+Open data
-Basic information
Entry | Database: PDB / ID: 1r6n | ||||||
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Title | HPV11 E2 TAD complex crystal structure | ||||||
Components | HPV11 REGULATORY PROTEIN E2 | ||||||
Keywords | TRANSCRIPTION / REPLICATION / Papillomavirus / E2 TAD / TAD / X-ray structure | ||||||
Function / homology | Function and homology information viral DNA genome replication / regulation of DNA replication / DNA replication / DNA-binding transcription factor activity / nucleotide binding / DNA-templated transcription / host cell nucleus / DNA binding Similarity search - Function | ||||||
Biological species | Human papillomavirus type 11 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Wang, Y. / Coulombe, R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Crystal Structure of the E2 Transactivation Domain of Human Papillomavirus Type 11 Bound to a Protein Interaction Inhibitor Authors: Wang, Y. / Coulombe, R. / Cameron, D.R. / Thauvette, L. / Massariol, M.-J. / Amon, L.M. / Fink, D. / Titolo, S. / Welchner, E. / Yoakim, C. / Archambault, J. / White, P.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1r6n.cif.gz | 57.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1r6n.ent.gz | 40.2 KB | Display | PDB format |
PDBx/mmJSON format | 1r6n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r6/1r6n ftp://data.pdbj.org/pub/pdb/validation_reports/r6/1r6n | HTTPS FTP |
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-Related structure data
Related structure data | 1r6kSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 24434.838 Da / Num. of mol.: 1 / Fragment: TRANSACTIVATION DOMAIN (RESIDUES 2-201) Source method: isolated from a genetically manipulated source Details: inhibited form / Source: (gene. exp.) Human papillomavirus type 11 / Genus: Alphapapillomavirus / Species: Human papillomavirus - 6 / Gene: E2 / Production host: Escherichia coli (E. coli) / Strain (production host): B834 / References: UniProt: P04015 | ||||||
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#2: Chemical | #3: Chemical | ChemComp-ALQ / | #4: Chemical | ChemComp-DMS / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.14 Å3/Da / Density % sol: 60.6 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5 Details: Na Citrate, MPD, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.5 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
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: X25 / Wavelength: 1 Å |
Detector | Type: BRANDEIS - B4 / Detector: CCD / Date: Mar 1, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. all: 11028 / Num. obs: 10792 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.44 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 27.47 |
Reflection shell | Resolution: 2.4→2.49 Å / Rmerge(I) obs: 0.474 / Mean I/σ(I) obs: 2.01 / Num. unique all: 964 / % possible all: 86.4 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 11028 / Num. measured all: 70999 |
Reflection shell | *PLUS % possible obs: 86.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: HPV11 E2 TAb apo (1R6K) Resolution: 2.4→50 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 60.61 Å2 | |||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 50 Å / Rfactor Rwork: 0.21 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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