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- PDB-1lnu: CRYSTAL STRUCTURE OF CLASS II MHC MOLECULE IAb BOUND TO EALPHA3K ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lnu | |||||||||
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Title | CRYSTAL STRUCTURE OF CLASS II MHC MOLECULE IAb BOUND TO EALPHA3K PEPTIDE | |||||||||
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![]() | SUGAR BINDING PROTEIN / Protein-peptide complex / T cell receptor / antigen presentation | |||||||||
Function / homology | ![]() positive regulation of antigen processing and presentation / positive regulation of alpha-beta T cell activation / positive regulation of T-helper 1 type immune response / protein antigen binding / antigen processing and presentation of peptide antigen / B cell affinity maturation / positive regulation of T cell differentiation / response to type II interferon / antigen processing and presentation / toxic substance binding ...positive regulation of antigen processing and presentation / positive regulation of alpha-beta T cell activation / positive regulation of T-helper 1 type immune response / protein antigen binding / antigen processing and presentation of peptide antigen / B cell affinity maturation / positive regulation of T cell differentiation / response to type II interferon / antigen processing and presentation / toxic substance binding / negative regulation of T cell proliferation / multivesicular body / cellular response to type II interferon / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / 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 / adaptive immune response / lysosome / early endosome / immune response / lysosomal membrane / external side of plasma membrane / ubiquitin protein ligase binding / protein-containing complex binding / Golgi apparatus / cell surface / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Liu, X. / Dai, S. / Crawford, F. / Fruge, R. / Marrack, P. / Kappler, J. | |||||||||
![]() | ![]() Title: Alternate interactions define the binding of peptides to the MHC molecule IA(b). Authors: Liu, X. / Dai, S. / Crawford, F. / Fruge, R. / Marrack, P. / Kappler, J. | |||||||||
History |
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Remark 999 | SEQUENCE Author states two separate sequences, an Ealpha3K peptide(1-13) and linker(14-28), which ...SEQUENCE Author states two separate sequences, an Ealpha3K peptide(1-13) and linker(14-28), which start from residue 1 to residue 28 were added to the N-terminus of the beta chain of the class II MHC IAB of chains B,D,F and H. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 328.2 KB | Display | ![]() |
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PDB format | ![]() | 267.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 536.3 KB | Display | ![]() |
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Full document | ![]() | 675.7 KB | Display | |
Data in XML | ![]() | 79.5 KB | Display | |
Data in CIF | ![]() | 106.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2iadS S: Starting model for refinement |
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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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3 | ![]()
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4 | ![]()
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Unit cell |
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Details | One molecule includes one alpha chain and one beta chain with the peptide |
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Components
#1: Protein | Mass: 20597.957 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 24938.830 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Sugar | ChemComp-NAG / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.97 Å3/Da / Density % sol: 58.53 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG8000, MES, KH2PO4, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||||||||||||
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: SDMS / Detector: AREA DETECTOR / Date: Dec 6, 2001 |
Radiation | Monochromator: Yale mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99187 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→40 Å / Num. all: 54497 / Num. obs: 54497 / % possible obs: 74.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): -3 / Redundancy: 2.2 % / Biso Wilson estimate: 14.4 Å2 / Rmerge(I) obs: 0.089 |
Reflection shell | Resolution: 2.5→2.59 Å / Rmerge(I) obs: 0.352 / Num. unique all: 1829 / % possible all: 21.3 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 40 Å |
Reflection shell | *PLUS % possible obs: 21.3 % / Num. unique obs: 1829 / Mean I/σ(I) obs: 4.3 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2IAD Resolution: 2.5→38.39 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 53511.21 / Data cutoff high rms absF: 53511.21 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 28.563 Å2 / ksol: 0.342183 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.6 Å2 | |||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→38.39 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: CONSTR | |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.5→2.66 Å / Rfactor Rfree error: 0.032 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 40 Å / Num. reflection obs: 54427 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Lowest resolution: 2.59 Å / Rfactor Rfree: 0.313 / Num. reflection Rfree: 66 / Rfactor Rwork: 0.277 / Num. reflection obs: 1591 |