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Yorodumi- PDB-1ngl: HUMAN NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN (HNGAL), REGULAR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ngl | ||||||
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Title | HUMAN NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN (HNGAL), REGULARISED AVERAGE NMR STRUCTURE | ||||||
Components | PROTEIN (NGAL) | ||||||
Keywords | TRANSPORT PROTEIN / MMP-9 COMPONENT / LIPOCALIN | ||||||
Function / homology | Function and homology information siderophore transport / Metal sequestration by antimicrobial proteins / iron ion sequestering activity / enterobactin binding / small molecule binding / Iron uptake and transport / specific granule lumen / positive regulation of cold-induced thermogenesis / Interleukin-4 and Interleukin-13 signaling / defense response to bacterium ...siderophore transport / Metal sequestration by antimicrobial proteins / iron ion sequestering activity / enterobactin binding / small molecule binding / Iron uptake and transport / specific granule lumen / positive regulation of cold-induced thermogenesis / Interleukin-4 and Interleukin-13 signaling / defense response to bacterium / iron ion binding / innate immune response / apoptotic process / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Coles, M. / Diercks, T. / Muehlenweg, B. / Bartsch, S. / Zoelzer, V. / Tschesche, H. / Kessler, H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. Authors: Coles, M. / Diercks, T. / Muehlenweg, B. / Bartsch, S. / Zolzer, V. / Tschesche, H. / Kessler, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ngl.cif.gz | 75.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ngl.ent.gz | 57.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ngl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ng/1ngl ftp://data.pdbj.org/pub/pdb/validation_reports/ng/1ngl | HTTPS FTP |
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-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: 20703.697 Da / Num. of mol.: 1 / Fragment: MATURE SEQUENCE Source method: isolated from a genetically manipulated source Details: METHIONINE PRECEDES MATURE PROTEIN SEQUENCE / Source: (gene. exp.) Homo sapiens (human) / Cell: NEUTROPHIL / Cellular location: EXTRACELLULAR MATRIX / Production host: Escherichia coli (E. coli) / Strain (production host): BL21[DE3] / References: UniProt: P80188 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: MEAN STRUCTURE. STRUCTURE DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 15N AND 13C/15N LABELLED HNGAL. |
-Sample preparation
Sample conditions | Ionic strength: 50 mM / pH: 6.1 / Pressure: 1 atm / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX750 / Manufacturer: Bruker / Model: DMX750 / Field strength: 750 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |