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Yorodumi- PDB-3pxm: Reduced sweetness of a monellin (MNEI) mutant results from increa... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3pxm | ||||||
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Title | Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix | ||||||
Components | Monellin chain B/Monellin chain A chimeric protein | ||||||
Keywords | PLANT PROTEIN / a poly-(L-proline) II (PPII) helix / sweet protein | ||||||
Function / homology | Function and homology information Monellin, A chain / Monellin, A chain superfamily / Monellin, B chain / Monellin / Monellin / Nuclear Transport Factor 2; Chain: A, - #10 / Cystatin superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | Dioscoreophyllum cumminsii (serendipity berry) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Hobbs, J.R. / Templeton, C.M. / Pour, S.O. / Blanch, E.W. / Munger, S.M. / Conn, G.L. | ||||||
Citation | Journal: Chem Senses / Year: 2011 Title: Reduced Sweetness of a Monellin (MNEI) Mutant Results from Increased Protein Flexibility and Disruption of a Distant Poly-(L-Proline) II Helix. Authors: Templeton, C.M. / Ostovar Pour, S. / Hobbs, J.R. / Blanch, E.W. / Munger, S.D. / Conn, G.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3pxm.cif.gz | 57.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3pxm.ent.gz | 41.3 KB | Display | PDB format |
PDBx/mmJSON format | 3pxm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/px/3pxm ftp://data.pdbj.org/pub/pdb/validation_reports/px/3pxm | HTTPS FTP |
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-Related structure data
Related structure data | 3pyjC 3q2pC 1iv9S 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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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 11390.995 Da / Num. of mol.: 2 / Mutation: V37A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dioscoreophyllum cumminsii (serendipity berry) Plasmid: pET22b / Production host: Escherichia coli (E. coli) / References: UniProt: P02882, UniProt: P02881 #2: 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: 2.32 Å3/Da / Density % sol: 47.04 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 0.2 M Li2SO4, 0.1M HEPES and 25% w/v PEG4000, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.548 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 20, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.548 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→22.43 Å / Num. obs: 17472 / Redundancy: 3.5 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1IV9 Resolution: 1.8→24.63 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.925 / SU B: 2.73 / SU ML: 0.087 / Cross valid method: THROUGHOUT / ESU R Free: 0.137 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.586 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→24.63 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.847 Å / Total num. of bins used: 20
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