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Open data
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Basic information
Entry | Database: PDB / ID: 1b9m | ||||||
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Title | REGULATOR FROM ESCHERICHIA COLI | ||||||
![]() | PROTEIN (MODE) | ||||||
![]() | TRANSCRIPTION / DNA-BINDING / GENE REGULATION / WINGED HELIX TURN HELIX / MOLYBDATE / OB FOLD | ||||||
Function / homology | ![]() ModE complex / molybdate ion transport / negative regulation of DNA-templated transcription initiation / molybdenum ion binding / cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hall, D.R. / Gourley, D.G. / Hunter, W.N. | ||||||
![]() | ![]() Title: The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds. Authors: Hall, D.R. / Gourley, D.G. / Leonard, G.A. / Duke, E.M. / Anderson, L.A. / Boxer, D.H. / Hunter, W.N. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1999 Title: Two crystal forms of ModE, the molybdate-dependent transcriptional regulator from Escherichia coli. Authors: Hall, D.R. / Gourley, D.G. / Duke, E.M. / Leonard, G.A. / Anderson, L.A. / Pau, R.N. / Boxer, D.H. / Hunter, W.N. #2: Journal: Eur.J.Biochem. / Year: 1997 Title: Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli. Authors: Anderson, L.A. / Palmer, T. / Price, N.C. / Bornemann, S. / Boxer, D.H. / Pau, R.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.8 KB | Display | ![]() |
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PDB format | ![]() | 91.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 443.1 KB | Display | ![]() |
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Full document | ![]() | 460.8 KB | Display | |
Data in XML | ![]() | 26.1 KB | Display | |
Data in CIF | ![]() | 37.9 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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Components
#1: Protein | Mass: 28731.100 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-NI / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 59 % Description: THESE ARE THE PARAMETERS FOR THE DATA SET USED FOR REFINEMENT. THE DATA USED FOR STRUCTURE SOLUTION ARE ALSO SUPPLIED. | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / pH: 60 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: PRINCETON 2K / Detector: CCD / Date: Apr 1, 1998 | |||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.75→24.15 Å / Num. obs: 205040 / % possible obs: 80.2 % / Redundancy: 3 % / Biso Wilson estimate: 31.43 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 31.8 | |||||||||
Reflection shell | Resolution: 1.75→1.78 Å / Redundancy: 1 % / Rmerge(I) obs: 0.368 / Mean I/σ(I) obs: 2.9 / % possible all: 66.4 | |||||||||
Reflection | *PLUS Num. obs: 53298 / Num. measured all: 205040 | |||||||||
Reflection shell | *PLUS % possible obs: 66.4 % |
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Processing
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Refinement | Method to determine structure: ![]() Details: SULPHUR ATOMS OF ALL METHIONINE RESIDUES WERE REPLACED BY SELENIUM ATOMS.
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Displacement parameters | Biso mean: 41.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→24.15 Å
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Refine LS restraints |
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