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Yorodumi- PDB-1bwx: THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39... -
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-Basic information
Entry | Database: PDB / ID: 1bwx | ||||||
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Title | THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES | ||||||
Components | PARATHYROID HORMONE | ||||||
Keywords | PEPTIDE HORMONE / SOLUTION STRUCTURE / HUMAN PARATHYROID HORMONE | ||||||
Function / homology | Function and homology information type 1 parathyroid hormone receptor binding / parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / positive regulation of osteoclast proliferation / negative regulation of apoptotic process in bone marrow cell / hormone-mediated apoptotic signaling pathway / response to parathyroid hormone / positive regulation of cell proliferation in bone marrow / magnesium ion homeostasis / positive regulation of signal transduction ...type 1 parathyroid hormone receptor binding / parathyroid hormone receptor binding / negative regulation of bone mineralization involved in bone maturation / positive regulation of osteoclast proliferation / negative regulation of apoptotic process in bone marrow cell / hormone-mediated apoptotic signaling pathway / response to parathyroid hormone / positive regulation of cell proliferation in bone marrow / magnesium ion homeostasis / positive regulation of signal transduction / macromolecule biosynthetic process / response to fibroblast growth factor / phosphate ion homeostasis / cAMP metabolic process / response to vitamin D / negative regulation of chondrocyte differentiation / Class B/2 (Secretin family receptors) / positive regulation of inositol phosphate biosynthetic process / peptide hormone receptor binding / bone mineralization / Rho protein signal transduction / activation of phospholipase C activity / positive regulation of glycogen biosynthetic process / positive regulation of bone mineralization / response to cadmium ion / homeostasis of number of cells within a tissue / bone resorption / skeletal system development / positive regulation of glucose import / response to lead ion / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / intracellular calcium ion homeostasis / cell-cell signaling / G alpha (s) signalling events / regulation of gene expression / response to ethanol / transcription by RNA polymerase II / receptor ligand activity / response to xenobiotic stimulus / G protein-coupled receptor signaling pathway / negative regulation of gene expression / positive regulation of gene expression / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
Authors | Marx, U.C. / Roesch, P. / Adermann, K. / Bayer, P. / Forssmann, W.-G. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2000 Title: Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37). Authors: Marx, U.C. / Adermann, K. / Bayer, P. / Forssmann, W.G. / Rosch, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bwx.cif.gz | 129.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bwx.ent.gz | 110 KB | Display | PDB format |
PDBx/mmJSON format | 1bwx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bw/1bwx ftp://data.pdbj.org/pub/pdb/validation_reports/bw/1bwx | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4537.273 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-39 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01270 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: THE DISTANCE RESTRAINTS USED FOR STRUCTURE CALCULATION WERE OBTAINED FROM TWO-DIMENSIONAL HOMONUCLEAR 1H- NOESY SPECTRA. |
-Sample preparation
Details | Contents: 10% D2O/90% H2O |
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Sample conditions | Ionic strength: 320 mM / pH: 5.8 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1 Details: THE STRUCTURE CALCULATION FOLLOWED STANDARD PROCEDURES EMPLOYING A HYBRID DISTANCE GEOMETRY MOLECULAR DYNAMICS APPROACH WITH SIMULATED ANNEALING REFINEMENT AND SUBSEQUENT ENERGY MINIMIZATION. ...Details: THE STRUCTURE CALCULATION FOLLOWED STANDARD PROCEDURES EMPLOYING A HYBRID DISTANCE GEOMETRY MOLECULAR DYNAMICS APPROACH WITH SIMULATED ANNEALING REFINEMENT AND SUBSEQUENT ENERGY MINIMIZATION. FOR THE REFINEMENT THE DIELECTRIC CONSTANT WAS CHANGED TO 4. STRUCTURE PARAMETERS WERE EXTRACTED FROM THE STANDARD FILES PARALLHDG.PRO AND TOPALLHDG.PRO OF X-PLOR 3.1. IN EACH ROUND OF THE STRUCTURE CALCULATION 30 STRUCTURES WERE CALCULATED. OF THE 30 STRUCTURES RESULTING FROM THE FINAL ROUND OF STRUCTURE CALCULATION, THOSE 10 STRUCTURES THAT SHOWED THE LOWEST TOTAL ENERGY VALUES WERE SELECTED FOR FURTHER CHARACTERIZATION. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY, AGREEMENT WITH EXPERIMENTAL DATA Conformers calculated total number: 30 / Conformers submitted total number: 10 |