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Entry
Database: PDB / ID: 7h8r
TitleGroup deposition for crystallographic fragment screening of Chikungunya virus nsP3 macrodomain -- Crystal structure of Chikungunya virus nsP3 macrodomain in complex with Z218760918 (CHIKV_MacB-x1288)
ComponentsNon-structural protein 3
KeywordsVIRAL PROTEIN / Diamond Light Source / I04-1 / READDI / Chikungunya Virus / crystallographic fragment screening / PanDDA / XChemExplorer
Function / homology
Function and homology information


host cell filopodium / ADP-ribose 1''-phosphate phosphatase / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / polynucleotide adenylyltransferase / poly(A) RNA polymerase activity / mRNA modification / regulation of cytoskeleton organization ...host cell filopodium / ADP-ribose 1''-phosphate phosphatase / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / polynucleotide adenylyltransferase / poly(A) RNA polymerase activity / mRNA modification / regulation of cytoskeleton organization / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / 7-methylguanosine mRNA capping / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / cysteine-type peptidase activity / Transferases; Transferring one-carbon groups; Methyltransferases / host cell cytoplasmic vesicle membrane / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / nucleoside-triphosphate phosphatase / methylation / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host innate immune response / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / GTP binding / host cell plasma membrane / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding
Similarity search - Function
: / Tomato mosaic virus helicase, N-terminal domain / Alphavirus nsp2 protease (nsp2pro) domain / Alphavirus nsP2 protease domain superfamily / : / : / Peptidase family C9 / Non-structural protein 3, zinc-binding domain / Alphavirus nsp2 protease (nsp2pro) domain profile. / Viral methyltransferase ...: / Tomato mosaic virus helicase, N-terminal domain / Alphavirus nsp2 protease (nsp2pro) domain / Alphavirus nsP2 protease domain superfamily / : / : / Peptidase family C9 / Non-structural protein 3, zinc-binding domain / Alphavirus nsp2 protease (nsp2pro) domain profile. / Viral methyltransferase / Alphavirus-like methyltransferase (MT) domain / Alphavirus-like methyltransferase (MT) domain profile. / Tymovirus, RNA-dependent RNA polymerase / RNA dependent RNA polymerase / Viral (Superfamily 1) RNA helicase / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Non-structural protein 3, X-domain-like / Macro domain / Appr-1"-p processing enzyme / Macro domain / Macro domain profile. / Macro domain-like / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
1,2-benzoxazol-3-amine / Polyprotein P1234
Similarity search - Component
Biological speciesChikungunya virus
Chikungunya Virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.53 Å
AuthorsAschenbrenner, J.C. / Fairhead, M. / Godoy, A.S. / Balcomb, B.H. / Capkin, E. / Chandran, A.V. / Dolci, I. / Golding, M. / Koekemoer, L. / Lithgo, R.M. ...Aschenbrenner, J.C. / Fairhead, M. / Godoy, A.S. / Balcomb, B.H. / Capkin, E. / Chandran, A.V. / Dolci, I. / Golding, M. / Koekemoer, L. / Lithgo, R.M. / Marples, P.G. / Ni, X. / Oliva, G. / Thompson, W. / Tomlinson, C.W.E. / Wild, C. / Winokan, M. / Xavier, M.-A.E. / Fearon, D. / von Delft, F.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)U19AI171292 United States
CitationJournal: To Be Published
Title: Group deposition for crystallographic fragment screening of Chikungunya virus nsP3 macrodomain
Authors: Aschenbrenner, J.C. / Fairhead, M. / Godoy, A.S. / Balcomb, B.H. / Capkin, E. / Chandran, A.V. / Dolci, I. / Golding, M. / Koekemoer, L. / Lithgo, R.M. / Marples, P.G. / Ni, X. / Oliva, G. / ...Authors: Aschenbrenner, J.C. / Fairhead, M. / Godoy, A.S. / Balcomb, B.H. / Capkin, E. / Chandran, A.V. / Dolci, I. / Golding, M. / Koekemoer, L. / Lithgo, R.M. / Marples, P.G. / Ni, X. / Oliva, G. / Thompson, W. / Tomlinson, C.W.E. / Wild, C. / Winokan, M. / Xavier, M.-A.E. / Fearon, D. / von Delft, F.
History
DepositionApr 26, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 29, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Non-structural protein 3
B: Non-structural protein 3
C: Non-structural protein 3
D: Non-structural protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,82435
Polymers71,2774
Non-polymers2,54731
Water10,160564
1
A: Non-structural protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,80512
Polymers17,8191
Non-polymers98611
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Non-structural protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,2597
Polymers17,8191
Non-polymers4396
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Non-structural protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,1676
Polymers17,8191
Non-polymers3485
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Non-structural protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,59310
Polymers17,8191
Non-polymers7749
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)87.613, 87.613, 85.695
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number144
Space group name H-MP31

