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Open data
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Basic information
Entry | Database: PDB / ID: 2qep | ||||||
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Title | Crystal structure of the D1 domain of PTPRN2 (IA2beta) | ||||||
![]() | Receptor-type tyrosine-protein phosphatase N2 | ||||||
![]() | HYDROLASE / PTPRN2 / PTPRP / Phogrin / IA-2 beta / autoantigen / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() regulation of secretion / transmembrane receptor protein tyrosine phosphatase activity / Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases / neurotransmitter secretion / insulin secretion involved in cellular response to glucose stimulus / ficolin-1-rich granule membrane / protein dephosphorylation / protein-tyrosine-phosphatase / secretory granule membrane / secretory granule ...regulation of secretion / transmembrane receptor protein tyrosine phosphatase activity / Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases / neurotransmitter secretion / insulin secretion involved in cellular response to glucose stimulus / ficolin-1-rich granule membrane / protein dephosphorylation / protein-tyrosine-phosphatase / secretory granule membrane / secretory granule / lipid metabolic process / synaptic vesicle membrane / receptor complex / synapse / Neutrophil degranulation / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ugochukwu, E. / Barr, A. / Alfano, I. / Berridge, G. / Burgess-Brown, N. / Das, S. / Fedorov, O. / King, O. / Niesen, F. / Watt, S. ...Ugochukwu, E. / Barr, A. / Alfano, I. / Berridge, G. / Burgess-Brown, N. / Das, S. / Fedorov, O. / King, O. / Niesen, F. / Watt, S. / Savitsky, P. / Salah, E. / Pike, A.C.W. / Bunkoczi, G. / von Delft, F. / Sundstrom, M. / Edwards, A. / Arrowsmith, C.H. / Weigelt, J. / Knapp, S. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Large-scale structural analysis of the classical human protein tyrosine phosphatome. Authors: Barr, A.J. / Ugochukwu, E. / Lee, W.H. / King, O.N. / Filippakopoulos, P. / Alfano, I. / Savitsky, P. / Burgess-Brown, N.A. / Muller, S. / Knapp, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 122.4 KB | Display | ![]() |
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PDB format | ![]() | 93.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.4 KB | Display | ![]() |
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Full document | ![]() | 443.4 KB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 29.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ahsC ![]() 2b49C ![]() 2cfvC ![]() 2cjzC ![]() 2gjtC ![]() 2h4vC ![]() 2i75C ![]() 2jjdC ![]() 2nlkC ![]() 2nz6C ![]() 2oc3C ![]() 2ooqC ![]() 2p6xC ![]() 2pa5C ![]() 3b7oC ![]() 2i1yS S: Starting model for refinement C: citing same article ( |
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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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1 / Refine code: 4
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Components
#1: Protein | Mass: 34977.453 Da / Num. of mol.: 2 / Fragment: D1 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Strain (production host): Phage-resistant derivative of BL21(DE3) References: UniProt: Q92932, protein-tyrosine-phosphatase #2: Chemical | ChemComp-CL / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.39 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.2 M Na/KPO4, 0.1 M Bis-tris-propane pH 6.5, 20.0% PEG 3350, 10.0% Ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: May 10, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9999 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→59.23 Å / Num. all: 23096 / Num. obs: 23096 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rmerge(I) obs: 0.139 / Rsym value: 0.139 / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.465 / Mean I/σ(I) obs: 1.9 / Num. unique all: 11455 / Rsym value: 0.465 / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2I1Y Resolution: 2.5→59.23 Å / Cor.coef. Fo:Fc: 0.916 / Cor.coef. Fo:Fc free: 0.874 / SU B: 25.532 / SU ML: 0.266 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.629 / ESU R Free: 0.329 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.042 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→59.23 Å
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Refine LS restraints |
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Refine LS restraints NCS | Ens-ID: 1 / Number: 3422 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.5→2.565 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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