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- PDB-6t49: 3C-like protease from Southampton virus complexed with FMOPL000582a. -

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Basic information

Entry
Database: PDB / ID: 6t49
Title3C-like protease from Southampton virus complexed with FMOPL000582a.
Components(Genome polyprotein) x 2
KeywordsHYDROLASE / Viral protease.
Function / homology
Function and homology information


calicivirin / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / RNA helicase activity / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / proteolysis ...calicivirin / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / RNA helicase activity / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / proteolysis / RNA binding / ATP binding
Similarity search - Function
Viral polyprotein, Caliciviridae N-terminal / Viral polyprotein N-terminal / Norovirus 3C-like protease (NV 3CLpro) domain profile. / Norovirus peptidase C37 / Southampton virus-type processing peptidase / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / RNA-directed RNA polymerase, C-terminal domain ...Viral polyprotein, Caliciviridae N-terminal / Viral polyprotein N-terminal / Norovirus 3C-like protease (NV 3CLpro) domain profile. / Norovirus peptidase C37 / Southampton virus-type processing peptidase / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Chem-MH5 / PHOSPHATE ION / Genome polyprotein
Similarity search - Component
Biological speciesSouthampton virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.56 Å
AuthorsGuo, J. / Cooper, J.B.
CitationJournal: J Struct Biol X / Year: 2020
Title: In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors.
Authors: Guo, J. / Douangamath, A. / Song, W. / Coker, A.R. / Chan, A.W.E. / Wood, S.P. / Cooper, J.B. / Resnick, E. / London, N. / Delft, F.V.
History
DepositionOct 13, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 19, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 24, 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
A: Genome polyprotein
B: Genome polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,2358
Polymers36,5802
Non-polymers6556
Water3,801211
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, Structure suggests terameric.
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2770 Å2
ΔGint-2 kcal/mol
Surface area15060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.704, 89.303, 60.701
Angle α, β, γ (deg.)90.000, 96.520, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-391-

HOH

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein Genome polyprotein


Mass: 18387.350 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Southampton virus (serotype 3) / Gene: ORF1
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q04544, nucleoside-triphosphate phosphatase, calicivirin, RNA-directed RNA polymerase
#2: Protein Genome polyprotein


Mass: 18193.119 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Southampton virus (serotype 3) / Gene: ORF1
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q04544, nucleoside-triphosphate phosphatase, calicivirin, RNA-directed RNA polymerase

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Non-polymers , 4 types, 217 molecules

#3: Chemical ChemComp-MH5 / 3-[(5-methylthiophen-2-yl)methylamino]benzoic acid


Mass: 247.313 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C13H13NO2S / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 211 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.31 Å3/Da / Density % sol: 46.71 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 5.1
Details: Protein at concentration of 5 mg/ml or 10 mg/ml with 0.2 M ammonium citrate and 12% (v/v) PEG3350.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92819 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Oct 5, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92819 Å / Relative weight: 1
ReflectionResolution: 1.56→60.31 Å / Num. obs: 47120 / % possible obs: 99.8 % / Redundancy: 3.2 % / CC1/2: 0.998 / Rmerge(I) obs: 0.07 / Rpim(I) all: 0.046 / Rrim(I) all: 0.083 / Net I/σ(I): 7.2
Reflection shell

Diffraction-ID: 1 / % possible all: 99.8

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all
1.56-1.62.60.781.334730.4540.6040.991
6.98-60.313.30.0375530.9980.0230.044

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Processing

Software
NameVersionClassification
Aimless0.5.29data scaling
REFMAC5.8.0253refinement
PDB_EXTRACT3.25data extraction
xia2data reduction
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 6t1q

6t1q


Resolution: 1.56→60.31 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.954 / SU B: 5.292 / SU ML: 0.077 / SU R Cruickshank DPI: 0.0949 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.095 / ESU R Free: 0.089
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS ANISOTROPIC U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.221 2222 4.8 %RANDOM
Rwork0.1534 ---
obs0.1565 44479 98.85 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 128.25 Å2 / Biso mean: 23.361 Å2 / Biso min: 10.5 Å2
Baniso -1Baniso -2Baniso -3
1--0.42 Å2-0 Å2-0.01 Å2
2---0.25 Å2-0 Å2
3---0.66 Å2
Refinement stepCycle: final / Resolution: 1.56→60.31 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2564 0 38 211 2813
Biso mean--39.99 38.59 -
Num. residues----342
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0132701
X-RAY DIFFRACTIONr_bond_other_d0.0010.0172576
X-RAY DIFFRACTIONr_angle_refined_deg1.8371.6383673
X-RAY DIFFRACTIONr_angle_other_deg1.3971.575948
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.245352
X-RAY DIFFRACTIONr_dihedral_angle_2_deg26.30420.092109
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.31615432
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.7781518
X-RAY DIFFRACTIONr_chiral_restr0.0930.2359
X-RAY DIFFRACTIONr_gen_planes_refined0.010.023041
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02589
X-RAY DIFFRACTIONr_rigid_bond_restr3.35935277
LS refinement shellResolution: 1.56→1.6 Å / Rfactor Rfree error: 0
RfactorNum. reflection% reflection
Rfree0.392 179 -
Rwork0.367 3177 -
obs--96.27 %

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