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- PDB-1vpt: AS11 VARIANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vpt | ||||||
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Title | AS11 VARIANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE | ||||||
![]() | VP39 | ||||||
![]() | METHYLTRANSFERASE / RNA CAP / POLY(A) POLYMERASE / VACCINIA | ||||||
Function / homology | ![]() regulation of mRNA 3'-end processing / 7-methylguanosine mRNA capping / translation elongation factor activity / virion component / methyltransferase cap1 / mRNA (nucleoside-2'-O-)-methyltransferase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hodel, A.E. / Gershon, P.D. / Shi, X. / Quiocho, F.A. | ||||||
![]() | ![]() Title: The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends. Authors: Hodel, A.E. / Gershon, P.D. / Shi, X. / Quiocho, F.A. #1: ![]() Title: Methyltransferase-Specific Domains within Vp39, a Bifunctional Enzyme which Participates in the Modification of Both Mrna Ends Authors: Shi, X. / Yao, P. / Jose, T. / Gershon, P.D. #2: ![]() Title: Mutational Analysis of a Multifunctional Protein, with Mrna 5' CAP-Specific (Nucleoside-2'-O-)-Methyltransferase and 3'-Adenylyltransferase Stimulatory Activities, Encoded by Vaccinia Virus Authors: Schnierle, B.S. / Gershon, P.D. / Moss, B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.8 KB | Display | ![]() |
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PDB format | ![]() | 57.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 689.3 KB | Display | ![]() |
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Full document | ![]() | 693.1 KB | Display | |
Data in XML | ![]() | 15 KB | Display | |
Data in CIF | ![]() | 21.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 39925.895 Da / Num. of mol.: 1 / Mutation: AS11 VARIANT (R140A, K142A, R143A) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P07617, polynucleotide adenylyltransferase |
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#2: Chemical | ChemComp-SAM / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||||||
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Crystal grow | pH: 4.5 / Details: pH 4.5 | ||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MAC Science DIP-2030 / Detector: IMAGE PLATE / Date: Dec 13, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→15 Å / Num. obs: 33404 / % possible obs: 98 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 39.8 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 6.2 / % possible all: 88.6 |
Reflection | *PLUS Num. measured all: 208238 / Rmerge(I) obs: 0.05 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 28.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |