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Yorodumi- PDB-1hth: The solution structure of cyclic human parathyroid hormone fragme... -
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-Basic information
Entry | Database: PDB / ID: 1hth | ||||||
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Title | The solution structure of cyclic human parathyroid hormone fragment 1-34, NMR, 10 structures | ||||||
Components | CYCLIC PARATHYROID HORMONE | ||||||
Keywords | HORMONE / HUMAN PARATHYROID HORMONE / CYCLIC / ORNITHINE / NORLEUCINE | ||||||
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 / : / 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 | Roesch, P. / Seidel, G. / Schaefer, W. / Esswein, A. / Hofmann, E. | ||||||
Citation | Journal: Febs Lett. / Year: 1999 Title: The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution. Authors: Weidler, M. / Marx, U.C. / Seidel, G. / Schaefer, W. / Hoffmann, E. / Esswein, A. / Roesch, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hth.cif.gz | 118.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hth.ent.gz | 102 KB | Display | PDB format |
PDBx/mmJSON format | 1hth.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ht/1hth ftp://data.pdbj.org/pub/pdb/validation_reports/ht/1hth | 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: 4116.704 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-34 / Mutation: M8NLE, K13ORN, S17E, M18NLE 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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-Sample preparation
Sample conditions | pH: 5.0 / Temperature: 298 K |
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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 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY, AGREEMENT WITH EXPERIMENTAL DATA Conformers calculated total number: 50 / Conformers submitted total number: 10 |