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Open data
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Basic information
Entry | Database: PDB / ID: 1iea | ||||||
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Title | HISTOCOMPATIBILITY ANTIGEN | ||||||
![]() | (MHC CLASS II I-EK) x 2 | ||||||
![]() | HISTOCOMPATIBILITY ANTIGEN | ||||||
Function / homology | ![]() Phosphorylation of CD3 and TCR zeta chains / Translocation of ZAP-70 to Immunological synapse / PD-1 signaling / Generation of second messenger molecules / Downstream TCR signaling / MHC class II antigen presentation / immunoglobulin mediated immune response / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / peptide antigen binding ...Phosphorylation of CD3 and TCR zeta chains / Translocation of ZAP-70 to Immunological synapse / PD-1 signaling / Generation of second messenger molecules / Downstream TCR signaling / MHC class II antigen presentation / immunoglobulin mediated immune response / 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 / lysosomal membrane / external side of plasma membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fremont, D.H. / Hendrickson, W.A. / Marrack, P. / Kappler, J. | ||||||
![]() | ![]() Title: Structures of an MHC class II molecule with covalently bound single peptides. Authors: Fremont, D.H. / Hendrickson, W.A. / Marrack, P. / Kappler, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 173.3 KB | Display | ![]() |
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PDB format | ![]() | 140.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.2 KB | Display | ![]() |
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Full document | ![]() | 430.2 KB | Display | |
Data in XML | ![]() | 19.2 KB | Display | |
Data in CIF | ![]() | 30.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1iebC ![]() 1dlhS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 22324.008 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: WITH COVALENTLY BOUND HB PEPTIDE / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 25892.832 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: WITH COVALENTLY BOUND HB PEPTIDE / Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Sugar | ChemComp-NAG / #4: Water | ChemComp-HOH / | Compound details | THIS ENTRY CONTAINS COORDINATES FOR THE EXTRACELLULAR DOMAINS OF THE MURINE MHC CLASS II MOLECULE I- ...THIS ENTRY CONTAINS COORDINATE | Sequence details | CHAINS B AND D CONTAIN THE HB PEPTIDE AND LINKER REGIONS. THE BETA CHAIN AMINO TERMINUS, PEPTIDE P1 ...CHAINS B AND D CONTAIN THE HB PEPTIDE AND LINKER REGIONS. THE BETA CHAIN AMINO TERMINUS, PEPTIDE P1 - P9 AND LINKER ARE NOTED WITH THE INSERTION CODES N, P, AND L. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.2 Details: 8% PEG 4000, 2% EG, 200MM A.S, 100MM CITRATE PH 5.2 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown / PH range low: 5.6 / PH range high: 5.2 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: FUJI / Detector: IMAGE PLATE | |||||||||
Radiation | Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 2.3→20 Å / Num. obs: 38809 / % possible obs: 89.2 % / Redundancy: 4.35 % / Biso Wilson estimate: 34.2 Å2 / Rsym value: 0.075 | |||||||||
Reflection | *PLUS Num. measured all: 169034 / Rmerge(I) obs: 0.075 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1DLH Resolution: 2.3→6 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.01 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 32.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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