+Open data
-Basic information
Entry | Database: PDB / ID: 1cmv | ||||||
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Title | HUMAN CYTOMEGALOVIRUS PROTEASE | ||||||
Components | HUMAN CYTOMEGALOVIRUS PROTEASE | ||||||
Keywords | SERINE PROTEASE / COAT PROTEIN / HYDROLASE / PHOSPHORYLATION | ||||||
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 / MIR / Resolution: 2.27 Å | ||||||
Authors | Shieh, H.-S. / Kurumbail, R.G. / Stevens, A.M. / Stegeman, R.A. / Sturman, E.J. / Pak, J.Y. / Wittwer, A.J. / Palmier, M.O. / Wiegand, R.C. / Holwerda, B.C. / Stallings, W.C. | ||||||
Citation | Journal: Nature / Year: 1996 Title: Three-dimensional structure of human cytomegalovirus protease. Authors: Shieh, H.S. / Kurumbail, R.G. / Stevens, A.M. / Stegeman, R.A. / Sturman, E.J. / Pak, J.Y. / Wittwer, A.J. / Palmier, M.O. / Wiegand, R.C. / Holwerda, B.C. / Stallings, W.C. #1: Journal: J.Biol.Chem. / Year: 1994 Title: Activity of Two-Chain Recombinant Human Cytomegalovirus Protease Authors: Holwerda, B.C. / Wittwer, A.J. / Duffin, K.L. / Smith, C. / Toth, M.V. / Carr, L.S. / Wiegand, R.C. / Bryant, M.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cmv.cif.gz | 106.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cmv.ent.gz | 83.1 KB | Display | PDB format |
PDBx/mmJSON format | 1cmv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cm/1cmv ftp://data.pdbj.org/pub/pdb/validation_reports/cm/1cmv | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 28071.480 Da / Num. of mol.: 2 / Mutation: V141A, A144P Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 5 / Genus: Cytomegalovirus / Plasmid: PMON9059 / Production host: Escherichia coli (E. coli) References: UniProt: P16753, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases #2: Water | ChemComp-HOH / | |
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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: 2.2 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 28-30% MONOMETHYL POLYETHYLENE GLYCOL 550 0.05-0.2 M NACL 10% GLYCEROL 50 MM HEPES AT PH 7.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 296 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 24, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.27→40 Å / Num. obs: 23705 / % possible obs: 94.5 % / Observed criterion σ(I): -1.5 / Redundancy: 12.5 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 17.38 |
Reflection shell | Resolution: 2.26→2.34 Å / Rmerge(I) obs: 0.411 / Mean I/σ(I) obs: 1.81 / % possible all: 75.7 |
Reflection | *PLUS Num. measured all: 297289 |
Reflection shell | *PLUS % possible obs: 75.7 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.27→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 26 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.27→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.311 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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