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Open data
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Basic information
Entry | Database: PDB / ID: 3tjh | ||||||
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Title | 42F3-p3A1/H2-Ld complex | ||||||
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![]() | IMMUNE SYSTEM / IG MHC / Antigen Recognition / TCR-pMHC / Membrane Receptor | ||||||
Function / homology | ![]() antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / lumenal side of endoplasmic reticulum membrane / MHC class I protein complex / defense response / positive regulation of T cell mediated cytotoxicity / phagocytic vesicle membrane / peptide antigen binding / immune response / external side of plasma membrane ...antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / lumenal side of endoplasmic reticulum membrane / MHC class I protein complex / defense response / positive regulation of T cell mediated cytotoxicity / phagocytic vesicle membrane / peptide antigen binding / immune response / external side of plasma membrane / signaling receptor binding / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Adams, J.J. / Kruse, A. / Kranz, D.M. / Garcia, K.C. | ||||||
![]() | ![]() Title: T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex. Authors: Adams, J.J. / Narayanan, S. / Liu, B. / Birnbaum, M.E. / Kruse, A.C. / Bowerman, N.A. / Chen, W. / Levin, A.M. / Connolly, J.M. / Zhu, C. / Kranz, D.M. / Garcia, K.C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 147.9 KB | Display | ![]() |
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PDB format | ![]() | 113.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3tf7SC ![]() 3tfkC ![]() 3tpuC 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 21072.260 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1116.266 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: GenScript |
#3: Antibody | Mass: 24917.635 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus, Homo sapiens / Plasmid: pAcGP67a/BD BaculoGold / Production host: ![]() |
#4: Protein | Mass: 28431.451 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus, Homo sapiens / Plasmid: pAcGP67a/BD BaculoGold / Production host: ![]() |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.23 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 6.6 Details: 16% PEG 3350, 0.2M ammonium nitrate and 0.1M Bis-Tris pH 6.6 in a 1:1 (v/v) drop with the TCR-pMHC complex. Crystals were soaked stepwise into well solution with 20% ethylene glycol and ...Details: 16% PEG 3350, 0.2M ammonium nitrate and 0.1M Bis-Tris pH 6.6 in a 1:1 (v/v) drop with the TCR-pMHC complex. Crystals were soaked stepwise into well solution with 20% ethylene glycol and flash frozen in liquid nitrogen, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Mar 31, 2010 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.12→58.86 Å / Num. all: 49357 / Num. obs: 49259 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2.12→2.23 Å / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3TF7 Resolution: 2.12→29.735 Å / SU ML: 0.3 / σ(F): 1.35 / Phase error: 23.47 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.882 Å2 / ksol: 0.345 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.12→29.735 Å
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Refine LS restraints |
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LS refinement shell |
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