+Open data
-Basic information
Entry | Database: PDB / ID: 6bs6 | |||||||||
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Title | SusG with mixed linkage amylosaccharide | |||||||||
Components | Alpha-amylase SusG | |||||||||
Keywords | HYDROLASE / glycoside hydrolase family 13 / GH13 / amylase / SusG | |||||||||
Function / homology | Function and homology information starch catabolic process / oligosaccharide catabolic process / starch binding / alpha-amylase / outer membrane / alpha-amylase activity / cell outer membrane / calcium ion binding / magnesium ion binding Similarity search - Function | |||||||||
Biological species | Bacteroides thetaiotaomicron (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.17 Å | |||||||||
Authors | Koropatkin, N.M. / Cockburn, D.W. | |||||||||
Citation | Journal: Protein Sci. / Year: 2018 Title: Structural basis for the flexible recognition of alpha-glucan substrates by Bacteroides thetaiotaomicron SusG. Authors: Arnal, G. / Cockburn, D.W. / Brumer, H. / Koropatkin, N.M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6bs6.cif.gz | 571.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6bs6.ent.gz | 469.9 KB | Display | PDB format |
PDBx/mmJSON format | 6bs6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bs/6bs6 ftp://data.pdbj.org/pub/pdb/validation_reports/bs/6bs6 | HTTPS FTP |
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-Related structure data
Related structure data | 3k8lS S: Starting model for refinement |
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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
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 75367.938 Da / Num. of mol.: 2 / Mutation: D498N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) (bacteria) Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 / Gene: susG, BT_3698 / Plasmid: pET-28 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta(DE3)pLysS / References: UniProt: Q8A1G3, alpha-amylase |
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-Sugars , 5 types, 6 molecules
#2: Polysaccharide | #3: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-4)-alpha-D- ...alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-[alpha-D-glucopyranose-(1-6)]alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | Source method: isolated from a genetically manipulated source #4: Polysaccharide | alpha-D-glucopyranose-(1-4)-[alpha-D-glucopyranose-(1-6)]alpha-D-glucopyranose-(1-4)-alpha-D- ...alpha-D-glucopyranose-(1-4)-[alpha-D-glucopyranose-(1-6)]alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | Source method: isolated from a genetically manipulated source #5: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltotriose | #6: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-4)-alpha-D- ...alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-[alpha-D-glucopyranose-(1-6)]alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | Source method: isolated from a genetically manipulated source |
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-Non-polymers , 4 types, 698 molecules
#7: Chemical | ChemComp-CA / #8: Chemical | ChemComp-GOL / | #9: Chemical | ChemComp-ACT / | #10: 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: 3.59 Å3/Da / Density % sol: 65.74 % / Description: thin needles |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Protein crystals of the SusG-D498N mutant were obtained via hanging drop vapor diffusion by mixing the protein (A280 = 15) with 10 mM alpha-D-glucosyl-maltotriosyl-maltotriose (O-GMH, ...Details: Protein crystals of the SusG-D498N mutant were obtained via hanging drop vapor diffusion by mixing the protein (A280 = 15) with 10 mM alpha-D-glucosyl-maltotriosyl-maltotriose (O-GMH, Megazyme) against a crystallization liquor containing 18-20% PEG 4K, 100 mM HEPES pH 7.5, and 70 mM calcium acetate. Temp details: room temp - 20C |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: liquid nitrogen vapor |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.979 Å |
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Dec 1, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→45.4 Å / Num. obs: 701034 / % possible obs: 99.68 % / Redundancy: 6.4 % / Biso Wilson estimate: 36.49 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.0969 / Rrim(I) all: 0.1055 / Net I/σ(I): 8.89 |
Reflection shell | Resolution: 2.17→2.248 Å / Redundancy: 6.4 % / Rmerge(I) obs: 1.065 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 69620 / CC1/2: 0.795 / Rrim(I) all: 0.1055 / % possible all: 99.31 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3K8L Resolution: 2.17→45.4 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 28.86
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 109.7 Å2 / Biso mean: 44.1319 Å2 / Biso min: 16.09 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.17→45.4 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 27
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Refinement TLS params. | Method: refined / Origin x: 3.4953 Å / Origin y: 81.3875 Å / Origin z: -13.7897 Å
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Refinement TLS group |
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