+Open data
-Basic information
Entry | Database: PDB / ID: 3rwi | ||||||
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Title | Rhesus macaque MHC class I molecule Mamu-B*17-GW10 | ||||||
Components |
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Keywords | IMMUNE SYSTEM / antigenic peptides / T lymphocytes / immune response | ||||||
Function / homology | Function and homology information antigen processing and presentation of peptide antigen via MHC class I / viral life cycle / 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 / ER to Golgi transport vesicle membrane / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / positive regulation of T cell mediated cytotoxicity ...antigen processing and presentation of peptide antigen via MHC class I / viral life cycle / 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 / ER to Golgi transport vesicle membrane / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / positive regulation of T cell mediated cytotoxicity / recycling endosome membrane / phagocytic vesicle membrane / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / positive regulation of T cell activation / MHC class II protein complex binding / late endosome membrane / early endosome membrane / host cell cytoplasm / immune response / lysosomal membrane / external side of plasma membrane / signaling receptor binding / host cell plasma membrane / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Macaca mulatta (Rhesus monkey) Simian immunodeficiency virus | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.009 Å | ||||||
Authors | Wu, Y. / Gao, F. / Liu, J. / Qi, J.X. / Price, D.A. / Gao, G.F. | ||||||
Citation | Journal: J.Immunol. / Year: 2011 Title: Structural basis of diverse peptide accommodation by the rhesus macaque MHC class I molecule Mamu-B*17: insights into immune protection from simian immunodeficiency virus Authors: Wu, Y. / Gao, F. / Liu, J. / Qi, J.X. / Gostick, E. / Price, D.A. / Gao, G.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3rwi.cif.gz | 188.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3rwi.ent.gz | 149.4 KB | Display | PDB format |
PDBx/mmJSON format | 3rwi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rw/3rwi ftp://data.pdbj.org/pub/pdb/validation_reports/rw/3rwi | HTTPS FTP |
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-Related structure data
Related structure data | 3rwcC 3rwdC 3rweC 3rwfC 3rwgC 3rwhC 3rwjC 2bvoS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 32025.082 Da / Num. of mol.: 1 / Fragment: residues 24-297 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Macaca mulatta (Rhesus monkey) / Gene: MHCI-B / Production host: Escherichia coli (E. coli) / References: UniProt: Q9GJ77 |
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#2: Protein | Mass: 11660.079 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Macaca mulatta (Rhesus monkey) / Gene: B2M / Production host: Escherichia coli (E. coli) / References: UniProt: Q6V7J5 |
#3: Protein/peptide | Mass: 1176.258 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthtic peptide / Source: (synth.) Simian immunodeficiency virus / References: UniProt: Q89490 |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.15 % |
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU |
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Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Aug 8, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.009→50 Å / Num. obs: 32167 / Biso Wilson estimate: 26.21 Å2 |
-Processing
Software | Name: PHENIX / Version: (phenix.refine: 1.6.4_486) / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2BVO Resolution: 2.009→24.399 Å / Occupancy max: 1 / Occupancy min: 0.41 / FOM work R set: 0.8667 / SU ML: 0.25 / σ(F): 1.36 / Phase error: 20.48 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.72 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 52.168 Å2 / ksol: 0.379 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 132.33 Å2 / Biso mean: 31.6043 Å2 / Biso min: 5.31 Å2
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Refinement step | Cycle: LAST / Resolution: 2.009→24.399 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10
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Refinement TLS params. | Method: refined / Origin x: -4.5109 Å / Origin y: -0.1184 Å / Origin z: -20.6266 Å
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Refinement TLS group |
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