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Open data
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Basic information
Entry | Database: PDB / ID: 2k23 | ||||||
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Title | Solution Structure Analysis of the rLcn2 | ||||||
![]() | Lipocalin 2 | ||||||
![]() | TRANSPORT PROTEIN / beta barrel | ||||||
Function / homology | ![]() sequestering of iron ion / Metal sequestration by antimicrobial proteins / Iron uptake and transport / positive regulation of cell projection organization / cytoplasmic vesicle lumen / response to mycotoxin / siderophore transport / response to xenobiotic stimulus => GO:0009410 / enterobactin binding / response to herbicide ...sequestering of iron ion / Metal sequestration by antimicrobial proteins / Iron uptake and transport / positive regulation of cell projection organization / cytoplasmic vesicle lumen / response to mycotoxin / siderophore transport / response to xenobiotic stimulus => GO:0009410 / enterobactin binding / response to herbicide / Neutrophil degranulation / small molecule binding / cellular response to interleukin-1 / cellular response to nutrient levels / extrinsic apoptotic signaling pathway in absence of ligand / response to nutrient levels / response to bacterium / response to virus / cellular response to hydrogen peroxide / cellular response to tumor necrosis factor / positive regulation of cold-induced thermogenesis / protease binding / cellular response to lipopolysaccharide / response to oxidative stress / defense response to bacterium / iron ion binding / innate immune response / positive regulation of gene expression / extracellular space / extracellular region / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Zhang, F. / Lin, D.H. | ||||||
![]() | ![]() Title: NMR solution structure of rat lipocalin 2 Authors: Zhang, F. / Lin, D.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 916.7 KB | Display | ![]() |
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PDB format | ![]() | 801.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 20513.975 Da / Num. of mol.: 1 / Fragment: UNP residues 21-298 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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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: 0.8mM [U-99% 13C; U-99% 15N] sodium phosphate, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.8 mM / Component: sodium phosphate / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Ionic strength: 0.15 / pH: 6 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 150 / Conformers submitted total number: 15 |