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- PDB-1fmf: REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING S... -
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Basic information
Entry | Database: PDB / ID: 1fmf | ||||||
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Title | REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM | ||||||
![]() | METHYLASPARTATE MUTASE S CHAIN | ||||||
![]() | ISOMERASE / nucleotide binding fold / Rossmann fold | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, simulated annealing refinement, energy minimization | ||||||
![]() | Hoffmann, B. / Konrat, R. / Tollinger, M. / Huhta, M. / Marsh, E.N.G. / Kraeutler, B. | ||||||
![]() | ![]() Title: A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum. Authors: Hoffmann, B. / Tollinger, M. / Konrat, R. / Huhta, M. / Marsh, E.N. / Krautler, B. #1: ![]() 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.G. / Kraeutler, B. #2: ![]() 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.G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 997.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 361.3 KB | Display | ![]() |
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Full document | ![]() | 535.7 KB | Display | |
Data in XML | ![]() | 58.2 KB | Display | |
Data in CIF | ![]() | 103.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 14763.856 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
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Sample preparation
Details | Contents: 1.5mM MutS U-98% 15N,13C; 11mM phosphate buffer; / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 11mM KXH3-XPO4 / pH: 6 / Pressure: 1 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
NMR software |
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Refinement | Method: distance geometry, simulated annealing, simulated annealing refinement, energy minimization Software ordinal: 1 Details: The MutS structure models 1-15 are based on a total of 1792 restraints, 1553 are NOE-derived distance constraints, 184 dihedral angle restraints, 55 distance restraints from hydrogen bonds. ...Details: The MutS structure models 1-15 are based on a total of 1792 restraints, 1553 are NOE-derived distance constraints, 184 dihedral angle restraints, 55 distance restraints from hydrogen bonds. Backbone dihedral angles Phi and Psi were obtained by employing TALOS software [G. Cornilescu et al., J. Biomol. NMR 1999, 13, 289-302]. Phi and Psi torsion angle restraints for the MutS residues 23-30, which form a "nascent" helix [M. Tollinger et al., Structure 1998, 6, 1021-1033], were not used in structure calculations for MutS models 16-30. | ||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 30 |