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- PDB-1ln3: Structure of Human Phosphatidylcholine Transfer Protein in Comple... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ln3 | ||||||
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Title | Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein) | ||||||
![]() | Phosphatidylcholine transfer protein | ||||||
![]() | LIPID BINDING PROTEIN / START Domain | ||||||
Function / homology | ![]() phosphatidylcholine transporter activity / Mitochondrial Fatty Acid Beta-Oxidation / phosphatidylcholine binding / phospholipid transport / negative regulation of cold-induced thermogenesis / lipid transport / Synthesis of PC / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Roderick, S.L. / Chan, W.W. / Agate, D.S. / Olsen, L.R. / Vetting, M.W. / Rajashankar, K.R. / Cohen, D.E. | ||||||
![]() | ![]() Title: Structure of human phosphatidylcholine transfer protein in complex with its ligand. Authors: Roderick, S.L. / Chan, W.W. / Agate, D.S. / Olsen, L.R. / Vetting, M.W. / Rajashankar, K.R. / Cohen, D.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95 KB | Display | ![]() |
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PDB format | ![]() | 79.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological assembly is a monomer. Two monomers are related by approximately (1/2,1/2,1/2). |
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Components
#1: Protein | Mass: 25199.564 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 66.85 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: sodium formate, sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.7 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 28, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→27.5 Å / Num. all: 17846 / Num. obs: 17846 / % possible obs: 92.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.06 |
Reflection shell | Resolution: 2.9→3.08 Å / % possible all: 88 |
Reflection | *PLUS Highest resolution: 2.9 Å / Num. measured all: 60811 / Rmerge(I) obs: 0.06 |
Reflection shell | *PLUS % possible obs: 83.6 % / Rmerge(I) obs: 0.19 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 27.0871 Å2 / ksol: 0.356755 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.44 Å / Luzzati sigma a free: 0.65 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→27.53 Å
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Refine LS restraints |
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LS refinement shell | Highest resolution: 2.9 Å / Total num. of bins used: 6 /
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Xplor file |
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Refinement | *PLUS % reflection Rfree: 5 % / Rfactor Rwork: 0.226 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 3.08 Å / Rfactor Rfree: 0.361 / Rfactor Rwork: 0.279 |