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Open data
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Basic information
Entry | Database: PDB / ID: 1w47 | ||||||
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Title | P4 protein from Bacteriophage PHI12 in complex with ADP and MN | ||||||
![]() | NTPASE P4 | ||||||
![]() | HYDROLASE / DSRNA VIRUS / PACKAGING ATPASE / HEXAMERIC HELICASE / MOLECULAR MOTOR / NON-HYDROLYSABLE ATP ANALOGUE | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mancini, E.J. / Kainov, D.E. / Grimes, J.M. / Tuma, R. / Bamford, D.H. / Stuart, D.I. | ||||||
![]() | ![]() Title: Atomic Snapshots of an RNA Packaging Motor Reveal Conformational Changes Linking ATP Hydrolysis to RNA Translocation Authors: Mancini, E.J. / Kainov, D.E. / Grimes, J.M. / Tuma, R. / Bamford, D.H. / Stuart, D.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 186.2 KB | Display | ![]() |
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PDB format | ![]() | 147.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 40.9 KB | Display | |
Data in CIF | ![]() | 55.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1w44C ![]() 1w46C ![]() 1w48C ![]() 1w49C ![]() 1w4aC ![]() 1w4bC ![]() 1w4cC C: citing same article ( |
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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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 35150.430 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 48.2 % Description: CO-CRYSTALS OF P4-ADP-MN ARE ISOMORPHOUS TO P4-ADP CRYSTALS |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: 10% PEG 1500, 100MM SODIUM ACETATE PH 4.8 10 MM ADP 10MM MNCL, PROTEIN CONCENTRATION 10 MG/ML, SITTING DROPS, 22C |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 10, 2003 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.74363 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 36738 / % possible obs: 100 % / Redundancy: 12.2 % / Biso Wilson estimate: 50.316 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 31.3 |
Reflection shell | Resolution: 2.5→2.6 Å / Redundancy: 7 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 5.3 / % possible all: 96 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2.5→30 Å / Data cutoff high absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Solvent model: MASK / Bsol: 80 Å2 / ksol: 0.34 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.759 Å2
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Refine analyze | Luzzati d res low obs: 30 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.6 Å / Total num. of bins used: 8 /
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Xplor file |
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