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- PDB-2zcz: Crystal structures and thermostability of mutant TRAP3 A7 (ENGINE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2zcz | ||||||
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Title | Crystal structures and thermostability of mutant TRAP3 A7 (ENGINEERED TRAP) | ||||||
![]() | Transcription attenuation protein mtrB | ||||||
![]() | RNA BINDING PROTEIN / LINKER / ARTIFICIAL / ENGINEERED / RING PROTEIN / 12-mer / RNA-binding / Transcription / Transcription regulation | ||||||
Function / homology | ![]() DNA-templated transcription termination / regulation of DNA-templated transcription / RNA binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Watanabe, M. / Mishima, Y. / Yamashita, I. / Park, S.Y. / Tame, J.R.H. / Heddle, J.G. | ||||||
![]() | ![]() Title: Intersubunit linker length as a modifier of protein stability: crystal structures and thermostability of mutant TRAP. Authors: Watanabe, M. / Mishima, Y. / Yamashita, I. / Park, S.Y. / Tame, J.R. / Heddle, J.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.5 KB | Display | ![]() |
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PDB format | ![]() | 74.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 491.4 KB | Display | ![]() |
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Full document | ![]() | 496.9 KB | Display | |
Data in XML | ![]() | 18.7 KB | Display | |
Data in CIF | ![]() | 27.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2zd0C ![]() 2exsS S: Starting model for refinement 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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2 | ![]()
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Unit cell |
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Details | THE POLYPEPTIDE CHAIN CONTAINS THREE (3) COPIES OF THE TRAP PROTEIN LINKED IN TANDEM, WHICH ARRANGE THEMSELVES TO MAKE A 12-MER RING IN SOLUTION. EACH CHAIN IN THIS MODEL REPRESENTS ONE COPY OF TRAP, NOT A SEPARATE POLYPEPTIDE. THE LINKER PEPTIDES ARE MAINLY NOT VISIBLE IN THE ELECTRON DENSITY. THE 12MER RINGS ARE ALIGNED WITH THE CRYSTALLOGRAPHIC FOUR-FOLD AXIS. THERE ARE SIX COPIES OF TRAP PRESENT IN THE ASYMMETRIC UNIT. FOR THIS PROTEIN, CALLED T3A7, THE LINKER PEPTIDES CONSIST OF SEVEN (7) ALANINE RESIDUES. |
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Components
#1: Protein | Mass: 8754.920 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: NCA 26, ATCC 12980 / Gene: mtrB / Plasmid: pET21b / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Chemical | ChemComp-TRP / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.38 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 0.1M sodium citrate pH5.5, 30%(w/v)MPD, 0.2M ammonium acetate, 10mM L-tryptophan, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 190 / Detector: CCD / Date: Mar 3, 2007 / Details: mirrors |
Radiation | Monochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 39479 / % possible obs: 94.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 14.2 Å2 / Rmerge(I) obs: 0.08 / Rsym value: 0.062 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.304 / Mean I/σ(I) obs: 9 / Num. unique all: 2921 / Rsym value: 0.454 / % possible all: 70.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2EXS Resolution: 1.8→20 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.906 / SU B: 2.84 / SU ML: 0.09 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.137 / ESU R Free: 0.137 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.19 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.801→1.848 Å / Rfactor Rfree error: 0.072 / Total num. of bins used: 20
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