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Yorodumi- PDB-6f3w: Backbone structure of free bradykinin (BK) in DDM/CHS detergent m... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6f3w | |||||||||||||||
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Title | Backbone structure of free bradykinin (BK) in DDM/CHS detergent micelle determined by MAS SSNMR | |||||||||||||||
Components | Kininogen-1 | |||||||||||||||
Keywords | MEMBRANE PROTEIN / GPCR / DNP | |||||||||||||||
Function / homology | Function and homology information negative regulation of blood coagulation / negative regulation of cell adhesion / cysteine-type endopeptidase inhibitor activity / Intrinsic Pathway of Fibrin Clot Formation / Peptide ligand-binding receptors / platelet alpha granule lumen / Post-translational protein phosphorylation / negative regulation of proteolysis / hormone activity / vasodilation ...negative regulation of blood coagulation / negative regulation of cell adhesion / cysteine-type endopeptidase inhibitor activity / Intrinsic Pathway of Fibrin Clot Formation / Peptide ligand-binding receptors / platelet alpha granule lumen / Post-translational protein phosphorylation / negative regulation of proteolysis / hormone activity / vasodilation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / blood coagulation / Platelet degranulation / heparin binding / positive regulation of cytosolic calcium ion concentration / G alpha (i) signalling events / G alpha (q) signalling events / collagen-containing extracellular matrix / blood microparticle / inflammatory response / positive regulation of apoptotic process / endoplasmic reticulum lumen / signaling receptor binding / extracellular space / extracellular exosome / zinc ion binding / extracellular region / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||
Method | SOLID-STATE NMR / torsion angle dynamics | |||||||||||||||
Authors | Mao, J. / Lopez, J.J. / Shukla, A.K. / Kuenze, G. / Meiler, J. / Schwalbe, H. / Michel, H. / Glaubitz, C. | |||||||||||||||
Funding support | Germany, United States, 4items
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Citation | Journal: Nat. Chem. Biol. / Year: 2018 Title: The molecular basis of subtype selectivity of human kinin G-protein-coupled receptors. Authors: Joedicke, L. / Mao, J. / Kuenze, G. / Reinhart, C. / Kalavacherla, T. / Jonker, H.R.A. / Richter, C. / Schwalbe, H. / Meiler, J. / Preu, J. / Michel, H. / Glaubitz, C. #1: Journal: Angew. Chem. Int. Ed. Engl. / Year: 2008 Title: The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy. Authors: Lopez, J.J. / Shukla, A.K. / Reinhart, C. / Schwalbe, H. / Michel, H. / Glaubitz, C. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6f3w.cif.gz | 35.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6f3w.ent.gz | 26.1 KB | Display | PDB format |
PDBx/mmJSON format | 6f3w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f3/6f3w ftp://data.pdbj.org/pub/pdb/validation_reports/f3/6f3w | HTTPS FTP |
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-Related structure data
Related structure data | 6f27C 6f3vC 6f3xC 6f3yC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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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/peptide | Mass: 1062.224 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans / Source: (synth.) Homo sapiens (human) / References: UniProt: P01042 |
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-Experimental details
-Experiment
Experiment | Method: SOLID-STATE NMR | ||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 125 mM / Label: LT / pH: 7.4 / Pressure: 1 atm / Temperature: 200 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / 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: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 500 / Conformers submitted total number: 10 |