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- PDB-2k6r: Protein folding on a highly rugged landscape: Experimental observ... -
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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 | ||||||
![]() | Full Sequence Design 1 Synthetic Superstable | ||||||
![]() | 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 | ||||||
![]() | Sadqi, M. / de Alba, E. / Perez-Jimenez, R. / Sanchez-Ruiz, J.M. / Munoz, V. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 209.7 KB | Display | ![]() |
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PDB format | ![]() | 184.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 356.9 KB | Display | ![]() |
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Full document | ![]() | 406 KB | Display | |
Data in XML | ![]() | 16.1 KB | Display | |
Data in CIF | ![]() | 23.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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 |