+Open data
-Basic information
Entry | Database: PDB / ID: 6dtu | |||||||||
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Title | Maltotetraose bound T. maritima MalE1 | |||||||||
Components | maltose-binding protein MalE1 | |||||||||
Keywords | SUGAR BINDING PROTEIN / periplasmic binding protein / maltose binding protein / maltotetraose | |||||||||
Function / homology | Function and homology information carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / proteasome core complex, alpha-subunit complex / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ubiquitin-dependent protein catabolic process Similarity search - Function | |||||||||
Biological species | Thermotoga maritima (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.5 Å | |||||||||
Authors | Cuneo, M.J. / Shukla, S. | |||||||||
Citation | Journal: Biochemistry / Year: 2018 Title: Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics. Authors: Shukla, S. / Bafna, K. / Gullett, C. / Myles, D.A.A. / Agarwal, P.K. / Cuneo, M.J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6dtu.cif.gz | 172.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6dtu.ent.gz | 134.9 KB | Display | PDB format |
PDBx/mmJSON format | 6dtu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6dtu_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 6dtu_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6dtu_validation.xml.gz | 32.3 KB | Display | |
Data in CIF | 6dtu_validation.cif.gz | 48.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dt/6dtu ftp://data.pdbj.org/pub/pdb/validation_reports/dt/6dtu | HTTPS FTP |
-Related structure data
Related structure data | 6dtqC 6dtrC 6dtsC 6dttC 2ghaS 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: 41334.316 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) (bacteria) Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / Gene: TM_1204 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9X0T1 #2: Polysaccharide | #3: 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: 2.1 Å3/Da / Density % sol: 41.52 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 25% poly-ethylene glycol (PEG) 4000, 18% isopropanol and 0.1M sodium citrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jun 12, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→50 Å / Num. obs: 90224 / % possible obs: 83.4 % / Redundancy: 2.1 % / Rmerge(I) obs: 0.077 / Net I/σ(I): 3 |
Reflection shell | Resolution: 1.5→1.55 Å / Rmerge(I) obs: 0.464 / Num. unique obs: 8982 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2GHA Resolution: 1.5→30.816 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 23.73
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→30.816 Å
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Refine LS restraints |
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LS refinement shell |
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