+Open data
-Basic information
Entry | Database: PDB / ID: 3zx6 | ||||||
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Title | Structure of Hamp(AF1503)-Tsr fusion - Hamp (A291V) mutant | ||||||
Components | HAMP, METHYL-ACCEPTING CHEMOTAXIS PROTEIN I | ||||||
Keywords | SIGNALING / HAMP DOMAIN / TSR RECEPTOR / FUSION | ||||||
Function / homology | Function and homology information regulation of protein histidine kinase activity / detection of chemical stimulus / methyl accepting chemotaxis protein complex / regulation of bacterial-type flagellum-dependent cell motility / regulation of chemotaxis / signal complex assembly / receptor clustering / cell motility / cellular response to amino acid stimulus / chemotaxis ...regulation of protein histidine kinase activity / detection of chemical stimulus / methyl accepting chemotaxis protein complex / regulation of bacterial-type flagellum-dependent cell motility / regulation of chemotaxis / signal complex assembly / receptor clustering / cell motility / cellular response to amino acid stimulus / chemotaxis / transmembrane signaling receptor activity / signal transduction / membrane / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ARCHAEOGLOBUS FULGIDUS (archaea) ESCHERICHIA COLI K-12 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å | ||||||
Authors | Zeth, K. / Ferris, H.U. / Lupas, A.L. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2014 Title: Axial Helix Rotation as a Mechanism for Signal Regulation Inferred from the Crystallographic Analysis of the E. Coli Serine Chemoreceptor. Authors: Ferris, H.U. / Zeth, K. / Hulko, M. / Dunin-Horkawicz, S. / Lupas, A.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3zx6.cif.gz | 235.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3zx6.ent.gz | 193.1 KB | Display | PDB format |
PDBx/mmJSON format | 3zx6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zx/3zx6 ftp://data.pdbj.org/pub/pdb/validation_reports/zx/3zx6 | HTTPS FTP |
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-Related structure data
Related structure data | 3zrxS S: Starting model for refinement |
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Similar 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: 36136.066 Da / Num. of mol.: 2 Fragment: HAMP RESIDUES 278-326, METHYL-ACCEPTING CHEMOTAXIS PROTEIN I RESIDUES 264-551 Mutation: YES Source method: isolated from a genetically manipulated source Details: CHIMERA, THREE RESIDUE LINKER INTERNALLY IN METHYL-ACCEPTING CHEMOTAXIS PROTEIN DOMAIN Source: (gene. exp.) ARCHAEOGLOBUS FULGIDUS (archaea), (gene. exp.) ESCHERICHIA COLI K-12 (bacteria) Strain: DSM 4304 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O28769, UniProt: P02942 #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | ENGINEERED | Sequence details | THREE RESIDUE QQQ LINKER INSERTED IN UNP P02942. | |
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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: 4.04 Å3/Da / Density % sol: 69.57 % / Description: NONE |
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Crystal grow | pH: 7 / Details: PH 7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 |
Detector | Type: MARRESEARCH MX-225 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.65→40 Å / Num. obs: 32412 / % possible obs: 96.1 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % / Biso Wilson estimate: 60 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 9.57 |
Reflection shell | Resolution: 2.65→2.75 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.6 / Mean I/σ(I) obs: 2 / % possible all: 96.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3ZRX Resolution: 2.65→29.48 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.922 / SU B: 27.79 / SU ML: 0.245 / Cross valid method: THROUGHOUT / ESU R: 0.387 / ESU R Free: 0.298 / 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: 62.377 Å2
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Refinement step | Cycle: LAST / Resolution: 2.65→29.48 Å
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