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- PDB-1cmc: THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cmc | ||||||
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Title | THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR | ||||||
![]() | MET REPRESSOR | ||||||
![]() | DNA-BINDING REGULATORY PROTEIN | ||||||
Function / homology | ![]() methionine biosynthetic process / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Somers, W.S. / Phillips, S.E.V. | ||||||
![]() | ![]() Title: Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor. Authors: Rafferty, J.B. / Somers, W.S. / Saint-Girons, I. / Phillips, S.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.3 KB | Display | ![]() |
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PDB format | ![]() | 45.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 482 KB | Display | ![]() |
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Full document | ![]() | 496.2 KB | Display | |
Data in XML | ![]() | 8.4 KB | Display | |
Data in CIF | ![]() | 12.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: THE IDENTITY OF RESIDUES 106 A AND 106 B IS UNKNOWN. EACH INTERACTS WITH HIS 14, GLU 19, A SYMMETRY RELATED GLU 103, AND THE C-TERMINUS. THE MAGNITUDE OF THE DENSITY PEAK SUGGESTS ATOMIC NUMBER IN ...1: THE IDENTITY OF RESIDUES 106 A AND 106 B IS UNKNOWN. EACH INTERACTS WITH HIS 14, GLU 19, A SYMMETRY RELATED GLU 103, AND THE C-TERMINUS. THE MAGNITUDE OF THE DENSITY PEAK SUGGESTS ATOMIC NUMBER IN RANGE 25 - 35. IT IS POSSIBLY ARSENIC FROM BUFFER. IN REFINEMENT IT WAS MODELLED BY A MAGNESIUM ION WITH OCCUPANCY 2.0. |
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Components
#1: Protein | Mass: 12027.557 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Nonpolymer details | THE IDENTITY OF RESIDUES 106 A AND 106 B IS UNKNOWN. EACH INTERACTS WITH HIS 14, GLU 19, A SYMMETRY ...THE IDENTITY OF RESIDUES 106 A AND 106 B IS UNKNOWN. EACH INTERACTS WITH HIS 14, GLU 19, A SYMMETRY RELATED GLU 103, AND THE C-TERMINUS. THE MAGNITUDE OF THE DENSITY PEAK SUGGESTS ATOMIC NUMBER IN RANGE 25 - 35. IT IS POSSIBLY ARSENIC FROM BUFFER. IN REFINEMENT | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.51 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: microdialysis / pH: 6.2 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.183 / Highest resolution: 1.8 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / σ(F): 3 / Rfactor obs: 0.183 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 6.2 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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