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Yorodumi- PDB-1nju: Complex structure of HCMV Protease and a peptidomimetic inhibitor -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nju | ||||||
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Title | Complex structure of HCMV Protease and a peptidomimetic inhibitor | ||||||
Components | Assemblin | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / Protease / Peptidomimetic Inhibitor / Induced-fit / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information assemblin / viral release from host cell / host cell cytoplasm / serine-type endopeptidase activity / host cell nucleus / proteolysis / identical protein binding Similarity search - Function | ||||||
Biological species | Human herpesvirus 5 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Khayat, R. / Batra, R. / Qian, C. / Halmos, T. / Bailey, M. / Tong, L. | ||||||
Citation | Journal: Biochemistry / Year: 2003 Title: Structural and Biochemical Studies of Inhibitor Binding to Human Cytomegalovirus Protease Authors: Khayat, R. / Batra, R. / Qian, C. / Halmos, T. / Bailey, M. / Tong, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nju.cif.gz | 193.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nju.ent.gz | 154.4 KB | Display | PDB format |
PDBx/mmJSON format | 1nju.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1nju_validation.pdf.gz | 686.8 KB | Display | wwPDB validaton report |
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Full document | 1nju_full_validation.pdf.gz | 727.4 KB | Display | |
Data in XML | 1nju_validation.xml.gz | 25.1 KB | Display | |
Data in CIF | 1nju_validation.cif.gz | 35.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nj/1nju ftp://data.pdbj.org/pub/pdb/validation_reports/nj/1nju | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 28130.547 Da / Num. of mol.: 4 / Mutation: A143Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 5 / Gene: UL80, APNG / Production host: Escherichia coli (E. coli) / References: UniProt: P16753, assemblin #2: Chemical | ChemComp-0FP / Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 717.939 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C37H63N7O7 Details: Residue peptide of the Peptidomimetic Inhibitor was chemically synthesized. References: N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~4~,N~4~-dimethyl-N~1~-[(1R)-1-methyl-2,3-dioxo-3-{[(1S)-1- phenylpropyl]amino}propyl]-L-aspartamide Nonpolymer details | THE INHIBITOR 0FP IS COVALENTLY CONNECTED AT CARBON C4 TO THE ACTIVE SITE SERINES (A 132, B 432, C ...THE INHIBITOR 0FP IS COVALENTLY | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.07 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 6, 2001 |
Radiation | Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. all: 32973 / Num. obs: 32973 / % possible obs: 95.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 36.2 Å2 |
Reflection shell | Resolution: 2.7→2.8 Å / % possible all: 93.5 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 30 Å / Num. measured all: 143394 / Rmerge(I) obs: 0.07 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→25.88 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 2089328.8 / Data cutoff high rms absF: 2089328.8 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 16.5992 Å2 / ksol: 0.323366 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→25.88 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: CONSTR | ||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.7→2.87 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 20 Å / Rfactor Rfree: 0.271 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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