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- PDB-3pab: Crystal Structure of H2-Kb in complex with a mutant of the chicke... -

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Basic information

Entry
Database: PDB / ID: 3pab
TitleCrystal Structure of H2-Kb in complex with a mutant of the chicken ovalbumin epitope OVA-E1
Components
  • Beta-2-microglobulinBeta-2 microglobulin
  • H-2 class I histocompatibility antigen, K-B alpha chain
  • Ovalbumin epitope, EIINFEKL
KeywordsIMMUNE SYSTEM / H2Kb / OVA / APL / altered peptide ligands / ovalbumin / TCR / T cell
Function / homology
Function and homology information


intracellular amino acid homeostasis / RUNX1 regulates transcription of genes involved in differentiation of keratinocytes / phagolysosome / monoatomic ion homeostasis / response to steroid hormone / Endosomal/Vacuolar pathway / DAP12 interactions / embryo development ending in birth or egg hatching / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway ...intracellular amino acid homeostasis / RUNX1 regulates transcription of genes involved in differentiation of keratinocytes / phagolysosome / monoatomic ion homeostasis / response to steroid hormone / Endosomal/Vacuolar pathway / DAP12 interactions / embryo development ending in birth or egg hatching / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / response to corticosterone / regulation of membrane depolarization / antigen processing and presentation of exogenous peptide antigen via MHC class I / inner ear development / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / cellular defense response / beta-2-microglobulin binding / monoatomic ion transport / phagocytic vesicle / Neutrophil degranulation / 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 / early endosome lumen / response to progesterone / Neutrophil degranulation / lumenal side of endoplasmic reticulum membrane / peptide binding / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / negative regulation of forebrain neuron differentiation / regulation of erythrocyte differentiation / peptide antigen assembly with MHC class I protein complex / response to molecule of bacterial origin / regulation of iron ion transport / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / cellular response to iron ion / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / multicellular organismal-level iron ion homeostasis / negative regulation of neurogenesis / peptide antigen assembly with MHC class II protein complex / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / response to estrogen / phagocytic vesicle membrane / peptide antigen binding / positive regulation of cellular senescence / antigen processing and presentation of exogenous peptide antigen via MHC class II / negative regulation of epithelial cell proliferation / positive regulation of immune response / antimicrobial humoral immune response mediated by antimicrobial peptide / sensory perception of smell / positive regulation of T cell activation / negative regulation of neuron projection development / MHC class II protein complex binding / late endosome membrane / T cell differentiation in thymus / iron ion transport / protein refolding / antibacterial humoral response / protein homotetramerization / intracellular iron ion homeostasis / protease binding / vesicle / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / amyloid fibril formation / learning or memory / defense response to Gram-positive bacterium / defense response to bacterium / immune response / lysosomal membrane / external side of plasma membrane / signaling receptor binding / intracellular membrane-bounded organelle / innate immune response / calcium ion binding / protein-containing complex binding / structural molecule activity / Golgi apparatus / endoplasmic reticulum / protein homodimerization activity / extracellular space / extracellular region / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Serpin, conserved site / Serpins signature. / Serpin superfamily, domain 2 / Serpin family / Serpin domain / Serpin superfamily / Serpin superfamily, domain 1 / Serpin (serine protease inhibitor) / SERine Proteinase INhibitors / MHC class I, alpha chain, C-terminal ...Serpin, conserved site / Serpins signature. / Serpin superfamily, domain 2 / Serpin family / Serpin domain / Serpin superfamily / Serpin superfamily, domain 1 / Serpin (serine protease inhibitor) / SERine Proteinase INhibitors / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Ovalbumin / Beta-2-microglobulin / H-2 class I histocompatibility antigen, K-B alpha chain
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.2 Å
AuthorsWesselingh, R. / Gras, S. / Guillonneau, C. / Turner, S.J. / Rossjohn, J.
CitationJournal: J.Immunol. / Year: 2011
Title: Affinity thresholds for naive CD8+ CTL activation by peptides and engineered influenza A viruses
Authors: Denton, A.E. / Wesselingh, R. / Gras, S. / Guillonneau, C. / Olson, M.R. / Mintern, J.D. / Zeng, W. / Jackson, D.C. / Rossjohn, J. / Hodgkin, P.D. / Doherty, P.C. / Turner, S.J.
History
DepositionOct 19, 2010Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Oct 19, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 9, 2011Group: Database references
Revision 1.2Jun 19, 2013Group: Database references
Revision 1.3Nov 1, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: H-2 class I histocompatibility antigen, K-B alpha chain
B: Beta-2-microglobulin
C: Ovalbumin epitope, EIINFEKL
D: H-2 class I histocompatibility antigen, K-B alpha chain
E: Beta-2-microglobulin
F: Ovalbumin epitope, EIINFEKL


