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Open data
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Basic information
Entry | Database: PDB / ID: 1tdj | ||||||
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Title | THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI | ||||||
![]() | BIOSYNTHETIC THREONINE DEAMINASE | ||||||
![]() | ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gallagher, D.T. / Gilliland, G.L. / Xiao, G. / Eisenstein, E. | ||||||
![]() | ![]() Title: Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. Authors: Gallagher, D.T. / Gilliland, G.L. / Xiao, G. / Zondlo, J. / Fisher, K.E. / Chinchilla, D. / Eisenstein, E. #1: ![]() Title: Polymorphous Crystallization and Diffraction of Threonine Deaminase from Escherichia Coli Authors: Gallagher, D.T. / Eisenstein, E. / Fisher, K.E. / Zondlo, J. / Chinchilla, D. / Yu, H.D. / Dill, J. / Winborne, E. / Ducote, K. / Xiao, G. / Gilliland, G.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 105.1 KB | Display | ![]() |
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PDB format | ![]() | 85 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Components
#1: Protein | Mass: 56263.070 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SCHIFF BASE LINKAGE BETWEEN LYS 62 AND PLP / Source: (natural) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PLP / ![]() |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 46 % / Description: C-DOMAIN IMAGED BY IMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 8 Details: PROTEIN AT 40 MG/ML WAS MIXED WITH, THEN EQUILIBRATED OVER 11% PEG 4K, 40 MM TRIS 8.0, 60 MM MGCL2, AT RT. Temp details: room temp | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging dropDetails: Gallagher, D.T., (1998) Acta Crystallogr.,Sect.D, 54, 467. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Sep 1, 1995 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.7→16 Å / Num. obs: 13860 / % possible obs: 78 % / Observed criterion σ(I): 0.5 / Redundancy: 2 % / Biso Wilson estimate: 28.3 Å2 / Rmerge(I) obs: 0.055 / Rsym value: 0.088 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.7→2.86 Å / Redundancy: 1 % / Rmerge(I) obs: 0.197 / Mean I/σ(I) obs: 2.9 / Rsym value: 0.372 / % possible all: 30 |
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Processing
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Refinement | Method to determine structure![]() ![]() Details: THE 61 ATOMS WITH B=100.0 MUST BE CONSIDERED TO BE MARGINALLY ORDERED.
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Solvent computation | Solvent model: BABINET SCALING / Bsol: 150 Å2 / ksol: 0.56 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→16 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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