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- PDB-1iii: CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C-DATA COLL... -
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Basic information
Entry | Database: PDB / ID: 1iii | ||||||
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Title | CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C-DATA COLLECTED AT ROOM TEMPERATURE | ||||||
![]() | TRANSTHYRETIN![]() | ||||||
![]() | ![]() ![]() | ||||||
Function / homology | ![]() Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Eneqvist, T. / Olofsson, A. / Ando, Y. / Lundgren, E. / Sauer-Eriksson, A.E. | ||||||
![]() | ![]() Title: Disulfide-Bond Formation in the Transthyretin Mutant Y114C Prevents Amyloid Fibril Formation in Vivo and in Vitro Authors: Eneqvist, T. / Olofsson, A. / Ando, Y. / Miyakawa, T. / Katsuragi, S. / Jass, J. / Lundgren, E. / Sauer-Eriksson, A.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 | ![]() | 60.7 KB | Display | ![]() |
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PDB format | ![]() | 44.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1iikC ![]() 1f41S 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 on special symmetry positions |
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Details | The second part of the biological assembly is generated by the two fold axis: -x, -y, z. |
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Components
#1: Protein | ![]() Mass: 13717.329 Da / Num. of mol.: 2 / Fragment: TRANSTHYRETIN / Mutation: Y114C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-BME / ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.04 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 2M ammonium sulphate, 0.1M sodium citrate, 2% PEG 200, 1% BME, pH 5.0, VAPOR DIFFUSION, HANGING DROP at 298K, temperature 298.0K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Sep 3, 1998 |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2→20 Å / Num. all: 17049 / Num. obs: 17049 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.3 % / Biso Wilson estimate: 16.7 Å2 / Rmerge(I) obs: 0.091 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.398 / Mean I/σ(I) obs: 4.3 / Num. unique all: 1661 / % possible all: 97.2 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 155823 |
Reflection shell | *PLUS % possible obs: 97.2 % / Num. unique obs: 1661 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1F41 Resolution: 2→19.54 Å / SU B: 5.509 / SU ML: 0.1578 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.2109 / ESU R Free: 0.175 / Stereochemistry target values: Engh & Huber Details: Occupancy of BME molecules were refined after structural overall B-factor refinement
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Displacement parameters | Biso mean: 19.88 Å2
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Refinement step | Cycle: LAST / Resolution: 2→19.54 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 19.5 Å / Rfactor Rfree![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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