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- PDB-1ied: CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUM... -

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Basic information

Entry
Database: PDB / ID: 1ied
TitleCRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE
ComponentsCAPSID PROTEIN P40: ASSEMBLIN PROTEASE
KeywordsHYDROLASE / COAT PROTEIN / SERINE PROTEASE / CATALYTIC TRIAD / VIRAL PROTEASE
Function / homology
Function and homology information


assemblin / nuclear capsid assembly / viral release from host cell / host cell cytoplasm / serine-type endopeptidase activity / host cell nucleus / proteolysis / identical protein binding
Similarity search - Function
Serine Protease, Human Cytomegalovirus Protease; Chain A / Herpesvirus/Caudovirus protease domain / Peptidase S21 / Herpesvirus protease superfamily / Assemblin (Peptidase family S21) / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
Capsid scaffolding protein
Similarity search - Component
Biological speciesHuman herpesvirus 5
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsKhayat, R. / Batra, R. / Massariol, M.J. / Lagace, L. / Tong, L.
CitationJournal: Biochemistry / Year: 2001
Title: Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease.
Authors: Khayat, R. / Batra, R. / Massariol, M.J. / Lagace, L. / Tong, L.
History
DepositionApr 9, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 6, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Oct 27, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Feb 7, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CAPSID PROTEIN P40: ASSEMBLIN PROTEASE
B: CAPSID PROTEIN P40: ASSEMBLIN PROTEASE


Theoretical massNumber of molelcules
Total (without water)56,2432
Polymers56,2432
Non-polymers00
Water3,549197
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3050 Å2
ΔGint-15 kcal/mol
Surface area19060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.200, 76.200, 170.600
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein CAPSID PROTEIN P40: ASSEMBLIN PROTEASE / HCMV PROTEASE


Mass: 28121.514 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-256 / Mutation: A143Q, H157E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human herpesvirus 5 / Genus: Cytomegalovirus / Strain: AD169 / Gene: UL80 / Production host: Escherichia coli (E. coli) / References: UniProt: P16753, assemblin
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 197 / 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: 2.2 Å3/Da / Density % sol: 44.1 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 21% PEG3350, 0.1M MES 6.0, 15% GLYCEROL, 5% t-BuOH, 0.4M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Crystal grow
*PLUS
Temperature: 21 ℃ / pH: 5
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
114 mg/mlprotein1drop
220 mM1dropNaOAc
380 mM1dropNaCl
419-21 %PEG33501reservoir
50.1 MMES1reservoir
615 %glycerol1reservoir
75 %tert-butyl alcohol1reservoir
80.3-0.4 M1reservoirNaCl

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 32-ID / Wavelength: 0.9876 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Oct 20, 1999
RadiationMonochromator: Diamond 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9876 Å / Relative weight: 1
ReflectionResolution: 2→30 Å / Num. all: 34845 / Num. obs: 31009 / % possible obs: 87 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.07 % / Biso Wilson estimate: 12.6 Å2 / Rmerge(I) obs: 0.097 / Net I/σ(I): 14.5
Reflection shellResolution: 2→2.07 Å / Redundancy: 2.107 % / Rmerge(I) obs: 0.284 / % possible all: 77.6
Reflection
*PLUS
Num. measured all: 136174

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Processing

Software
NameVersionClassification
GLRFphasing
CNS1refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→29.23 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 2047854.29 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.269 2329 7.7 %RANDOM
Rwork0.226 ---
all0.226 32381 --
obs0.226 30313 87 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 52.6 Å2 / ksol: 0.371 e/Å3
Displacement parametersBiso mean: 29.6 Å2
Baniso -1Baniso -2Baniso -3
1--3.94 Å20 Å20 Å2
2---3.94 Å20 Å2
3---7.88 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.3 Å0.25 Å
Luzzati d res low-5 Å
Luzzati sigma a0.23 Å0.21 Å
Refinement stepCycle: LAST / Resolution: 2→29.23 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3421 0 0 197 3618
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.006
X-RAY DIFFRACTIONc_angle_deg1.2
X-RAY DIFFRACTIONc_dihedral_angle_d22.3
X-RAY DIFFRACTIONc_improper_angle_d0.95
X-RAY DIFFRACTIONc_mcbond_it1.531.5
X-RAY DIFFRACTIONc_mcangle_it2.522
X-RAY DIFFRACTIONc_scbond_it1.952
X-RAY DIFFRACTIONc_scangle_it2.862.5
LS refinement shellResolution: 2→2.13 Å / Rfactor Rfree error: 0.017 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.287 293 7.3 %
Rwork0.264 3711 -
obs-4004 70.5 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refinement
*PLUS
σ(F): 1 / % reflection Rfree: 7.7 %
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 29.6 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_angle_deg1.2
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg22.3
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.95
X-RAY DIFFRACTIONc_mcbond_it1.5
X-RAY DIFFRACTIONc_scbond_it2
X-RAY DIFFRACTIONc_mcangle_it2
X-RAY DIFFRACTIONc_scangle_it2.5
LS refinement shell
*PLUS
Rfactor Rfree: 0.287 / % reflection Rfree: 7.3 % / Rfactor Rwork: 0.264

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