+Open data
-Basic information
Entry | Database: PDB / ID: 1b9n | ||||||
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Title | REGULATOR FROM ESCHERICHIA COLI | ||||||
Components | PROTEIN (MODE) | ||||||
Keywords | TRANSCRIPTION / DNA-BINDING / GENE REGULATION / WINGED HELIX TURN HELIX / MOLYBDATE / OB FOLD | ||||||
Function / homology | Function and homology information ModE complex / molybdate ion transport / negative regulation of DNA-templated transcription initiation / molybdenum ion binding / cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.09 Å | ||||||
Authors | Hall, D.R. / Gourley, D.G. / Hunter, W.N. | ||||||
Citation | Journal: EMBO J. / Year: 1999 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b9n.cif.gz | 114.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b9n.ent.gz | 87.9 KB | Display | PDB format |
PDBx/mmJSON format | 1b9n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b9/1b9n ftp://data.pdbj.org/pub/pdb/validation_reports/b9/1b9n | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 28590.416 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P0A9G8 #2: Chemical | ChemComp-NI / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 59 % Description: A STARTING MODEL WAS DERIVED FROM MAD PHASED MAPS OF A SELENOMETHIONYL DERIVATIVE OF THIS PROTEIN. | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / pH: 6 / 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: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 1, 1998 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.09→28.63 Å / Num. obs: 268449 / % possible obs: 99 % / Redundancy: 4 % / Biso Wilson estimate: 31.98 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 2.09→2.15 Å / Redundancy: 4 % / Rmerge(I) obs: 0.421 / Mean I/σ(I) obs: 2 / % possible all: 99.6 |
Reflection | *PLUS Num. obs: 37763 / Num. measured all: 268449 |
Reflection shell | *PLUS % possible obs: 99.6 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.09→28.63 Å / SU B: 5.01249 / SU ML: 0.13767 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.20739 / ESU R Free: 0.20519
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Displacement parameters | Biso mean: 39.12 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.09→28.63 Å
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Refine LS restraints |
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