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Yorodumi- PDB-6ddm: Crystal Structure Analysis of the Epitope of an Anti-MICA Antibody -
+Open data
-Basic information
Entry | Database: PDB / ID: 6ddm | ||||||
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Title | Crystal Structure Analysis of the Epitope of an Anti-MICA Antibody | ||||||
Components |
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Keywords | IMMUNE SYSTEM / Fab fragment-antigen complex / immunoglobulin domain | ||||||
Function / homology | Function and homology information 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 / positive regulation of T cell mediated cytotoxicity / peptide antigen binding / immune response / external side of plasma membrane / signaling receptor binding / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å | ||||||
Authors | Matsumoto, M.L. | ||||||
Citation | Journal: MAbs / Year: 2019 Title: High-resolution glycosylation site-engineering method identifies MICA epitope critical for shedding inhibition activity of anti-MICA antibodies. Authors: Lombana, T.N. / Matsumoto, M.L. / Berkley, A.M. / Toy, E. / Cook, R. / Gan, Y. / Du, C. / Schnier, P. / Sandoval, W. / Ye, Z. / Schartner, J.M. / Kim, J. / Spiess, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ddm.cif.gz | 229.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ddm.ent.gz | 181.3 KB | Display | PDB format |
PDBx/mmJSON format | 6ddm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dd/6ddm ftp://data.pdbj.org/pub/pdb/validation_reports/dd/6ddm | HTTPS FTP |
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-Related structure data
Related structure data | 6ddrC 6ddvC 1f3dS 1hyrS 1nz8S 4m1gS S: Starting model for refinement C: citing same article (ref.) |
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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
#1: Antibody | Mass: 23219.854 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: chimeric Fab fragment consisting of murine variable domains with human constant domains Source: (gene. exp.) Mus musculus (house mouse) / Strain: Balb/c / Plasmid: pBR322 / Production host: Escherichia coli (E. coli) / Strain (production host): 64B4 |
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#2: Protein | Mass: 10578.635 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: alpha 3 domain of the MICA*008 allele co-expressed with Streptomyces plicatu EndoH in the presence of kifunensine Source: (gene. exp.) Homo sapiens (human) / Gene: MICA, hCG_2001511 / Plasmid: pAcgp67 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q96QC4 |
#3: Antibody | Mass: 23441.264 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: himeric Fab fragment consisting of murine variable domains with human constant domains Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pBR322 / Production host: Escherichia coli (E. coli) |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 46.17 % / Mosaicity: 0.498 ° |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.6 / Details: 0.1 M sodium acetate, pH 4.6, 25% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RAYONIX MX300-HS / Detector: CCD / Date: Oct 14, 2015 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.3→35 Å / Num. obs: 126363 / % possible obs: 99.6 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.059 / Rpim(I) all: 0.037 / Rrim(I) all: 0.07 / Χ2: 0.997 / Net I/σ(I): 8.5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1F3D, 4M1G, 1HYR, 1NZ8 Resolution: 1.3→35 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.964 / SU B: 2.755 / SU ML: 0.054 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.054 / ESU R Free: 0.054 Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 67.47 Å2 / Biso mean: 20.983 Å2 / Biso min: 11.7 Å2
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Refinement step | Cycle: final / Resolution: 1.3→35 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.3→1.334 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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