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Yorodumi- PDB-2k6r: Protein folding on a highly rugged landscape: Experimental observ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2k6r | ||||||
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Title | Protein folding on a highly rugged landscape: Experimental observation of glassy dynamics and structural frustration | ||||||
Components | Full Sequence Design 1 Synthetic Superstable | ||||||
Keywords | DE NOVO PROTEIN / synthetic protein / non-natural amino acids / de novo protein design / rugged folding energy landscape / structural frustration | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Authors | Sadqi, M. / de Alba, E. / Perez-Jimenez, R. / Sanchez-Ruiz, J.M. / Munoz, V. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2009 Title: A designed protein as experimental model of primordial folding Authors: Sadqi, M. / de Alba, E. / Perez-Jimenez, R. / Sanchez-Ruiz, J.M. / Munoz, V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k6r.cif.gz | 209.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k6r.ent.gz | 184.7 KB | Display | PDB format |
PDBx/mmJSON format | 2k6r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2k6r_validation.pdf.gz | 356.9 KB | Display | wwPDB validaton report |
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Full document | 2k6r_full_validation.pdf.gz | 406 KB | Display | |
Data in XML | 2k6r_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 2k6r_validation.cif.gz | 23.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k6/2k6r ftp://data.pdbj.org/pub/pdb/validation_reports/k6/2k6r | HTTPS FTP |
-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: 3854.420 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic protein / Source: (synth.) synthetic construct (others) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1mM FSD-1SS, 0.05mM DSS, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O | |||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 5.0 / Pressure: ambient / Temperature: 323 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry 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: 300 / Conformers submitted total number: 20 / Representative conformer: 1 |