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- PDB-1egs: NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1egs | ||||||
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Title | NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES | ||||||
![]() | GROES | ||||||
![]() | CHAPERONIN / PROTEIN FOLDING / HEAT SHOCK | ||||||
Function / homology | ![]() GroEL-GroES complex / virion assembly / chaperone cofactor-dependent protein refolding / protein folding chaperone / unfolded protein binding / protein folding / protein-folding chaperone binding / response to heat / ATP binding / identical protein binding ...GroEL-GroES complex / virion assembly / chaperone cofactor-dependent protein refolding / protein folding chaperone / unfolded protein binding / protein folding / protein-folding chaperone binding / response to heat / ATP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / MOLECULAR DYNAMICS, SIMULATED ANNEALING | ||||||
![]() | Landry, S.J. | ||||||
![]() | ![]() Title: Interplay of structure and disorder in cochaperonin mobile loops. Authors: Landry, S.J. / Taher, A. / Georgopoulos, C. / van der Vies, S.M. #1: ![]() Title: Characterization of a Functionally Important Mobile Domain of Groes Authors: Landry, S.J. / Zeilstra-Ryalls, J. / Fayet, O. / Georgopoulos, C. / Gierasch, L.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.7 KB | Display | ![]() |
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PDB format | ![]() | 43.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 354.2 KB | Display | ![]() |
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Full document | ![]() | 456.9 KB | Display | |
Data in XML | ![]() | 5.5 KB | Display | |
Data in CIF | ![]() | 8.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 870.050 Da / Num. of mol.: 1 / Fragment: MOBILE LOOP Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 6.5 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian VXR500 / Manufacturer: Varian / Model: VXR500 / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: MOLECULAR DYNAMICS, SIMULATED ANNEALING / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | |||||||||
NMR ensemble | Conformers calculated total number: 20 / Conformers submitted total number: 20 |