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Yorodumi- PDB-1i5j: NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS -
+Open data
-Basic information
Entry | Database: PDB / ID: 1i5j | ||||||
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Title | NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS | ||||||
Components | APOLIPOPROTEIN CII | ||||||
Keywords | LIPID TRANSPORT / PROTEIN-LIPID INTERACTION / AMPHIPATHIC ALPHA HELIX | ||||||
Function / homology | Function and homology information positive regulation of very-low-density lipoprotein particle remodeling / positive regulation of phospholipid catabolic process / triglyceride-rich lipoprotein particle remodeling / positive regulation of triglyceride catabolic process / chylomicron remodeling / lipoprotein lipase activator activity / lipase inhibitor activity / negative regulation of cholesterol transport / negative regulation of very-low-density lipoprotein particle clearance / spherical high-density lipoprotein particle ...positive regulation of very-low-density lipoprotein particle remodeling / positive regulation of phospholipid catabolic process / triglyceride-rich lipoprotein particle remodeling / positive regulation of triglyceride catabolic process / chylomicron remodeling / lipoprotein lipase activator activity / lipase inhibitor activity / negative regulation of cholesterol transport / negative regulation of very-low-density lipoprotein particle clearance / spherical high-density lipoprotein particle / Assembly of active LPL and LIPC lipase complexes / negative regulation of lipid metabolic process / positive regulation of lipoprotein lipase activity / intermediate-density lipoprotein particle / chylomicron remnant clearance / negative regulation of receptor-mediated endocytosis / very-low-density lipoprotein particle remodeling / Chylomicron remodeling / Chylomicron assembly / positive regulation of fatty acid biosynthetic process / high-density lipoprotein particle clearance / chylomicron / phospholipid efflux / positive regulation of phospholipase activity / very-low-density lipoprotein particle / reverse cholesterol transport / low-density lipoprotein particle / triglyceride homeostasis / HDL remodeling / cholesterol efflux / phospholipase activator activity / phospholipase binding / lipid catabolic process / Retinoid metabolism and transport / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / molecular function activator activity / cholesterol homeostasis / early endosome / lipid binding / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle, Cartesian dynamics | ||||||
Authors | MacRaild, C.A. / Hatters, D.M. / Howlett, G.J. / Gooley, P.R. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate. Authors: MacRaild, C.A. / Hatters, D.M. / Howlett, G.J. / Gooley, P.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i5j.cif.gz | 513.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i5j.ent.gz | 430.7 KB | Display | PDB format |
PDBx/mmJSON format | 1i5j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1i5j_validation.pdf.gz | 344.9 KB | Display | wwPDB validaton report |
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Full document | 1i5j_full_validation.pdf.gz | 538.8 KB | Display | |
Data in XML | 1i5j_validation.xml.gz | 28.5 KB | Display | |
Data in CIF | 1i5j_validation.cif.gz | 45.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i5/1i5j ftp://data.pdbj.org/pub/pdb/validation_reports/i5/1i5j | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8921.864 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P02655 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.8 mM U-15N ApoC-II; 220 mM SDS; 20 mM sodium acetate, pH5 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 20 mM sodium acetate, 220 mM sodium dodecy sulfate pH: 5.0 / Pressure: ambient / Temperature: 313 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle, Cartesian dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: Structures with favourable non-bond energy and minimal constraint violations Conformers calculated total number: 100 / Conformers submitted total number: 25 |