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Yorodumi- PDB-1be1: GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE ST... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1be1 | ||||||
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Title | GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
Components | GLUTAMATE MUTASE | ||||||
Keywords | ISOMERASE / GLUTAMATE MUTASE / B12-BINDING SUBUNIT | ||||||
Function / homology | Function and homology information methylaspartate mutase / anaerobic glutamate catabolic process / methylaspartate mutase activity / glutamate catabolic process via L-citramalate / cobalamin binding / metal ion binding Similarity search - Function | ||||||
Biological species | Clostridium tetanomorphum (bacteria) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, ENERGY MINIMIZATION | ||||||
Authors | Tollinger, M. / Konrat, R. / Hilbert, B.H. / Marsh, E.N.G. / Kraeutler, B. | ||||||
Citation | Journal: Structure / Year: 1998 Title: How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum Authors: Tollinger, M. / Konrat, R. / Hilbert, B.H. / Marsh, E.N. / Krautler, B. #1: Journal: J.Biol.Chem. / Year: 1994 Title: Adenosylcobalamin-Dependent Glutamate Mutase from Clostridium Tetanomorphum. Overexpression in Escherichia Coli, Purification, and Characterization of the Recombinant Enzyme Authors: Holloway, D.E. / Marsh, E.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1be1.cif.gz | 51.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1be1.ent.gz | 37 KB | Display | PDB format |
PDBx/mmJSON format | 1be1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1be1_validation.pdf.gz | 246 KB | Display | wwPDB validaton report |
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Full document | 1be1_full_validation.pdf.gz | 245.7 KB | Display | |
Data in XML | 1be1_validation.xml.gz | 4.1 KB | Display | |
Data in CIF | 1be1_validation.cif.gz | 5.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/be/1be1 ftp://data.pdbj.org/pub/pdb/validation_reports/be/1be1 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14763.856 Da / Num. of mol.: 1 / Fragment: B12-BINDING SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium tetanomorphum (bacteria) / Strain: H1 / Gene: MUTS / Plasmid: PMUTSX / Gene (production host): MUTS / Production host: Escherichia coli (E. coli) / Strain (production host): BL12 (DE3) / References: UniProt: Q05488, methylaspartate mutase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 90% H2O,10% D2O |
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Sample conditions | Ionic strength: 11mM KXH3-XPO4 / pH: 6 / Pressure: ATMOSPHERIC atm / Temperature: 299 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING, ENERGY MINIMIZATION Software ordinal: 1 | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: MINIMIZED AVERAGE / Conformers calculated total number: 15 / Conformers submitted total number: 1 |