+Open data
-Basic information
Entry | Database: PDB / ID: 1p35 | ||||||
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Title | CRYSTAL STRUCTURE OF BACULOVIRUS P35 | ||||||
Components | P35 | ||||||
Keywords | APOPTOSIS / P35 / CELL DEATH / BACULOVIRUS | ||||||
Function / homology | Function and homology information symbiont-mediated suppression of host RNAi-mediated antiviral immune response / symbiont-mediated perturbation of host apoptosis / symbiont-mediated suppression of host apoptosis / cysteine-type endopeptidase inhibitor activity / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / virus-mediated perturbation of host defense response / negative regulation of apoptotic process / apoptotic process Similarity search - Function | ||||||
Biological species | Autographa californica nucleopolyhedrovirus | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.2 Å | ||||||
Authors | Fisher, A.J. / Delacruz, W.P. / Zoog, S.J. / Schneider, C.L. / Friesen, P.D. | ||||||
Citation | Journal: EMBO J. / Year: 1999 Title: Crystal structure of baculovirus P35: role of a novel reactive site loop in apoptotic caspase inhibition. Authors: Fisher, A.J. / Cruz, W. / Zoog, S.J. / Schneider, C.L. / Friesen, P.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p35.cif.gz | 191 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p35.ent.gz | 155.6 KB | Display | PDB format |
PDBx/mmJSON format | 1p35.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1p35_validation.pdf.gz | 401.6 KB | Display | wwPDB validaton report |
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Full document | 1p35_full_validation.pdf.gz | 421.5 KB | Display | |
Data in XML | 1p35_validation.xml.gz | 20.9 KB | Display | |
Data in CIF | 1p35_validation.cif.gz | 32.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p3/1p35 ftp://data.pdbj.org/pub/pdb/validation_reports/p3/1p35 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 34813.539 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Autographa californica nucleopolyhedrovirus Genus: Nucleopolyhedrovirus / Plasmid: BACULOVIRUS / Production host: Escherichia coli (E. coli) / References: UniProt: P08160 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 62 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 49 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: or batch | ||||||||||||||||||||||||||||||
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: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 66995 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Biso Wilson estimate: 41.6 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 14.1 |
Reflection | *PLUS Num. obs: 66997 / Num. measured all: 324073 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.2→30 Å / Rfactor Rfree error: 0.004 / Data cutoff high rms absF: 3350183.46 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
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Displacement parameters | Biso mean: 45.6 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Software | *PLUS Name: CNS / Version: 0.3 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 66997 / Rfactor Rfree: 0.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.292 |