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Yorodumi- PDB-2y5t: Crystal structure of the pathogenic autoantibody CIIC1 in complex... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2y5t | ||||||
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| Title | Crystal structure of the pathogenic autoantibody CIIC1 in complex with the triple-helical C1 peptide | ||||||
Components |
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Keywords | IMMUNE SYSTEM / ANTIBODY / RHEUMATOID ARTHRITIS / ARTHRITOGENIC | ||||||
| Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta Function and homology information | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Dobritzsch, D. / Lindh, I. / Schneider, N. / Uysal, H. / Nandakumar, K.S. / Burkhardt, H. / Schneider, G. / Holmdahl, R. | ||||||
Citation | Journal: Arthritis Rheum. / Year: 2011Title: Crystal Structure of an Arthritogenic Anticollagen Immune Complex. Authors: Dobritzsch, D. / Lindh, I. / Uysal, H. / Nandakumar, K.S. / Burkhardt, H. / Schneider, G. / Holmdahl, R. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2y5t.cif.gz | 216.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2y5t.ent.gz | 176 KB | Display | PDB format |
| PDBx/mmJSON format | 2y5t.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2y5t_validation.pdf.gz | 473.7 KB | Display | wwPDB validaton report |
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| Full document | 2y5t_full_validation.pdf.gz | 476.2 KB | Display | |
| Data in XML | 2y5t_validation.xml.gz | 23.4 KB | Display | |
| Data in CIF | 2y5t_validation.cif.gz | 34 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y5/2y5t ftp://data.pdbj.org/pub/pdb/validation_reports/y5/2y5t | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2vl5S 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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| Unit cell |
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Components
-Protein/peptide , 2 types, 3 molecules EGF
| #3: Protein/peptide | Mass: 3073.250 Da / Num. of mol.: 2 / Fragment: C1-EPITOPE / Source method: obtained synthetically Details: TRIPLE-HELICAL SYNTHETIC PEPTIDE, CHAINS CROSSLINKED AT C-TERMINUS, CONTAINS C1-EPITOPE OF COLLAGEN TYPE II FROM MOUSE FLANKED BY GPO REPEATS Source: (synth.) ![]() #4: Protein/peptide | | Mass: 3551.835 Da / Num. of mol.: 1 / Fragment: C1-EPITOPE / Source method: obtained synthetically Details: TRIPLE-HELICAL SYNTHETIC PEPTIDE, CHAINS CROSSLINKED AT C-TERMINUS, CONTAINS C1-EPITOPE OF COLLAGEN TYPE II FROM MOUSE FLANKED BY GPO REPEATS Source: (synth.) ![]() |
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-Antibody , 2 types, 2 molecules AB
| #1: Antibody | Mass: 24894.230 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: DISULFIDE BRIDGE BETWEEN A22 AND A96, A146 AND A201, A134 AND A218 A22 AND A96, A146 AND A201, A134 AND A218 Source: (natural) ![]() |
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| #2: Antibody | Mass: 24059.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: DISULFIDE BRIDGE BETWEEN B23 AND B92, B138 AND B198 Source: (natural) ![]() |
-Non-polymers , 3 types, 296 molecules 




| #5: Chemical | ChemComp-CL / | ||
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| #6: Chemical | | #7: Water | ChemComp-HOH / | |
-Details
| Nonpolymer details | L-HYDROXYPRO |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54 % / Description: NONE |
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| Crystal grow | pH: 8 Details: 100 MM TRIS PH 8.0, 55-57% (V/V) 2-METHYL-2,4-PENTANEDIOL. |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.979 |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 12, 2010 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
| Reflection | Resolution: 2.2→56.2 Å / Num. obs: 33244 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 5.2 % / Biso Wilson estimate: 38.5 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 11.5 |
| Reflection shell | Resolution: 2.2→2.32 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.63 / Mean I/σ(I) obs: 2 / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 2VL5 Resolution: 2.2→43.85 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.925 / SU B: 12.386 / SU ML: 0.141 / Cross valid method: THROUGHOUT / ESU R: 0.227 / ESU R Free: 0.201 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.RESIDUES A223-233, E1-5, E32-34, F1-5, F33-38, G1-3, G28-34 ARE DISORDERED AND NOT VISIBLE IN THE MAP
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 16.984 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.2→43.85 Å
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| Refine LS restraints |
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