+Open data
-Basic information
Entry | Database: PDB / ID: 6ew4 | ||||||
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Title | Human myelin protein P2 F57A mutant, monoclinic crystal form | ||||||
Components | Myelin P2 protein | ||||||
Keywords | LIPID TRANSPORT / fatty acid binding protein / beta barrel / portal region | ||||||
Function / homology | Function and homology information membrane organization / cholesterol binding / fatty acid transport / fatty acid binding / myelin sheath / extracellular exosome / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.271 Å | ||||||
Authors | Laulumaa, S. / Lehtimaki, M. / Kursula, P. | ||||||
Citation | Journal: BMC Struct. Biol. / Year: 2018 Title: Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the beta barrel in fatty acid binding proteins. Authors: Laulumaa, S. / Nieminen, T. / Raasakka, A. / Krokengen, O.C. / Safaryan, A. / Hallin, E.I. / Brysbaert, G. / Lensink, M.F. / Ruskamo, S. / Vattulainen, I. / Kursula, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ew4.cif.gz | 104.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ew4.ent.gz | 80.8 KB | Display | PDB format |
PDBx/mmJSON format | 6ew4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6ew4_validation.pdf.gz | 674 KB | Display | wwPDB validaton report |
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Full document | 6ew4_full_validation.pdf.gz | 674.7 KB | Display | |
Data in XML | 6ew4_validation.xml.gz | 10.4 KB | Display | |
Data in CIF | 6ew4_validation.cif.gz | 15.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/6ew4 ftp://data.pdbj.org/pub/pdb/validation_reports/ew/6ew4 | HTTPS FTP |
-Related structure data
Related structure data | 6ew2C 6ew5C 2wutS C: citing same article (ref.) S: Starting model for refinement |
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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: Protein | Mass: 14915.374 Da / Num. of mol.: 1 / Mutation: F57A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PMP2 / Production host: Escherichia coli (E. coli) / References: UniProt: P02689 |
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#2: Chemical | ChemComp-PLM / |
#3: 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: 2.11 Å3/Da / Density % sol: 41.71 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 40-42% PEG 6000 / PH range: 6-7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X12 / Wavelength: 1.1 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Jun 14, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.27→20 Å / Num. obs: 31892 / % possible obs: 96.8 % / Redundancy: 2.9 % / CC1/2: 0.996 / Rrim(I) all: 0.092 / Rsym value: 0.076 / Net I/σ(I): 8.2 |
Reflection shell | Resolution: 1.27→1.3 Å / Redundancy: 1.8 % / Mean I/σ(I) obs: 1.2 / Num. unique obs: 1880 / CC1/2: 0.436 / Rrim(I) all: 0.781 / Rsym value: 0.607 / % possible all: 77.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2wut Resolution: 1.271→19.112 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 27.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.271→19.112 Å
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Refine LS restraints |
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LS refinement shell |
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