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Open data
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Basic information
| Entry | Database: PDB / ID: 3zrw | ||||||
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| Title | The structure of the dimeric Hamp-Dhp fusion A291V mutant | ||||||
Components | (AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ) x 2 | ||||||
Keywords | SIGNALING PROTEIN / OSMOREGULATION / OMPR / OMPC | ||||||
| Function / homology | Function and homology informationresponse to osmotic stress / phosphorelay sensor kinase activity / histidine kinase / phosphorelay signal transduction system / phosphoprotein phosphatase activity / kinase activity / outer membrane-bounded periplasmic space / protein autophosphorylation / signal transduction / protein homodimerization activity ...response to osmotic stress / phosphorelay sensor kinase activity / histidine kinase / phosphorelay signal transduction system / phosphoprotein phosphatase activity / kinase activity / outer membrane-bounded periplasmic space / protein autophosphorylation / signal transduction / protein homodimerization activity / ATP binding / metal ion binding / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
| Biological species | ![]() ARCHAEOGLOBUS FULGIDUS (archaea)![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Zeth, K. / Hulko, M. / Ferris, H.U. / Martin, J. / Lupas, A.N. | ||||||
Citation | Journal: Structure / Year: 2012Title: Mechanism of Regulation of Receptor Histidine Kinases. Authors: Ferris, H.U. / Dunin-Horkwicz, S. / Hornig, N. / Hulko, M. / Martin, J. / Schultz, J.E. / Zeth, K. / Lupas, A.N. / Coles, M. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3zrw.cif.gz | 192.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3zrw.ent.gz | 156.7 KB | Display | PDB format |
| PDBx/mmJSON format | 3zrw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3zrw_validation.pdf.gz | 454.6 KB | Display | wwPDB validaton report |
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| Full document | 3zrw_full_validation.pdf.gz | 468.8 KB | Display | |
| Data in XML | 3zrw_validation.xml.gz | 21.5 KB | Display | |
| Data in CIF | 3zrw_validation.cif.gz | 30.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zr/3zrw ftp://data.pdbj.org/pub/pdb/validation_reports/zr/3zrw | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2lfrC ![]() 2lfsC ![]() 3zrvC ![]() 3zrxC ![]() 2asmS C: citing same article ( S: Starting model for refinement |
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| Similar 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 domain:
NCS domain segments:
NCS ensembles :
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Components
| #1: Protein | Mass: 13136.903 Da / Num. of mol.: 3 / Fragment: RESIDUES 278-326,228-288 / Mutation: YES Source method: isolated from a genetically manipulated source Details: CHIMERIC PROTEIN, RESIDUES OF THE PROTEIN AF1503 FROM A. FULGIDUS AND THE OSMOLARITY SENSING PROTEIN FROM E. COLI -ONE MUTATION IN POSITION A291V IS INTRODUCED Source: (gene. exp.) ![]() ARCHAEOGLOBUS FULGIDUS (archaea), (gene. exp.) ![]() Strain: DSM 4304, K-12 / Description: PCR FROM E. COLI WT DNA AND A. FULGIDUS WT DNA / Production host: ![]() References: UniProt: O28769, UniProt: P0AEJ4, histidine kinase #2: Protein | | Mass: 13151.875 Da / Num. of mol.: 1 / Fragment: RESIDUES 278-326,228-288 / Mutation: YES Source method: isolated from a genetically manipulated source Details: CHIMERIC PROTEIN, RESIDUES OF THE PROTEIN AF1503 FROM A. FULGIDUS AND THE OSMOLARITY SENSING PROTEIN FROM E. COLI -ONE MUTATION IN POSITION A291V IS INTRODUCED Source: (gene. exp.) ![]() ARCHAEOGLOBUS FULGIDUS (archaea), (gene. exp.) ![]() Strain: DSM 4304, K-12 / Description: PCR FROM E. COLI WT DNA AND A. FULGIDUS WT DNA / Production host: ![]() References: UniProt: O28769, UniProt: P0AEJ4, histidine kinase #3: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, ALA 291 TO VAL ENGINEERED RESIDUE IN CHAIN B, ALA 291 TO VAL ...ENGINEERED | Sequence details | O28769 AND P0AEJ4 DOMAINS ARE FUSED BY CLONING. | |
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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: 2.47 Å3/Da / Density % sol: 50.2 % / Description: NONE |
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| Crystal grow | pH: 7 / Details: 0.4 M MAGNESIUM FORMATE, 0.1 M BIS/TRIS, PH 7. |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.979 |
| Detector | Type: MARRESEARCH MX-225 / Detector: CCD |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
| Reflection | Resolution: 2.25→20 Å / Num. obs: 23404 / % possible obs: 99.7 % / Observed criterion σ(I): 2.6 / Redundancy: 3.7 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 12 |
| Reflection shell | Resolution: 2.25→2.3 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.53 / Mean I/σ(I) obs: 2.6 / % possible all: 99.7 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 2ASM Resolution: 2.25→25 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.899 / SU B: 16.245 / SU ML: 0.18 / Cross valid method: THROUGHOUT / ESU R: 0.322 / ESU R Free: 0.246 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 42.216 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.25→25 Å
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| Refine LS restraints |
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ARCHAEOGLOBUS FULGIDUS (archaea)
X-RAY DIFFRACTION
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