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Open data
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Basic information
Entry | Database: PDB / ID: 6xw9 | ||||||
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Title | Human myelin protein P2 mutant K120S | ||||||
![]() | Myelin P2 protein | ||||||
![]() | LIPID BINDING PROTEIN / mutant / peripheral membrane protein / FABP / beta barrel | ||||||
Function / homology | ![]() membrane organization / cholesterol binding / fatty acid transport / fatty acid binding / myelin sheath / extracellular exosome / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ruskamo, S. / Lehtimaki, M. / Kursula, P. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice. Authors: Ruskamo, S. / Krokengen, O.C. / Kowal, J. / Nieminen, T. / Lehtimaki, M. / Raasakka, A. / Dandey, V.P. / Vattulainen, I. / Stahlberg, H. / Kursula, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.3 KB | Display | ![]() |
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PDB format | ![]() | 47.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 613.1 KB | Display | ![]() |
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Full document | ![]() | 613.3 KB | Display | |
Data in XML | ![]() | 7.3 KB | Display | |
Data in CIF | ![]() | 8.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6stsC ![]() 6xu5C ![]() 6xu9C ![]() 6xuaC ![]() 6xuwC ![]() 6xvqC ![]() 6xvrC ![]() 6xvsC ![]() 6xvyC ![]() 2wutS S: Starting model for refinement C: citing same article ( |
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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
#1: Protein | Mass: 14949.368 Da / Num. of mol.: 1 / Mutation: K120S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CL / |
#3: Chemical | ChemComp-PLM / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.44 Å3/Da / Density % sol: 64.23 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5 / Details: 30% PEG 6000, 0.1 M citrate pH 5.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Mar 24, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→40 Å / Num. obs: 4976 / % possible obs: 99.6 % / Redundancy: 7.2 % / Biso Wilson estimate: 72 Å2 / CC1/2: 0.998 / Rrim(I) all: 0.144 / Rsym value: 0.133 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 2.9→2.98 Å / Mean I/σ(I) obs: 1.8 / Num. unique obs: 336 / CC1/2: 0.859 / Rrim(I) all: 1.145 / Rsym value: 1.065 / % possible all: 97.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2wut Resolution: 2.9→40 Å / Cross valid method: FREE R-VALUE
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Displacement parameters | Biso mean: 73.31 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→40 Å
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Refine LS restraints |
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