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Yorodumi- PDB-1egs: NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETI... -
+Open data
-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 | ||||||
Components | GROES | ||||||
Keywords | CHAPERONIN / PROTEIN FOLDING / HEAT SHOCK | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / MOLECULAR DYNAMICS, SIMULATED ANNEALING | ||||||
Authors | Landry, S.J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 Title: Interplay of structure and disorder in cochaperonin mobile loops. Authors: Landry, S.J. / Taher, A. / Georgopoulos, C. / van der Vies, S.M. #1: Journal: Nature / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1egs.cif.gz | 55.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1egs.ent.gz | 43.5 KB | Display | PDB format |
PDBx/mmJSON format | 1egs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1egs_validation.pdf.gz | 354.2 KB | Display | wwPDB validaton report |
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Full document | 1egs_full_validation.pdf.gz | 456.9 KB | Display | |
Data in XML | 1egs_validation.xml.gz | 5.5 KB | Display | |
Data in CIF | 1egs_validation.cif.gz | 8.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eg/1egs ftp://data.pdbj.org/pub/pdb/validation_reports/eg/1egs | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Escherichia coli (E. coli) / References: UniProt: P0A6F9 |
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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 |