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Yorodumi- PDB-2qgc: Human transthyretin (TTR) complexed with 2-(3,5-Dimethyl-4-hydrox... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2qgc | ||||||
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Title | Human transthyretin (TTR) complexed with 2-(3,5-Dimethyl-4-hydroxyphenyl)benzoxazole | ||||||
Components | Transthyretin | ||||||
Keywords | Hormone/Growth Factor / Transthyretin / Tetramer / Amyloidogenesis Inhibitors / Hormone-Growth Factor COMPLEX | ||||||
Function / homology | Function and homology information Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / thyroid hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation ...Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / thyroid hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å | ||||||
Authors | Connelly, S. / Wilson, I.A. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2008 Title: Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors. Authors: Johnson, S.M. / Connelly, S. / Wilson, I.A. / Kelly, J.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qgc.cif.gz | 115.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qgc.ent.gz | 89.7 KB | Display | PDB format |
PDBx/mmJSON format | 2qgc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2qgc_validation.pdf.gz | 453.7 KB | Display | wwPDB validaton report |
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Full document | 2qgc_full_validation.pdf.gz | 457.3 KB | Display | |
Data in XML | 2qgc_validation.xml.gz | 13.7 KB | Display | |
Data in CIF | 2qgc_validation.cif.gz | 19.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qg/2qgc ftp://data.pdbj.org/pub/pdb/validation_reports/qg/2qgc | HTTPS FTP |
-Related structure data
Related structure data | 2qgbC 2qgdC 2qgeC 2fbrS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 13777.360 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TTR, PALB / Plasmid: pmmHA / Production host: Escherichia coli (E. coli) / Strain (production host): Epicurean Gold / References: UniProt: P02766 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 42.67 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: The WT-TTR was concentrated to 4 mg/mL in 10 mM NaPi, 100 mM KCl, at pH 7.6 and co-crystallized at room temperature with inhibitors using the vapor-diffusion sitting drop method. Crystals ...Details: The WT-TTR was concentrated to 4 mg/mL in 10 mM NaPi, 100 mM KCl, at pH 7.6 and co-crystallized at room temperature with inhibitors using the vapor-diffusion sitting drop method. Crystals were grown from 1.395 M sodium citrate, 3.5% v/v glycerol at pH 5.5. The crystals were frozen using a cryo-protectant solution of 1.395 M sodium citrate, pH 5.5, containing 10% v/v glycerol., VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.9791 Å |
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Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jan 11, 2007 Details: Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (ho rizontal focusing) |
Radiation | Monochromator: Side scattering bent cube-root I-beam single crystal; asymmetric cut 4.965 degs Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→50 Å / Num. obs: 59153 / % possible obs: 99.9 % / Redundancy: 7.1 % / Biso Wilson estimate: 14.1 Å2 / Rsym value: 0.036 / Χ2: 0.996 / Net I/σ(I): 13.9 |
Reflection shell | Resolution: 1.3→1.35 Å / Redundancy: 7 % / Rmerge(I) obs: 0.558 / Mean I/σ(I) obs: 3.75 / Num. unique all: 5841 / Rsym value: 0.558 / Χ2: 1.023 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Human Transthyretin PDB 2FBR Resolution: 1.3→50 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.969 / SU B: 1.287 / SU ML: 0.025 / Isotropic thermal model: Aniosotropic / Cross valid method: THROUGHOUT / ESU R: 0.049 / ESU R Free: 0.045 / 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: 13.555 Å2
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Refinement step | Cycle: LAST / Resolution: 1.3→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.3→1.333 Å / Total num. of bins used: 20
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