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- PDB-1urg: X-ray structures from the maltose-maltodextrin binding protein of... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1urg | |||||||||
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Title | X-ray structures from the maltose-maltodextrin binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius | |||||||||
![]() | MALTOSE-BINDING PROTEIN | |||||||||
![]() | MALTOSE-BINDING PROTEIN / MALTODEXTRIN-BINDING PROTEIN / ACIDOPHILE / THERMOACIDOPHILE / HYPERTHERMOPHILE / THERMOPHILE | |||||||||
Function / homology | ![]() carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Schafer, K. / Magnusson, U. / Scheffel, F. / Schiefner, A. / Sandgren, M.O.J. / Diederichs, K. / Welte, W. / Hulsmann, A. / Schneider, E. / Mowbray, S.L. | |||||||||
![]() | ![]() Title: X-Ray Structures of the Maltose-Maltodextrin-Binding Protein of the Thermoacidophilic Bacterium Alicyclobacillus Acidocaldarius Provide Insight Into Acid Stability of Proteins. Authors: Schafer, K. / Magnusson, U. / Scheffel, F. / Schiefner, A. / Sandgren, M.O.J. / Diederichs, K. / Welte, W. / Hulsmann, A. / Schneider, E. / Mowbray, S.L. | |||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 89.2 KB | Display | ![]() |
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PDB format | ![]() | 65.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 798 KB | Display | ![]() |
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Full document | ![]() | 801.8 KB | Display | |
Data in XML | ![]() | 16.8 KB | Display | |
Data in CIF | ![]() | 23.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1urdC ![]() 1ursC ![]() 1anfS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 43312.719 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Plasmid: PFR1 / Production host: ![]() ![]() |
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.85 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 9.5 / Details: pH 9.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.2 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54179 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 35989 / % possible obs: 99.5 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.155 / Net I/σ(I): 7.5 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.524 / Mean I/σ(I) obs: 2.1 / % possible all: 91.4 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 50 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.155 |
Reflection shell | *PLUS % possible obs: 91.4 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.524 / Mean I/σ(I) obs: 2.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ANF Resolution: 1.8→50 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→50 Å
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Refine LS restraints |
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Xplor file |
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Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 50 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |