+Open data
-Basic information
Entry | Database: PDB / ID: 6ent | ||||||||||||
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Title | Structure of the rat RKIP variant delta143-146 | ||||||||||||
Components | Phosphatidylethanolamine-binding protein 1 | ||||||||||||
Keywords | SIGNALING PROTEIN / RKIP / PEBP / PBP | ||||||||||||
Function / homology | Function and homology information positive regulation of acetylcholine biosynthetic process / positive regulation of acetylcholine metabolic process / Negative regulation of MAPK pathway / MAP2K and MAPK activation / regulation of the force of heart contraction / receptor serine/threonine kinase binding / mitogen-activated protein kinase binding / sperm capacitation / eating behavior / response to corticosterone ...positive regulation of acetylcholine biosynthetic process / positive regulation of acetylcholine metabolic process / Negative regulation of MAPK pathway / MAP2K and MAPK activation / regulation of the force of heart contraction / receptor serine/threonine kinase binding / mitogen-activated protein kinase binding / sperm capacitation / eating behavior / response to corticosterone / negative regulation of MAPK cascade / spermatid development / positive regulation of cAMP-mediated signaling / axon terminus / response to electrical stimulus / response to cAMP / response to organonitrogen compound / positive regulation of mitotic nuclear division / negative regulation of protein phosphorylation / response to activity / response to organic substance / hippocampus development / serine-type endopeptidase inhibitor activity / response to organic cyclic compound / response to toxic substance / kinase binding / response to calcium ion / MAPK cascade / synaptic vesicle / apical part of cell / response to ethanol / response to oxidative stress / mitochondrial outer membrane / response to xenobiotic stimulus / signaling receptor binding / neuronal cell body / lipid binding / protein kinase binding / enzyme binding / cell surface / extracellular space / ATP binding Similarity search - Function | ||||||||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.66 Å | ||||||||||||
Authors | Koelmel, W. / Hirschbeck, M. / Schindelin, H. / Lorenz, K. / Kisker, C. | ||||||||||||
Funding support | United States, Germany, 3items
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Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017 Title: Conserved salt-bridge competition triggered by phosphorylation regulates the protein interactome. Authors: Skinner, J.J. / Wang, S. / Lee, J. / Ong, C. / Sommese, R. / Sivaramakrishnan, S. / Koelmel, W. / Hirschbeck, M. / Schindelin, H. / Kisker, C. / Lorenz, K. / Sosnick, T.R. / Rosner, M.R. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ent.cif.gz | 88 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ent.ent.gz | 67.1 KB | Display | PDB format |
PDBx/mmJSON format | 6ent.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/en/6ent ftp://data.pdbj.org/pub/pdb/validation_reports/en/6ent | HTTPS FTP |
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-Related structure data
Related structure data | 6ensSC S: Starting model for refinement C: citing same article (ref.) |
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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 on special symmetry positions |
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-Components
#1: Protein | Mass: 21212.816 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Pebp1, Pbp, Pebp / Production host: Escherichia coli (E. coli) / References: UniProt: P31044 |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-CL / |
#4: 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: 2.7 Å3/Da / Density % sol: 54.52 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop / Details: PEG 3350, sodium fluoride |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.91841 Å |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Sep 23, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 2.66→55.63 Å / Num. obs: 6706 / % possible obs: 100 % / Redundancy: 12.1 % / Rmerge(I) obs: 0.106 / Net I/σ(I): 14.7 |
Reflection shell | Resolution: 2.66→2.81 Å / Redundancy: 11.5 % / Rmerge(I) obs: 1.465 / Mean I/σ(I) obs: 1.8 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6ENS Resolution: 2.66→20 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.933 / SU B: 31.629 / SU ML: 0.293 / Cross valid method: THROUGHOUT / ESU R: 0.849 / ESU R Free: 0.322 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 86.067 Å2
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Refinement step | Cycle: 1 / Resolution: 2.66→20 Å
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Refine LS restraints |
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