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- PDB-6hak: Crystal structure of HIV-1 reverse transcriptase (RT) in complex ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6hak | |||||||||
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Title | Crystal structure of HIV-1 reverse transcriptase (RT) in complex with a double stranded RNA represents the RT transcription initiation complex prior to nucleotide incorporation | |||||||||
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Function / homology | ![]() : / : / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Das, K. / Martinez, S.E. / Arnold, E. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of HIV-1 RT/dsRNA initiation complex prior to nucleotide incorporation. Authors: Das, K. / Martinez, S.E. / DeStefano, J.J. / Arnold, E. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 447.7 KB | Display | ![]() |
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PDB format | ![]() | 351.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5txlS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein , 2 types, 4 molecules ACBD
#1: Protein | Mass: 64022.414 Da / Num. of mol.: 2 / Mutation: Q258C, C280S, D498N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: gag-pol / Production host: ![]() ![]() ![]() References: UniProt: P03366, HIV-1 retropepsin, RNA-directed DNA polymerase, DNA-directed DNA polymerase, retroviral ribonuclease H, exoribonuclease H, Transferases; Transferring phosphorus- ...References: UniProt: P03366, ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Protein | Mass: 51928.629 Da / Num. of mol.: 2 / Mutation: C280S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: gag-pol / Production host: ![]() ![]() ![]() References: UniProt: P03366, HIV-1 retropepsin, RNA-directed DNA polymerase, DNA-directed DNA polymerase, retroviral ribonuclease H, exoribonuclease H, Transferases; Transferring phosphorus- ...References: UniProt: P03366, ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
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-RNA chain , 2 types, 4 molecules TEPF
#3: RNA chain | Mass: 7519.592 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: pbs SEQUENCE / Source: (synth.) ![]() ![]() ![]() #4: RNA chain | Mass: 5331.189 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: tRNA(LYS3) / Source: (synth.) ![]() ![]() |
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-Sugars , 1 types, 1 molecules
#5: Polysaccharide | beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose / ![]() |
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-Non-polymers , 2 types, 2 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#6: Chemical | ChemComp-MG / |
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#7: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.39 Å3/Da / Density % sol: 63.72 % |
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Crystal grow![]() | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: PEG 8000, AMMONIUM SULFATE, MGCL2, GLYCEROL, SUCROSE PH range: 6.8 - 7.2 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Mar 28, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.95→87.62 Å / Num. obs: 31549 / % possible obs: 99.9 % / Redundancy: 10.8 % / Biso Wilson estimate: 159.27 Å2 / Rmerge(I) obs: 0.236 / Net I/σ(I): 6.7 |
Reflection shell | Resolution: 3.95→4.16 Å / Redundancy: 10.1 % / Rmerge(I) obs: 2.446 / Mean I/σ(I) obs: 0.9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 5TXL Resolution: 3.95→87.62 Å / SU ML: 1.02 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 45.86 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.95→87.62 Å
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Refine LS restraints |
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LS refinement shell |
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