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- PDB-2cax: STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX RE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cax | ||||||
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Title | STRUCTURAL BASIS FOR COOPERATIVE BINDING OF RIBBON-HELIX-HELIX REPRESSOR OMEGA TO MUTATED DIRECT DNA HEPTAD REPEATS | ||||||
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![]() | TRANSCRIPTIONAL REPRESSOR / INC18 FAMILY OF PLASMIDS / RHH / METJ/ARC SUPERFAMILY / COOPERATIVE DNA BINDING / DNA HEPTAD 5'- A/T ATCAC A/T -3' / PLASMID MAINTENANCE / DNA- BINDING / REGULATORY PROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() | ||||||
![]() | Weihofen, W.A. / Cicek, A. / Pratto, F. / Alonso, J.C. / Saenger, W. | ||||||
![]() | ![]() Title: Structures of Omega Repressors Bound to Direct and Inverted DNA Repeats Explain Modulation of Transcription. Authors: Weihofen, W.A. / Cicek, A. / Pratto, F. / Alonso, J.C. / Saenger, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 92 KB | Display | ![]() |
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PDB format | ![]() | 68.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.1 KB | Display | ![]() |
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Full document | ![]() | 446.3 KB | Display | |
Data in XML | ![]() | 7.6 KB | Display | |
Data in CIF | ![]() | 11.2 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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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | THE DESIGNATION OF THE QUATERNARY STRUCTURE AS OCTAMERICREFLECTS THE STANDARD PQS CONVENTION FOR DESCRIBINGHETEROGENEOUS ASSEMBLIES. HOWEVER, THE CRYSTALLOGRAPHICASYMMETRIC UNIT ACTUALLY CONTAINS ONE DNA FRAGMENT(COMPRISED OF CHAINS E AND F) WHICH IS BOUND TO TWOPROTEIN DIMERS (CHAINS A, B, C AND D). A FURTHER FREEDNA FRAGMENT (CHAINS G AND H) IS PRESENT IN THE A.U.THE INTERFACE BETWEEN THE TWO PROTEIN DIMERS AND DNAIS 1600 ANGSTROMS**2 AND THE INTERFACE BETWEEN THETWO PROTEIN DIMERS IS 280 ANGSTROMS**2. THE INTERFACEBETWEEN THE PROTEIN DIMER (CHAIN A, B OR CHAINS C, D)IS 1809 ANGSTROMS**2. |
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Components
-DNA chain , 4 types, 4 molecules GHUY
#2: DNA chain | Mass: 5197.428 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#3: DNA chain | Mass: 5254.402 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: IN INC18 FAMILY PLASMIDS, DIRECT REPEATS OCCUR IN PROMOTER REGIONS PRECEDING GENES CONTROLLED BY OMEGA TRANSCRIPTIONAL REPRESSOR Source: (synth.) synthetic construct |
#4: DNA chain | Mass: 5502.609 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#5: DNA chain | Mass: 5528.573 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: IN INC18 FAMILY PLASMIDS, DIRECT REPEATS OCCUR IN PROMOTER REGIONS PRECEDING GENES CONTROLLED BY OMEGA TRANSCRIPTIONAL REPRESSOR Source: (synth.) synthetic construct |
-Protein / Non-polymers , 2 types, 46 molecules ABCD![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#1: Protein | Mass: 6137.223 Da / Num. of mol.: 4 / Fragment: RIBBON-HELIX-HELIX DOMAIN, RESIDUES 20-71 Source method: isolated from a genetically manipulated source Details: 19 N-TERMINAL RESIDUES DELETED, NEW N- TERMINAL RESIDUE MET19 IS A CLONING ARTEFACT Source: (gene. exp.) ![]() Description: OMEGA TRANSCRIPTIONAL REPRSSSOR IS ENCODED BY PLASMID PSM19035 OF THE INC18 FAMILY OF PLASMIDS. Plasmid: PET28A-DELTA19OMEGA / Production host: ![]() ![]() #6: Water | ChemComp-HOH / | |
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-Details
Sequence details | 19 N-TERMINAL RESIDUES TRUNCATED, NEW MET19 IS A CLONING ARTIFACT |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.03 Å3/Da / Density % sol: 69.27 % / Description: STRUCTURE IS ISOMORPHOUS TO PDB ENTRY 2BNW |
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Crystal grow | pH: 7.5 Details: 150 MM NA/KPO4, PH 7.0, 2.4 M NA2MALONATE, PH 7.5, 2% AMINOCAPROIC ACID |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 7, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→30 Å / Num. obs: 14144 / % possible obs: 88.6 % / Observed criterion σ(I): 2.5 / Redundancy: 2.6 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 2.9→2.97 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 2.5 / % possible all: 68.8 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2.9→30 Å / Cor.coef. Fo:Fc: 0.921 / Cor.coef. Fo:Fc free: 0.876 / SU B: 20.726 / SU ML: 0.241 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 1.43 / ESU R Free: 0.372 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.67 Å2
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Refinement step | Cycle: LAST / Resolution: 2.9→30 Å
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Refine LS restraints |
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