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Open data
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Basic information
Entry | Database: PDB / ID: 4zn1 | ||||||
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Title | Crystal Structure of MjSpt4:Spt5 complex conformation A | ||||||
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![]() | TRANSCRIPTION / protein-protein complex | ||||||
Function / homology | ![]() transcription elongation-coupled chromatin remodeling / translation elongation factor activity / regulation of DNA-templated transcription elongation / ribosome / structural constituent of ribosome / mRNA binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guo, G.R. / Zhou, H.H. / Gao, Y.X. / Zhu, Z.L. / Niu, L.W. / Teng, M.K. | ||||||
![]() | ![]() Title: Structural and biochemical insights into the DNA-binding mode of MjSpt4p:Spt5 complex at the exit tunnel of RNAPII Authors: Guo, G.R. / Gao, Y.X. / Zhu, Z.L. / Zhao, D. / Liu, Z. / Zhou, H.H. / Niu, L.W. / Teng, M.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 52 KB | Display | ![]() |
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PDB format | ![]() | 34.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.7 KB | Display | ![]() |
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Full document | ![]() | 441.8 KB | Display | |
Data in XML | ![]() | 9.2 KB | Display | |
Data in CIF | ![]() | 11.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4zn3C ![]() 1nppS ![]() 1ryqS ![]() 3ewgS C: citing same article ( 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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Unit cell |
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Components
#1: Protein | Mass: 16158.936 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: DSM 2661 / Gene: spt5 / Plasmid: pRSFDuet / Production host: ![]() ![]() |
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#2: Protein | Mass: 8075.311 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: DSM 2661 / Gene: spt4 / Plasmid: pRSFDuet / Production host: ![]() ![]() |
#3: Chemical | ChemComp-ZN / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.7 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: PEG 5000MME, propanol, MES, sarcosine |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: May 20, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→37.93 Å / Num. obs: 6086 / % possible obs: 99.6 % / Redundancy: 4 % / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 4 % / Rmerge(I) obs: 0.299 / Mean I/σ(I) obs: 3.7 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3EWG, 1RYQ, 1NPP Resolution: 2.8→37.93 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.904 / SU B: 15.284 / SU ML: 0.273 / Cross valid method: THROUGHOUT / ESU R: 1.525 / ESU R Free: 0.393 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 69.501 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→37.93 Å
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Refine LS restraints |
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