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- PDB-6t2i: 3C-like protease from Southampton virus complexed with FMOPL000157a. -

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Basic information

Entry
Database: PDB / ID: 6t2i
Title3C-like protease from Southampton virus complexed with FMOPL000157a.
Components(Genome polyprotein) x 2
KeywordsHYDROLASE / Viral protease.
Function / homology
Function and homology information


calicivirin / host cell Golgi membrane / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / RNA helicase activity / host cell endoplasmic reticulum membrane / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity ...calicivirin / host cell Golgi membrane / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / RNA helicase activity / host cell endoplasmic reticulum membrane / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / proteolysis / RNA binding / ATP binding / metal ion binding / membrane
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
N-(2-phenylethyl)methanesulfonamide / Genome polyprotein
Similarity search - Component
Biological speciesSouthampton virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.61 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 8, 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

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Assembly

Deposited unit
A: Genome polyprotein
B: Genome polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,0524
Polymers36,7752
Non-polymers2772
Water4,774265
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, Structure suggests may be tetrameric.
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2060 Å2
ΔGint-11 kcal/mol
Surface area15590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.739, 89.450, 60.907
Angle α, β, γ (deg.)90.000, 96.920, 90.000
Int Tables number5
Space group name H-MC121

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Components

#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: 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
#3: Chemical ChemComp-JFM / N-(2-phenylethyl)methanesulfonamide


Mass: 199.270 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H13NO2S / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 265 / Source method: isolated from a natural source / Formula: H2O
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: 46.68 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.1
Details: 0.2 M ammonium citrate, 12% (v/v) PEG3350. Protein concentration = 4 mg/ml.

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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: 1.61→51.11 Å / Num. obs: 43021 / % possible obs: 99.8 % / Redundancy: 3.1 % / CC1/2: 0.998 / Rmerge(I) obs: 0.054 / Rpim(I) all: 0.036 / Rrim(I) all: 0.065 / Net I/σ(I): 8.3
Reflection shellResolution: 1.61→1.65 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.756 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 3176 / CC1/2: 0.621 / Rpim(I) all: 0.596 / Rrim(I) all: 0.967 / % possible all: 99.7

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Processing

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

6t1q


Resolution: 1.61→51.11 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.953 / SU B: 7.002 / SU ML: 0.098 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.113 / ESU R Free: 0.105
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : ANISOTROPIC REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2378 2124 5 %RANDOM
Rwork0.154 ---
obs0.1581 40305 98.32 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 145.8 Å2 / Biso mean: 28.674 Å2 / Biso min: 14.81 Å2
Baniso -1Baniso -2Baniso -3
1-0.81 Å2-0 Å2-0.13 Å2
2---0.46 Å2-0 Å2
3----0.31 Å2
Refinement stepCycle: final / Resolution: 1.61→51.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2577 0 17 265 2859
Biso mean--34.08 45.22 -
Num. residues----344
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0132668
X-RAY DIFFRACTIONr_bond_other_d0.0010.0172548
X-RAY DIFFRACTIONr_angle_refined_deg1.8731.6423623
X-RAY DIFFRACTIONr_angle_other_deg1.3541.5695885
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.6635344
X-RAY DIFFRACTIONr_dihedral_angle_2_deg27.28820.092109
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.91315427
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.9461518
X-RAY DIFFRACTIONr_chiral_restr0.0890.2357
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.022970
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02580
X-RAY DIFFRACTIONr_rigid_bond_restr3.51735216
LS refinement shellResolution: 1.61→1.652 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.373 148 -
Rwork0.388 2863 -
all-3011 -
obs--94.66 %

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