+Open data
-Basic information
Entry | Database: PDB / ID: 6nc1 | ||||||
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Title | FtsY-NG high-resolution | ||||||
Components | Signal recognition particle receptor FtsY | ||||||
Keywords | TRANSPORT PROTEIN / FtsY / SRP / Signal recognition particle receptor / SR | ||||||
Function / homology | Function and homology information signal recognition particle binding / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane / stringent response / protein targeting / cytoplasmic side of plasma membrane / GTPase activity / GTP binding / ATP hydrolysis activity / protein homodimerization activity ...signal recognition particle binding / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane / stringent response / protein targeting / cytoplasmic side of plasma membrane / GTPase activity / GTP binding / ATP hydrolysis activity / protein homodimerization activity / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli K-12 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.598 Å | ||||||
Authors | Ataide, S.F. / Faoro, C. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2019 Title: Structural insights into the G-loop dynamics of E. coli FtsY NG domain. Authors: Faoro, C. / Ataide, S.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6nc1.cif.gz | 366.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6nc1.ent.gz | 303.2 KB | Display | PDB format |
PDBx/mmJSON format | 6nc1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nc/6nc1 ftp://data.pdbj.org/pub/pdb/validation_reports/nc/6nc1 | HTTPS FTP |
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-Related structure data
Related structure data | 6n5iC 6n5jC 6n6nC 6n9bC 6nc4C 6cqpS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 33101.043 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K12 / Gene: ftsY, b3464, JW3429 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: P10121 #2: Chemical | ChemComp-GDP / | #3: Chemical | ChemComp-K / #4: Chemical | ChemComp-MG / | #5: 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: 2.14 Å3/Da / Density % sol: 42.65 % |
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Crystal grow | Temperature: 297.15 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Bis-Tris pH 7, 30% PEG 2000 MME, 150 mM KBr |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: May 6, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.598→37.99 Å / Num. obs: 72072 / % possible obs: 97.8 % / Redundancy: 2 % / Net I/σ(I): 18.33 |
Reflection shell | Resolution: 1.598→1.6 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6CQP Resolution: 1.598→37.99 Å / SU ML: 0.16 / Cross valid method: NONE / σ(F): 1.38 / Phase error: 21.43 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.598→37.99 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -23.1067 Å / Origin y: 12.3252 Å / Origin z: 27.0328 Å
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Refinement TLS group | Selection details: all |