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- PDB-1rpo: RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rpo | ||||||
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Title | RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE | ||||||
![]() | ROP PROTEIN | ||||||
![]() | TRANSCRIPTION REGULATION | ||||||
Function / homology | Helix Hairpins - #230 / Regulatory protein Rop / Rop-like superfamily / Rop protein / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / identical protein binding / Regulatory protein rop![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Vlassi, M. / Kokkinidis, M. | ||||||
![]() | ![]() Title: Restored heptad pattern continuity does not alter the folding of a four-alpha-helix bundle. Authors: Vlassi, M. / Steif, C. / Weber, P. / Tsernoglou, D. / Wilson, K.S. / Hinz, H.J. / Kokkinidis, M. #1: ![]() Title: Correlation between Protein Stability and Crystal Properties of Designed Rop Variants Authors: Kokkinidis, M. / Vlassi, M. / Papanikolaou, Y. / Kotsifaki, D. / Kingswell, A. / Tsernoglou, D. / Hinz, H.J. #2: ![]() Title: Structure of the Col(Asterisk)E1 (Asterisk)Rop Protein at 1.7 Angstroms Resolution Authors: Banner, D.W. / Kokkinidis, M. / Tsernoglou, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 25.8 KB | Display | ![]() |
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PDB format | ![]() | 17 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.2 KB | Display | ![]() |
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Full document | ![]() | 362.1 KB | Display | |
Data in XML | ![]() | 2.8 KB | Display | |
Data in CIF | ![]() | 4.2 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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Details | THE MOLECULE EXISTS IN SOLUTION AS A DIMER WHICH IS FORMED IN THE CRYSTAL BY THE CRYSTALLOGRAPHIC DYAD AXIS. THE SECOND MONOMER RESULTS FROM THE TRANSFORMATION: W' = R W +T WHERE W IS THE COLUMN VECTOR XSUB,YSUB,ZSUB R IS THE ROTATION MATRIX: SYMTY1 1 -0.999780 0.000000 0.000230 40.86282 SYMTY2 1 0.000000 1.000000 0.000000 0.00000 SYMTY3 1 0.000000 0.000000 -1.000020 31.25076 |
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Components
#1: Protein | Mass: 7379.194 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.89 Å3/Da / Density % sol: 34.79 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 5.4 / PH range high: 5 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.4 Å / Num. obs: 10456 / % possible obs: 96 % / Rmerge(I) obs: 0.043 |
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Processing
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Refinement | Resolution: 1.4→6 Å / σ(I): 1.5 /
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Refinement step | Cycle: LAST / Resolution: 1.4→6 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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