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Non-structural protein 3 / nsP3


Mass: 17819.215 Da / Num. of mol.: 4 / Fragment: macrodomain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chikungunya virus / Production host: Escherichia coli (E. coli)
References: UniProt: Q8JUX6, ADP-ribose 1''-phosphate phosphatase

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Non-polymers , 5 types, 595 molecules

#2: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Formula: C2H6OS / Source: (gene. exp.) Chikungunya Virus / Production host: Escherichia coli (E. coli) / Comment: DMSO, precipitant*YM
#3: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C4H12NO3 / Source: (gene. exp.) Chikungunya Virus / Production host: Escherichia coli (E. coli) / Comment: pH buffer*YM
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
Formula: Cl / Source: (gene. exp.) Chikungunya Virus / Production host: Escherichia coli (E. coli)
#5: Chemical
ChemComp-HLR / 1,2-benzoxazol-3-amine


Mass: 134.135 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C7H6N2O / Source: (gene. exp.) Chikungunya Virus / Production host: Escherichia coli (E. coli) / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 564 / 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: 2.66 Å3/Da / Density % sol: 53.83 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.8
Details: 0.1 M Potassium thiocyanate, 0.1 M Sodium bromide, 0.1 M Tris, pH 7.8, 25 % PEG Smear Broad

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92124 Å
DetectorType: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Nov 21, 2023
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92124 Å / Relative weight: 1
ReflectionResolution: 1.53→75.83 Å / Num. obs: 111025 / % possible obs: 99.9 % / Redundancy: 10.3 % / CC1/2: 0.998 / Rmerge(I) obs: 0.084 / Rpim(I) all: 0.027 / Rrim(I) all: 0.088 / Χ2: 0.36 / Net I/σ(I): 12 / Num. measured all: 1144206
Reflection shellResolution: 1.53→1.56 Å / % possible obs: 97.1 % / Redundancy: 8.3 % / Rmerge(I) obs: 2.789 / Num. measured all: 44537 / Num. unique obs: 5385 / CC1/2: 0.272 / Rpim(I) all: 1.03 / Rrim(I) all: 2.977 / Χ2: 0.07 / Net I/σ(I) obs: 0.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
REFMAC5refinement
Aimlessdata scaling
PHASERphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.53→75.88 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.96 / SU B: 3.53 / SU ML: 0.114 / Cross valid method: THROUGHOUT / ESU R: 0.107 / ESU R Free: 0.104 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22253 5515 5.1 %RANDOM
Rwork0.18433 ---
obs0.18621 102851 97.58 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 31.189 Å2
Baniso -1Baniso -2Baniso -3
1-0.22 Å20.11 Å20 Å2
2--0.22 Å20 Å2
3----0.7 Å2
Refinement stepCycle: 1 / Resolution: 1.53→75.88 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4962 0 147 564 5673
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0159447
X-RAY DIFFRACTIONr_bond_other_d0.0010.0146917
X-RAY DIFFRACTIONr_angle_refined_deg1.5371.6519837
X-RAY DIFFRACTIONr_angle_other_deg1.3271.60816003
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.1755986
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.9120.253356
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.387151318
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.361572
X-RAY DIFFRACTIONr_chiral_restr0.0780.2894
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.029248
X-RAY DIFFRACTIONr_gen_planes_other0.0030.021736
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.8113.0255203
X-RAY DIFFRACTIONr_mcbond_other2.0222.9944172
X-RAY DIFFRACTIONr_mcangle_it2.8764.3874692
X-RAY DIFFRACTIONr_mcangle_other2.8764.3864691
X-RAY DIFFRACTIONr_scbond_it2.9893.5214244
X-RAY DIFFRACTIONr_scbond_other2.9883.5224245
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.7694.9745146
X-RAY DIFFRACTIONr_long_range_B_refined7.87637.2629410
X-RAY DIFFRACTIONr_long_range_B_other7.72236.7989031
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.53→1.57 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.42 284 -
Rwork0.41 5800 -
obs--73.91 %

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