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Open data
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Basic information
Entry | Database: PDB / ID: 1adv | ||||||
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Title | EARLY E2A DNA-BINDING PROTEIN | ||||||
![]() | ADENOVIRUS SINGLE-STRANDED DNA-BINDING PROTEIN | ||||||
![]() | DNA BINDING PROTEIN / DNA-BINDING PROTEIN / SSDNA BINDING PROTEIN | ||||||
Function / homology | ![]() viral DNA strand displacement replication / viral DNA genome replication / DNA duplex unwinding / DNA unwinding involved in DNA replication / positive regulation of DNA replication / viral capsid / single-stranded DNA binding / DNA-templated transcription / host cell nucleus / DNA binding ...viral DNA strand displacement replication / viral DNA genome replication / DNA duplex unwinding / DNA unwinding involved in DNA replication / positive regulation of DNA replication / viral capsid / single-stranded DNA binding / DNA-templated transcription / host cell nucleus / DNA binding / zinc ion binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kanellopoulos, P.N. / Tsernoglou, D. / Van Der Vliet, P.C. / Tucker, P.A. | ||||||
![]() | ![]() Title: Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein. Authors: Kanellopoulos, P.N. / Tsernoglou, D. / van der Vliet, P.C. / Tucker, P.A. #1: ![]() Title: Crystal Structure of the Adenovirus DNA Binding Protein Reveals a Hook-on Model for Cooperative DNA Binding Authors: Tucker, P.A. / Tsernoglou, D. / Tucker, A.D. / Coenjaerts, F.E. / Leenders, H. / Van Der Vliet, P.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 123.1 KB | Display | ![]() |
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PDB format | ![]() | 95.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.9 KB | Display | ![]() |
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Full document | ![]() | 438.5 KB | Display | |
Data in XML | ![]() | 22.1 KB | Display | |
Data in CIF | ![]() | 29.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Details | THE MOLECULES FORM AN INFINITE CHAIN ALONG THE CRYSTALLOGRAPHIC Z AXIS. PAIRS OF MOLECULES IN THE CHAIN ARE RELATED BY A CRYSTALLOGRAPHIC SCREW AXIS. |
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Components
#1: Protein | Mass: 39899.746 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN, RESIDUES 174 - 529 / Source method: isolated from a natural source / Details: SECOND CRYSTAL FORM, DATA COLLECTED AT 100 K / Source: (natural) ![]() ![]() #2: Chemical | ChemComp-ZN / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.29 % | |||||||||||||||
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Crystal grow | *PLUS 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 | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 10, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→25 Å / Num. obs: 13965 / % possible obs: 98.3 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.083 |
Reflection | *PLUS Num. measured all: 42619 |
Reflection shell | *PLUS Highest resolution: 3.2 Å / Lowest resolution: 3.6 Å / Rmerge(I) obs: 0.236 |
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Processing
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Refinement | Resolution: 3.2→6 Å / σ(F): 0
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Displacement parameters | Biso mean: 17.44 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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