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- PDB-3q37: Identification of Amino Acids that Account for Long-Range Interac... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3q37 | ||||||
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Title | Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes. | ||||||
![]() | TIM from Trypanosoma cruzi/ TIM from Trypanosoma brucei brucei chimera protein | ||||||
![]() | ISOMERASE / TIM barrel | ||||||
Function / homology | ![]() glycosome / triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / gluconeogenesis / glycolytic process / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Garcia-Torres, I. / Cabrera, N. / Torres-Larios, A. / Rodriguez-Bolanos, M. / Gomez-Puyou, A. / Perez-Montfort, R. | ||||||
![]() | ![]() Title: Identification of amino acids that account for long-range interactions in two triosephosphate isomerases from pathogenic trypanosomes. Authors: Garcia-Torres, I. / Cabrera, N. / Torres-Larios, A. / Rodriguez-Bolanos, M. / Diaz-Mazariegos, S. / Gomez-Puyou, A. / Perez-Montfort, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 214.6 KB | Display | ![]() |
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PDB format | ![]() | 170.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.2 KB | Display | ![]() |
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Full document | ![]() | 454.4 KB | Display | |
Data in XML | ![]() | 44.3 KB | Display | |
Data in CIF | ![]() | 66.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1tcdS 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27322.244 Da / Num. of mol.: 4 Fragment: UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Gene: TIM / Plasmid: pET3b / Production host: ![]() ![]() References: UniProt: P04789, UniProt: P52270, triose-phosphate isomerase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.48 % |
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Crystal grow | Temperature: 278 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.2 Sodium malonate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K |
-Data collection
Diffraction | Mean temperature: 110 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Nov 9, 2008 / Details: mirrors | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Kohzu / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.65→54.31 Å / Num. all: 107171 / Num. obs: 107171 / % possible obs: 91.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 2.3 / Redundancy: 3.1 % / Biso Wilson estimate: 13.4 Å2 / Rmerge(I) obs: 0.088 / Rsym value: 0.073 / Net I/σ(I): 10.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1TCD Resolution: 1.65→41.75 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze | Luzzati coordinate error obs: 0.21 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→41.75 Å
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Refine LS restraints |
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LS refinement shell |
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