Theoretical massNumber of molelcules
Total (without water)89,8216
Polymers89,8216
Non-polymers00
Water10,341574
1
A: H-2 class I histocompatibility antigen, K-B alpha chain
B: Beta-2-microglobulin
F: Ovalbumin epitope, EIINFEKL


Theoretical massNumber of molelcules
Total (without water)44,9113
Polymers44,9113
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4100 Å2
ΔGint-18 kcal/mol
Surface area19830 Å2
MethodPISA
2
C: Ovalbumin epitope, EIINFEKL
D: H-2 class I histocompatibility antigen, K-B alpha chain
E: Beta-2-microglobulin


Theoretical massNumber of molelcules
Total (without water)44,9113
Polymers44,9113
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4130 Å2
ΔGint-20 kcal/mol
Surface area19560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.683, 88.818, 89.121
Angle α, β, γ (deg.)90.000, 111.380, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein H-2 class I histocompatibility antigen, K-B alpha chain / H-2K(B)


Mass: 32199.971 Da / Num. of mol.: 2 / Fragment: Extracellular domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: H2-K1, H2-K / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01901
#2: Protein Beta-2-microglobulin / Beta-2 microglobulin


Mass: 11704.359 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: B2m / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01887
#3: Protein/peptide Ovalbumin epitope, EIINFEKL / Allergen Gal d II / Egg albumin / Plakalbumin


Mass: 1006.173 Da / Num. of mol.: 2 / Mutation: S1E / Source method: obtained synthetically / Details: synthetic peptide / References: UniProt: P01012
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 574 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.74 Å3/Da / Density % sol: 55.04 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 0.2M calcium acetate, 15% PEG 8K, 0.1M Na-malonate, pH 6, vapor diffusion, hanging drop, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.954 Å
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: Mar 27, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.954 Å / Relative weight: 1
ReflectionResolution: 2.2→100 Å / Num. obs: 49257 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 30.53 Å2 / Rmerge(I) obs: 0.094 / Net I/σ(I): 18.49
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
2.2-2.30.3350.385.964556615861550.4100
2.3-2.40.2750.3017.253792511951130.31799.9
2.4-2.50.2210.2538.545684433643270.26699.8
2.5-30.1370.1551314900914137141240.16399.9
3-3.50.0580.08123.875850720171920.08599.9
3.5-40.0340.06232.542067403140210.06599.8
4-4.50.0280.05337.326007248324820.056100
4.5-50.0250.04839.516313155915540.05199.7
5-60.0280.05235.418734179917960.05599.8
6-100.0270.0453719964195219440.04799.6
100.0180.0414752515555490.04398.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACT3.1data extraction
PHENIX1.6.1_357refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1vac

1vac


Resolution: 2.2→42.365 Å / Occupancy max: 1 / Occupancy min: 0 / FOM work R set: 0.766 / SU ML: 0.37 / σ(F): 0.02 / Phase error: 29.71 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.26 2248 5.09 %
Rwork0.1929 --
obs0.1963 44198 89.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 29.095 Å2 / ksol: 0.334 e/Å3
Displacement parametersBiso max: 121.29 Å2 / Biso mean: 27.1127 Å2 / Biso min: 6.63 Å2
Baniso -1Baniso -2Baniso -3
1--2.0059 Å20 Å2-0.7336 Å2
2--9.7958 Å20 Å2
3----7.7899 Å2
Refinement stepCycle: LAST / Resolution: 2.2→42.365 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6314 0 0 574 6888
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0076608
X-RAY DIFFRACTIONf_angle_d1.1168975
X-RAY DIFFRACTIONf_chiral_restr0.074918
X-RAY DIFFRACTIONf_plane_restr0.0041178
X-RAY DIFFRACTIONf_dihedral_angle_d14.7322483
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2-2.27870.34941880.26143714390279
2.2787-2.36990.32082200.23823755397581
2.3699-2.47770.32242170.22093928414584
2.4777-2.60830.27141910.21054015420686
2.6083-2.77170.29872110.21494168437989
2.7717-2.98570.27962100.20514228443891
2.9857-3.2860.28222420.19094408465095
3.286-3.76130.22582550.16444503475897
3.7613-4.73780.19752530.13984590484398
4.7378-42.37260.21172610.16564641490298

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