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- PDB-8hsw: CRYSTAL STRUCTURE OF BAT MHC CLASS I MYLU-B-67 FOR 2.1 ANGSTROM -

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Basic information

Entry
Database: PDB / ID: 8hsw
TitleCRYSTAL STRUCTURE OF BAT MHC CLASS I MYLU-B-67 FOR 2.1 ANGSTROM
Components
  • Beta-2-microglobulinBeta-2 microglobulin
  • Ig-like domain-containing protein
  • THR-PRO-GLN-SER-ALA-PRO-HIS-GLY-VAL
KeywordsIMMUNE SYSTEM / MHC / IMMUNOLIGY / IMMUNE SYSTEM TRANSFERASE COMPLEX.
Function / homology
Function and homology information


antigen processing and presentation of peptide antigen via MHC class I / lumenal side of endoplasmic reticulum membrane / MHC class I protein complex / phagocytic vesicle membrane / immune response / extracellular region
Similarity search - Function
MHC class I, alpha chain, C-terminal / MHC_I C-terminus / 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. ...MHC class I, alpha chain, C-terminal / MHC_I C-terminus / 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 / Nucleic acid-binding, OB-fold / Immunoglobulin-like fold
Similarity search - Domain/homology
Ig-like domain-containing protein / Beta-2-microglobulin
Similarity search - Component
Biological speciesMyotis lucifugus (little brown bat)
Pteropus alecto (black flying fox)
Severe acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.03 Å
AuthorsWang, S.Q. / Zhang, N.Z.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: CRYSTAL STRUCTURE OF BAT MHC CLASS I MYLU-B-67 FOR 2.1 ANGSTROM
Authors: Wang, S.Q. / Zhang, N.Z.
History
DepositionDec 20, 2022Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Dec 20, 2023Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ig-like domain-containing protein
B: Beta-2-microglobulin
C: THR-PRO-GLN-SER-ALA-PRO-HIS-GLY-VAL


Theoretical massNumber of molelcules
Total (without water)44,3673
Polymers44,3673
Non-polymers00
Water61334
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3820 Å2
ΔGint-18 kcal/mol
Surface area19160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)75.737, 80.150, 144.243
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein Ig-like domain-containing protein


Mass: 32112.572 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Myotis lucifugus (little brown bat) / Gene: B-67 / Production host: Escherichia coli (E. coli) / References: UniProt: G1PNR4
#2: Protein Beta-2-microglobulin / Beta-2 microglobulin


Mass: 11360.733 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pteropus alecto (black flying fox) / Gene: PAL_GLEAN10023531 / Production host: Escherichia coli (E. coli) / References: UniProt: L5K3Y9
#3: Protein/peptide THR-PRO-GLN-SER-ALA-PRO-HIS-GLY-VAL


Mass: 893.962 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Production host: Escherichia coli (E. coli)
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 34 / 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: 2.47 Å3/Da / Density % sol: 50.14 %
Crystal growTemperature: 300 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 1.2 M Potassium sodium tartrate tetrahydrate 0.1 M Tris

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.987 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 31, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.987 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 21262 / % possible obs: 98.9 % / Redundancy: 5.8 % / Rpim(I) all: 0.103 / Net I/σ(I): 6.2
Reflection shellResolution: 2→2.03 Å / Redundancy: 4.4 % / Mean I/σ(I) obs: 0.636 / Num. unique obs: 1374 / Rsym value: 0.231

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Processing

Software
NameVersionClassification
REFMAC5.8.0123refinement
HKL-30007.21data reduction
HKL-30007.21data scaling
PHASER2.7.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.03→30.8 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.925 / SU B: 9.964 / SU ML: 0.241 / Cross valid method: THROUGHOUT / ESU R: 0.404 / ESU R Free: 0.254 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2619 977 5 %RANDOM
Rwork0.2342 ---
obs0.23556 18531 67.85 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 45.804 Å2
Baniso -1Baniso -2Baniso -3
1--0.04 Å2-0 Å20 Å2
2---0.04 Å2-0 Å2
3---0.08 Å2
Refinement stepCycle: 1 / Resolution: 2.03→30.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3129 0 0 34 3163
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0133229
X-RAY DIFFRACTIONr_bond_other_d0.0010.0172799
X-RAY DIFFRACTIONr_angle_refined_deg1.5271.6584395
X-RAY DIFFRACTIONr_angle_other_deg1.2121.5796516
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.5425383
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.77321.837196
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.87915501
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.3061525
X-RAY DIFFRACTIONr_chiral_restr0.0650.2392
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.023663
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02724
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.1014.7461541
X-RAY DIFFRACTIONr_mcbond_other3.0994.7461540
X-RAY DIFFRACTIONr_mcangle_it4.8177.1141921
X-RAY DIFFRACTIONr_mcangle_other4.8177.1131922
X-RAY DIFFRACTIONr_scbond_it3.2935.0911688
X-RAY DIFFRACTIONr_scbond_other3.2925.0911689
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other5.2817.5032475
X-RAY DIFFRACTIONr_long_range_B_refined7.7254.6253573
X-RAY DIFFRACTIONr_long_range_B_other7.72154.6293574
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.03→2.083 Å /
RfactorNum. reflection
Rfree0.531 1
Rwork0.279 21

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