+Open data
-Basic information
Entry | Database: PDB / ID: 1pko | ||||||
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Title | Myelin Oligodendrocyte Glycoprotein (MOG) | ||||||
Components | Myelin Oligodendrocyte Glycoprotein | ||||||
Keywords | IMMUNE SYSTEM / IgV-domain | ||||||
Function / homology | Function and homology information response to lipid / response to folic acid / regulation of cytokine production / T cell receptor signaling pathway / cell adhesion / external side of plasma membrane / signaling receptor binding / cell surface Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.45 Å | ||||||
Authors | Breithaupt, C. / Schubart, A. / Zander, H. / Skerra, A. / Huber, R. / Linington, C. / Jacob, U. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2003 Title: Structural insights into the antigenicity of myelin oligodendrocyte glycoprotein Authors: Breithaupt, C. / Schubart, A. / Zander, H. / Skerra, A. / Huber, R. / Linington, C. / Jacob, U. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pko.cif.gz | 37.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pko.ent.gz | 28.6 KB | Display | PDB format |
PDBx/mmJSON format | 1pko.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1pko_validation.pdf.gz | 427.5 KB | Display | wwPDB validaton report |
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Full document | 1pko_full_validation.pdf.gz | 429.5 KB | Display | |
Data in XML | 1pko_validation.xml.gz | 8.2 KB | Display | |
Data in CIF | 1pko_validation.cif.gz | 11 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pk/1pko ftp://data.pdbj.org/pub/pdb/validation_reports/pk/1pko | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 15975.648 Da / Num. of mol.: 1 / Fragment: N-terminal Ig domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: MOG / Plasmid: pQE-12 / Production host: Escherichia coli (E. coli) / Strain (production host): B834(DE3) / References: UniProt: Q63345 |
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#2: 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: 1.72 Å3/Da / Density % sol: 27.85 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.4 Details: Tris/HCl, PEG8000, MgCl2, NaCl, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 291K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source | Source: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.05 Å | ||||||||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 9, 2002 | ||||||||||||||||||
Radiation |
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Radiation wavelength | Wavelength: 1.05 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Resolution: 1.45→20 Å / Num. obs: 20287 / % possible obs: 99.3 % / Redundancy: 3.9 % / Biso Wilson estimate: 17.2 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 28.1 | ||||||||||||||||||
Reflection shell | Resolution: 1.45→1.47 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.398 / Mean I/σ(I) obs: 3.9 / Num. unique all: 801 / % possible all: 99.6 | ||||||||||||||||||
Reflection | *PLUS Num. obs: 20292 | ||||||||||||||||||
Reflection shell | *PLUS % possible obs: 99.6 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.45→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 20.2 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.45→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.45→1.48 Å
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Refinement | *PLUS Rfactor Rwork: 0.195 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |