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Open data
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Basic information
Entry | Database: PDB / ID: 1tfr | ||||||
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Title | RNASE H FROM BACTERIOPHAGE T4 | ||||||
![]() | T4 RNASE H | ||||||
![]() | HYDROLASE / 5U-3U EXONUCLEASE / RNA:RNA / DNA:DNA / METAL-DEPENDENT / MAGNESIUM-CONTAINING / HYDROLASE (NUCLEIC ACID) | ||||||
Function / homology | ![]() DNA replication, Okazaki fragment processing / 5'-3' RNA exonuclease activity / 5'-flap endonuclease activity / DNA replication, removal of RNA primer / ribonuclease H / RNA-DNA hybrid ribonuclease activity / DNA binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Mueser, T.C. / Nossal, N.G. / Hyde, C.C. | ||||||
![]() | ![]() Title: Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins. Authors: Mueser, T.C. / Nossal, N.G. / Hyde, C.C. #1: ![]() Title: Purification of Bacteriophage T4 DNA Replication Proteins Authors: Nossal, N.G. / Hinton, D.M. / Hobbs, L.J. / Spacciapoli, P. #2: ![]() Title: Bacteriophage T4 Encodes an Rnase H which Removes RNA Primers Made by the T4 Replication System in Vitro Authors: Hollingsworth, H.C. / Nossal, N.G. #3: ![]() Title: Organization of the Bacteriophage T4 Genome between Map Positions 150.745 And 145.824 Authors: Hahn, S. / Ruger, W. #4: ![]() Title: The Region of Phage T4 Genes 34, 33 and 59: Primary Structures and Organization on the Genome Authors: Hahn, S. / Kruse, U. / Ruger, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 74.8 KB | Display | ![]() |
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PDB format | ![]() | 55.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.5 KB | Display | ![]() |
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Full document | ![]() | 421.9 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 20.8 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
#1: Protein | Mass: 35610.914 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: TWO OCTAHEDRALLY-COORDINATED MG2+ IONS IN ACTIVE SITE Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Oct 18, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.06→6 Å / Num. obs: 22706 / % possible obs: 93.6 % / Observed criterion σ(I): 0 / Redundancy: 2.58 % / Rmerge(I) obs: 0.05 |
Reflection | *PLUS Num. measured all: 58561 |
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Processing
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Refinement | Resolution: 2.06→6 Å / σ(F): 2
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Displacement parameters | Biso mean: 31.98 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.21 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.06→6 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.205 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |