+Open data
-Basic information
Entry | Database: PDB / ID: 1f70 | ||||||
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Title | REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN | ||||||
Components | CALMODULIN | ||||||
Keywords | TRANSPORT PROTEIN / Calcium binding / EF hands / four-helix bundle | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Xenopus laevis (African clawed frog) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Chou, J. / Li, S. / Bax, A. | ||||||
Citation | Journal: J.Biomol.NMR / Year: 2000 Title: Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings. Authors: Chou, J.J. / Li, S. / Bax, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f70.cif.gz | 245.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f70.ent.gz | 214.9 KB | Display | PDB format |
PDBx/mmJSON format | 1f70.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f7/1f70 ftp://data.pdbj.org/pub/pdb/validation_reports/f7/1f70 | 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 | Mass: 8454.353 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Production host: Escherichia coli (E. coli) / References: UniProt: P62155, UniProt: P0DP33*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 refined using previous NMR restraints and newly measured dipolar couplings |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 100 mM KCL / pH: 7.0 / Pressure: ambient / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 10 |