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Open data
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Basic information
Entry | Database: PDB / ID: 1oeb | ||||||
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Title | Mona/Gads SH3C domain | ||||||
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Function / homology | ![]() TCR signalosome / FLT3 Signaling / CD28 co-stimulation / GPVI-mediated activation cascade / FCERI mediated MAPK activation / Signaling by SCF-KIT / Generation of second messenger molecules / mast cell activation / FCERI mediated Ca+2 mobilization / DAP12 signaling ...TCR signalosome / FLT3 Signaling / CD28 co-stimulation / GPVI-mediated activation cascade / FCERI mediated MAPK activation / Signaling by SCF-KIT / Generation of second messenger molecules / mast cell activation / FCERI mediated Ca+2 mobilization / DAP12 signaling / plasma membrane raft / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Harkiolaki, M. / Lewitzky, M. / Gilbert, R.J.C. / Jones, E.Y. / Bourette, R.P. / Mouchiroud, G. / Sondermann, H. / Moarefi, I. / Feller, S.M. | ||||||
![]() | ![]() Title: Structural Basis for SH3 Domain-Mediated High-Affinity Binding between Mona/Gads and Slp-76 Authors: Harkiolaki, M. / Lewitzky, M. / Gilbert, R.J.C. / Jones, E.Y. / Bourette, R.P. / Mouchiroud, G. / Sondermann, H. / Moarefi, I. / Feller, S.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 46.7 KB | Display | ![]() |
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PDB format | ![]() | 32.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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 domain:
NCS domain segments: Component-ID: 1
NCS ensembles :
NCS oper:
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Components
#1: Protein | Mass: 7088.970 Da / Num. of mol.: 2 / Fragment: SH3C DOMAIN, RESIDUES 265-322 Source method: isolated from a genetically manipulated source Details: THROMBIN CLEAVAGE OVERHANG BETWEEN A-4 AND A-1 / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #2: Protein/peptide | ![]() Mass: 1380.589 Da / Num. of mol.: 2 / Fragment: PROTEIN INTERACTION PEPTIDE, RESIDUES 231-243 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() ![]() #3: Chemical | ChemComp-CD / | #4: Water | ChemComp-HOH / | ![]() Compound details | GADS/MONA:INTERACTS WITH SLP-76 TO REGULATE NF-AT ACTIVATION. SLP-76:INVOLVED IN T CELL ANTIGEN ...GADS/MONA:INTERACTS WITH SLP-76 TO REGULATE NF-AT ACTIVATION | Sequence details | SELENOMETHIONYL MONA/GADS SH3C WAS PRODUCED IN BL21(DE3) CELLS BY INHIBITION OF ENDOGENOUS ...SELENOMETH | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 36.3 % Description: MAD DATA COLLECTED AT SELENIUM PEAK, INFLECTION AND HIGH ENERGY REMOTE WAVELENGTHS. DATA STATISTICS REFLECT THE PEAK WAVELENGTH. | |||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 6.5 Details: PROTEIN WAS CRYSTALLISED FROM: 20% PEG4000, 5 MM CDCL2,50 MM NA CACODYLATE PH 6.5 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 15, 2002 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.69→36 Å / Num. obs: 15317 / % possible obs: 98 % / Observed criterion σ(I): 4 / Redundancy: 6.5 % / Rmerge(I) obs: 0.055 / Net I/σ(I): 28.2 |
Reflection shell | Resolution: 1.69→1.75 Å / Rmerge(I) obs: 0.404 / Mean I/σ(I) obs: 4 / % possible all: 81.4 |
Reflection | *PLUS Lowest resolution: 36 Å / % possible obs: 98.2 % / Num. measured all: 99470 |
Reflection shell | *PLUS % possible obs: 81.4 % |
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Processing
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Refinement | Method to determine structure![]() ![]()
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.64 Å2
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Refinement step | Cycle: LAST / Resolution: 1.76→19.69 Å
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