+Open data
-Basic information
Entry | Database: PDB / ID: 1yut | ||||||
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Title | Solution structure of Calcium-S100A13 (minimized mean structure) | ||||||
Components | S100 calcium-binding protein A13 | ||||||
Keywords | METAL BINDING PROTEIN / S100A13 / EF hand calcium-binding proteins / Copper(II) / Structural Genomics / Structural Proteomics in Europe / SPINE | ||||||
Function / homology | Function and homology information positive regulation of interleukin-1 alpha production / RAGE receptor binding / mast cell degranulation / fibroblast growth factor binding / positive regulation of cytokine production / calcium-dependent protein binding / protein transport / positive regulation of canonical NF-kappaB signal transduction / copper ion binding / lipid binding ...positive regulation of interleukin-1 alpha production / RAGE receptor binding / mast cell degranulation / fibroblast growth factor binding / positive regulation of cytokine production / calcium-dependent protein binding / protein transport / positive regulation of canonical NF-kappaB signal transduction / copper ion binding / lipid binding / calcium ion binding / positive regulation of cell population proliferation / nucleolus / perinuclear region of cytoplasm / protein homodimerization activity / extracellular space / zinc ion binding / extracellular region / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / Restrained energy minimization | ||||||
Model type details | minimized average | ||||||
Authors | Arnesano, F. / Banci, L. / Bertini, I. / Fantoni, A. / Tenori, L. / Viezzoli, M.S. / Structural Proteomics in Europe (SPINE) | ||||||
Citation | Journal: Angew.Chem.Int.Ed.Engl. / Year: 2005 Title: Structural Interplay between Calcium(II) and Copper(II) Binding to S100A13 Protein Authors: Arnesano, F. / Banci, L. / Bertini, I. / Fantoni, A. / Tenori, L. / Viezzoli, M.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1yut.cif.gz | 78 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1yut.ent.gz | 58.8 KB | Display | PDB format |
PDBx/mmJSON format | 1yut.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yu/1yut ftp://data.pdbj.org/pub/pdb/validation_reports/yu/1yut | HTTPS FTP |
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-Related structure data
Related structure data | 1yurC 1yusC 1yuuC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11490.193 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: S100A13 / Plasmid: pET21S100 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21Gold(DE3) / References: UniProt: Q99584 #2: Chemical | ChemComp-CA / |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 3D techniques |
-Sample preparation
Details | Contents: 1.5mM 13C, 15N labeled S100A13 / Solvent system: 20mM sodium acetate buffer, 10% D2O |
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Sample conditions | Ionic strength: 20mM sodium acetate buffer / pH: 5.6 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: Restrained energy minimization / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 1 |