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Open data
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Basic information
Entry | Database: PDB / ID: 2j16 | ||||||
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Title | Apo & Sulphate bound forms of SDP-1 | ||||||
![]() | (TYROSINE-PROTEIN PHOSPHATASE YIL113W) x 2 | ||||||
![]() | HYDROLASE / PROTEIN PHOSPHATASE / HYPOTHETICAL PROTEIN | ||||||
Function / homology | ![]() cell integrity MAPK cascade / MAP kinase tyrosine phosphatase activity / protein tyrosine/threonine phosphatase activity / MAP kinase tyrosine/serine/threonine phosphatase activity / negative regulation of MAPK cascade / dephosphorylation / protein-tyrosine-phosphatase / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Briggs, D.C. / McDonald, N.Q. | ||||||
![]() | ![]() Title: Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases. Authors: Fox, G.C. / Shafiq, M. / Briggs, D.C. / Knowles, P.P. / Collister, M. / Didmon, M.J. / Makrantoni, V. / Dickinson, R.J. / Hanrahan, S. / Totty, N. / Stark, M.J. / Keyse, S.M. / McDonald, N.Q. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 69.9 KB | Display | ![]() |
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PDB format | ![]() | 51.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 450.6 KB | Display | ![]() |
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Full document | ![]() | 452.8 KB | Display | |
Data in XML | ![]() | 12.5 KB | Display | |
Data in CIF | ![]() | 16.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.749, 0.6625, 0.004), Vector: |
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Components
#1: Protein | Mass: 20902.004 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-198 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: S288C / AB972 / Plasmid: PET14B / Production host: ![]() ![]() | ||
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#2: Protein | Mass: 20870.004 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-198 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: S288C / AB972 / Plasmid: PET14B / Production host: ![]() ![]() | ||
#3: Chemical | ChemComp-MG / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.65 Å3/Da / Density % sol: 66.01 % |
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Crystal grow | Method: vapor diffusion, sitting drop Details: 1.5M MGSO4, 0.1M HEPES, PH 7.5 7MG/ML PROTEIN 1:1 SITTING DROP VAPOUR DIFFUSION |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 1, 2000 / Details: MIRRORS |
Radiation | Monochromator: SI CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. obs: 13396 / % possible obs: 99.7 % / Observed criterion σ(I): 1 / Redundancy: 4.3 % / Rmerge(I) obs: 0.06 |
Reflection shell | Resolution: 2.7→2.8 Å / Rmerge(I) obs: 0.37 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: ENSEMBLE MODEL Resolution: 2.7→19.77 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.903 / SU B: 10.719 / SU ML: 0.224 / Cross valid method: THROUGHOUT / ESU R: 0.498 / ESU R Free: 0.299 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DISORDERED REGIONS AND SIDECHAIN ATOMS WERE OMMITTED.
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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: 42.49 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→19.77 Å
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Refine LS restraints |
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