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Yorodumi- PDB-2y0q: The mechanisms of HAMP-mediated signaling in transmembrane recept... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2y0q | ||||||
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Title | The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291C mutant | ||||||
Components | UNCHARACTERIZED PROTEIN | ||||||
Keywords | MEMBRANE PROTEIN / TRANSMEMBRANE SIGNALLING | ||||||
Function / homology | Function and homology information signal transduction / membrane / identical protein binding / metal ion binding Similarity search - Function | ||||||
Biological species | ARCHAEOGLOBUS FULGIDUS (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Zeth, K. / Ferris, H.U. / Hulko, M. / Lupas, A.N. | ||||||
Citation | Journal: Structure / Year: 2011 Title: The Mechanisms of Hamp-Mediated Signaling in Transmembrane Receptors. Authors: Ferris, H.U. / Dunin-Horkawicz, S. / Mondejar, L.G. / Hulko, M. / Hantke, K. / Martin, J. / Schultz, J.E. / Zeth, K. / Lupas, A.N. / Coles, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2y0q.cif.gz | 92 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2y0q.ent.gz | 73.5 KB | Display | PDB format |
PDBx/mmJSON format | 2y0q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y0/2y0q ftp://data.pdbj.org/pub/pdb/validation_reports/y0/2y0q | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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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: 6039.916 Da / Num. of mol.: 4 / Fragment: HAMP DOMAIN, RESIDUES 278-331 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARCHAEOGLOBUS FULGIDUS (archaea) / Description: GENOMIC DNA / Plasmid: GST-FUSION / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O28769 #2: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, ALA 291 TO CYS ENGINEERED RESIDUE IN CHAIN B, ALA 291 TO CYS ...ENGINEERED | |
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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: 1.84 Å3/Da / Density % sol: 32.74 % / Description: NONE |
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Crystal grow | pH: 5.6 / Details: pH 5.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 |
Detector | Type: MARMOSAIC 225 mm CCD / 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→2.05 Å / Num. obs: 10902 / % possible obs: 97.2 % / Observed criterion σ(I): 2.1 / Redundancy: 4.7 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 2.1 / % possible all: 97 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→25 Å / Cor.coef. Fo:Fc: 0.917 / Cor.coef. Fo:Fc free: 0.898 / SU B: 12.84 / SU ML: 0.167 / Cross valid method: THROUGHOUT / ESU R: 0.285 / ESU R Free: 0.217 / 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: 22.675 Å2
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Refinement step | Cycle: LAST / Resolution: 2→25 Å
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Refine LS restraints |
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