSTALS OF GFLV-F13 WERE GROWN AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 2.2 MG/ML AND A RESERVOIR CONTAINING 4% (M/V) PEG 3350, 0.1 M HEPES NA PH 7.5 ...Details: CRYSTALS OF GFLV-F13 WERE GROWN AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 2.2 MG/ML AND A RESERVOIR CONTAINING 4% (M/V) PEG 3350, 0.1 M HEPES NA PH 7.5 AND 0.2% (M/V) AGAROSE.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.98
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 24, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 3→135.426 Å / Num. obs: 1214112 / % possible obs: 88.1 % / Observed criterion σ(I): 0 / Redundancy: 2 % / Biso Wilson estimate: 36.31 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 9.2
Reflection shellResolution: 3→3.08 Å / Redundancy: 2 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2.5 / % possible all: 71.7

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Processing

Software
NameVersionClassification
AMoREmodel building
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XSCALEdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2Y26
Resolution: 3→135.426 Å / SU ML: 0.32 / σ(F): 0 / Phase error: 19.44 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2073 60925 5 %
Rwork0.1902 --
obs0.1911 1214112 88.26 %
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 5.791 Å2 / ksol: 0.332 e/Å3
Displacement parametersBiso mean: 36.27 Å2
Baniso -1Baniso -2Baniso -3
1-0.628 Å2-0.5939 Å22.5481 Å2
2---5.1409 Å25.1099 Å2
3---5.5261 Å2
Refinement stepCycle: LAST / Resolution: 3→135.426 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms79020 0 0 0 79020
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01243480
X-RAY DIFFRACTIONf_angle_d1.195331140
X-RAY DIFFRACTIONf_dihedral_angle_d14.53986520
X-RAY DIFFRACTIONf_chiral_restr0.07736900
X-RAY DIFFRACTIONf_plane_restr0.00542060
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11AA3951X-RAY DIFFRACTIONPOSITIONAL
12AB3951X-RAY DIFFRACTIONPOSITIONAL0.081
13AC3951X-RAY DIFFRACTIONPOSITIONAL0.083
14AD3951X-RAY DIFFRACTIONPOSITIONAL0.089
15AE3951X-RAY DIFFRACTIONPOSITIONAL0.089
16AF3951X-RAY DIFFRACTIONPOSITIONAL0.079
17AG3951X-RAY DIFFRACTIONPOSITIONAL0.09
18AH3951X-RAY DIFFRACTIONPOSITIONAL0.104
19AI3951X-RAY DIFFRACTIONPOSITIONAL0.09
110AJ3951X-RAY DIFFRACTIONPOSITIONAL0.107
111AK3951X-RAY DIFFRACTIONPOSITIONAL0.108
112AL3951X-RAY DIFFRACTIONPOSITIONAL0.29
113AM3951X-RAY DIFFRACTIONPOSITIONAL0.09
114AN3951X-RAY DIFFRACTIONPOSITIONAL0.105
115AO3951X-RAY DIFFRACTIONPOSITIONAL0.122
116AP3951X-RAY DIFFRACTIONPOSITIONAL0.245
117AQ3951X-RAY DIFFRACTIONPOSITIONAL0.098
118AR3951X-RAY DIFFRACTIONPOSITIONAL0.124
119AS3951X-RAY DIFFRACTIONPOSITIONAL0.098
120AT3951X-RAY DIFFRACTIONPOSITIONAL0.086
121BA3951X-RAY DIFFRACTIONPOSITIONAL0.085
122BB3951X-RAY DIFFRACTIONPOSITIONAL0.1
123BC3951X-RAY DIFFRACTIONPOSITIONAL0.077
124BD3951X-RAY DIFFRACTIONPOSITIONAL0.091
125BE3951X-RAY DIFFRACTIONPOSITIONAL0.079
126BF3951X-RAY DIFFRACTIONPOSITIONAL0.096
127BG3951X-RAY DIFFRACTIONPOSITIONAL0.084
128BH3951X-RAY DIFFRACTIONPOSITIONAL0.09
