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Yorodumi- PDB-1fb9: EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fb9 | |||||||||
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Title | EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN | |||||||||
Components | CALCITONIN ANALOGUE | |||||||||
Keywords | SIGNALING PROTEIN / alpha helix | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Oncorhynchus gorbuscha (pink salmon) | |||||||||
Method | SOLUTION NMR / distance geometry | |||||||||
Authors | Wu, H. / Mao, J. / Wang, Y. / Dou, H. | |||||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2003 Title: Solution structure and biological activity of recombinant salmon calcitonin S-sulfonated analog Authors: Wang, Y. / Dou, H. / Cao, C. / Zhang, N. / Ma, J. / Mao, J. / Wu, H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fb9.cif.gz | 101.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fb9.ent.gz | 86 KB | Display | PDB format |
PDBx/mmJSON format | 1fb9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fb/1fb9 ftp://data.pdbj.org/pub/pdb/validation_reports/fb/1fb9 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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: 3597.020 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oncorhynchus gorbuscha (pink salmon) / Organ: PAROTID Plasmid: PHARMACIA BIOTECH, PGEX-4T-3 GST GENE FUSION VECTOR Production host: Escherichia coli (E. coli) / References: GenBank: 459541, UniProt: Q8QG84*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details |
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Sample conditions | pH: 3.64 / Pressure: 1 atm / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 Details: the structures are based on a total of 530 restraints, 478 are NOE-derived distance constraints, 26 dihedral angle restraints, 26 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |