[English] 日本語
Yorodumi
- PDB-8j3t: Complex structure of human cytomegalovirus protease and a non-cov... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8j3t
TitleComplex structure of human cytomegalovirus protease and a non-covalent small-molecule ligand
ComponentsAssemblin
KeywordsHYDROLASE / 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
Peptidase S21 / Herpesvirus protease superfamily / Assemblin (Peptidase family S21)
Similarity search - Domain/homology
Chem-T1F / Capsid scaffolding protein
Similarity search - Component
Biological speciesHuman betaherpesvirus 5
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsYoshida, S. / Sako, Y. / Nikaido, E. / Ueda, T. / Kozono, I. / Ichihashi, Y. / Nakahashi, A. / Onishi, M. / Yamatsu, Y. / Kato, T. ...Yoshida, S. / Sako, Y. / Nikaido, E. / Ueda, T. / Kozono, I. / Ichihashi, Y. / Nakahashi, A. / Onishi, M. / Yamatsu, Y. / Kato, T. / Nishikawa, J. / Tachibana, Y.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Acs Med.Chem.Lett. / Year: 2023
Title: Peptide-to-Small Molecule: Discovery of Non-Covalent, Active-Site Inhibitors of beta-Herpesvirus Proteases.
Authors: Yoshida, S. / Sako, Y. / Nikaido, E. / Ueda, T. / Kozono, I. / Ichihashi, Y. / Nakahashi, A. / Onishi, M. / Yamatsu, Y. / Kato, T. / Nishikawa, J. / Tachibana, Y.
History
DepositionApr 18, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 8, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 29, 2023Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Assemblin
B: Assemblin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)59,6374
Polymers58,2612
Non-polymers1,3762
Water181
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3190 Å2
ΔGint-19 kcal/mol
Surface area17630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.364, 76.364, 215.030
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

-
Components

#1: Protein Assemblin / Protease


Mass: 29130.686 Da / Num. of mol.: 2 / Mutation: A143Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human betaherpesvirus 5 / Gene: UL80 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0G2TMR2, assemblin
#2: Chemical ChemComp-T1F / (4R)-1-[1-[(S)-[1-cyclopentyl-3-(2-methylphenyl)pyrazol-4-yl]-(4-methylphenyl)methyl]-2-oxidanylidene-pyridin-3-yl]-3-methyl-2-oxidanylidene-N-(3-oxidanylidene-2-azabicyclo[2.2.2]octan-4-yl)imidazolidine-4-carboxamide


Mass: 687.830 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C40H45N7O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.69 Å3/Da / Density % sol: 54.28 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: 0.05 M MES pH 5.5, 0.6 M NaCl, 0.097 M ammonium acetate, 0.005 M MgSO4

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 13, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→71.96 Å / Num. obs: 16515 / % possible obs: 99.9 % / Redundancy: 13 % / CC1/2: 0.999 / Rmerge(I) obs: 0.121 / Net I/σ(I): 15.2
Reflection shellResolution: 2.8→2.95 Å / Num. unique obs: 2345 / CC1/2: 0.959

-
Processing

Software
NameVersionClassification
REFMAC5.8.0218refinement
XDSdata scaling
XDSdata reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→71.96 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.871 / SU B: 19.829 / SU ML: 0.366 / Cross valid method: THROUGHOUT / ESU R: 1.01 / ESU R Free: 0.434 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.30945 743 5 %RANDOM
Rwork0.22426 ---
obs0.22864 14107 99.81 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 76.361 Å2
Baniso -1Baniso -2Baniso -3
1-5.29 Å2-0 Å2-0 Å2
2--5.29 Å2-0 Å2
3----10.58 Å2
Refinement stepCycle: 1 / Resolution: 2.9→71.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3082 0 102 1 3185
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0193261
X-RAY DIFFRACTIONr_bond_other_d0.0020.022946
X-RAY DIFFRACTIONr_angle_refined_deg1.7552.0094457
X-RAY DIFFRACTIONr_angle_other_deg0.8936749
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.2255405
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.55122.366131
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.31215447
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.9121529
X-RAY DIFFRACTIONr_chiral_restr0.0830.2496
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0213689
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02706
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_it5.6327.9321649
X-RAY DIFFRACTIONr_mcbond_other5.637.9291646
X-RAY DIFFRACTIONr_mcangle_it8.60911.862045
X-RAY DIFFRACTIONr_mcangle_other8.60611.862045
X-RAY DIFFRACTIONr_scbond_it5.2918.1451612
X-RAY DIFFRACTIONr_scbond_other5.298.1461613
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other8.1912.1022413
X-RAY DIFFRACTIONr_long_range_B_refined11.93193.9853691
X-RAY DIFFRACTIONr_long_range_B_other11.92993.9933692
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.9→2.975 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.478 47 -
Rwork0.376 1010 -
obs--100 %

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more