129BI3951X-RAY DIFFRACTIONPOSITIONAL0.108
130BJ3951X-RAY DIFFRACTIONPOSITIONAL0.11
131BK3951X-RAY DIFFRACTIONPOSITIONAL0.099
132BL3951X-RAY DIFFRACTIONPOSITIONAL0.291
133BM3951X-RAY DIFFRACTIONPOSITIONAL0.107
134BN3951X-RAY DIFFRACTIONPOSITIONAL0.095
135BO3951X-RAY DIFFRACTIONPOSITIONAL0.095
136BP3951X-RAY DIFFRACTIONPOSITIONAL0.252
137BQ3951X-RAY DIFFRACTIONPOSITIONAL0.104
138BR3951X-RAY DIFFRACTIONPOSITIONAL0.13
139BS3951X-RAY DIFFRACTIONPOSITIONAL0.1
140BT3951X-RAY DIFFRACTIONPOSITIONAL0.089
141CA3951X-RAY DIFFRACTIONPOSITIONAL0.097
142CB3951X-RAY DIFFRACTIONPOSITIONAL0.084
143CC3951X-RAY DIFFRACTIONPOSITIONAL0.081
144CD3951X-RAY DIFFRACTIONPOSITIONAL0.085
145CE3951X-RAY DIFFRACTIONPOSITIONAL0.077
146CF3951X-RAY DIFFRACTIONPOSITIONAL0.1
147CG3951X-RAY DIFFRACTIONPOSITIONAL0.107
148CH3951X-RAY DIFFRACTIONPOSITIONAL0.094
149CI3951X-RAY DIFFRACTIONPOSITIONAL0.085
150CJ3951X-RAY DIFFRACTIONPOSITIONAL0.102
151CK3951X-RAY DIFFRACTIONPOSITIONAL0.106
152CL3951X-RAY DIFFRACTIONPOSITIONAL0.289
153CM3951X-RAY DIFFRACTIONPOSITIONAL0.105
154CN3951X-RAY DIFFRACTIONPOSITIONAL0.086
155CO3951X-RAY DIFFRACTIONPOSITIONAL0.104
156CP3951X-RAY DIFFRACTIONPOSITIONAL0.238
157CQ3951X-RAY DIFFRACTIONPOSITIONAL0.099
158CR3951X-RAY DIFFRACTIONPOSITIONAL0.172
159CS3951X-RAY DIFFRACTIONPOSITIONAL0.09
160CT3951X-RAY DIFFRACTIONPOSITIONAL0.079
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3-3.03410.352514090.321427561X-RAY DIFFRACTION63
3.0341-3.06980.331418360.303834332X-RAY DIFFRACTION79
3.0698-3.10720.306618170.291334828X-RAY DIFFRACTION80
3.1072-3.14660.307718350.288434935X-RAY DIFFRACTION80
3.1466-3.1880.292519270.271635680X-RAY DIFFRACTION82
3.188-3.23160.290219050.273634942X-RAY DIFFRACTION81
3.2316-3.27780.296817520.267634579X-RAY DIFFRACTION79
3.2778-3.32680.27819610.249636804X-RAY DIFFRACTION84
3.3268-3.37870.256620480.238837208X-RAY DIFFRACTION86
3.3787-3.43410.254319980.229237846X-RAY DIFFRACTION87
3.4341-3.49340.253319800.227638341X-RAY DIFFRACTION88
3.4934-3.55690.240520920.212538352X-RAY DIFFRACTION89
3.5569-3.62530.233720570.213338400X-RAY DIFFRACTION88
3.6253-3.69930.226121190.206639055X-RAY DIFFRACTION90
3.6993-3.77980.206520130.188539189X-RAY DIFFRACTION90
3.7798-3.86770.197820800.181839492X-RAY DIFFRACTION91
3.8677-3.96440.195421130.173739854X-RAY DIFFRACTION92
3.9644-4.07160.18321420.163239968X-RAY DIFFRACTION92
4.0716-4.19140.164120570.145640378X-RAY DIFFRACTION92
4.1914-4.32670.160422260.142240291X-RAY DIFFRACTION93
4.3267-4.48140.144221400.130840614X-RAY DIFFRACTION93
4.4814-4.66080.146522180.13340788X-RAY DIFFRACTION94
4.6608-4.87290.149621140.134241075X-RAY DIFFRACTION94
4.8729-5.12990.1521760.139241265X-RAY DIFFRACTION95
5.1299-5.45130.174221160.159241026X-RAY DIFFRACTION94
5.4513-5.87220.186521620.169740996X-RAY DIFFRACTION94
5.8722-6.46310.179421420.166340981X-RAY DIFFRACTION94
6.4631-7.39830.164321100.156341299X-RAY DIFFRACTION95
7.3983-9.32070.17122160.158241574X-RAY DIFFRACTION95
9.3207-135.56460.229121640.228641534X-RAY DIFFRACTION95

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