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- PDB-2ml3: Solution Structure of AlgE6R3 subunit from the Azotobacter vinela... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ml3 | ||||||
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Title | Solution Structure of AlgE6R3 subunit from the Azotobacter vinelandii Mannuronan C5-epimerase | ||||||
![]() | Poly(beta-D-mannuronate) C5 epimerase 6 | ||||||
![]() | ISOMERASE / Alginate C-5 epimerase / mannuronan C-5 epimerase / R-module | ||||||
Function / homology | ![]() mannuronan 5-epimerase / alginic acid biosynthetic process / isomerase activity / calcium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Buchinger, E. / Wimmer, R. / Aachmann, F.L. | ||||||
![]() | ![]() Title: Structural and Functional Characterization of the R-modules in Alginate C-5 Epimerases AlgE4 and AlgE6 from Azotobacter vinelandii Authors: Buchinger, E. / Knudsen, D.H. / Behrens, M.A. / Pedersen, J.S. / Aarstad, O.A. / Tndervik, A. / Valla, S. / Skjak-Brk, G. / Wimmer, R. / Aachmann, F.L. #1: Journal: Biomol.Nmr Assign. / Year: 2011 Title: NMR assignments of 1H, 13C and 15N resonances of the C-terminal subunit from Azotobacter vinelandii mannuronan C5-epimerase 6 (AlgE6R3) Authors: Buchinger, E. / Skjak-Brk, G. / Valla, S. / Wimmer, R. / Aachmann, F.L. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 966.4 KB | Display | ![]() |
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PDB format | ![]() | 807.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 541 KB | Display | ![]() |
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Full document | ![]() | 753 KB | Display | |
Data in XML | ![]() | 95.3 KB | Display | |
Data in CIF | ![]() | 107.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ml1C ![]() 2ml2C C: citing same article ( |
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Similar structure data | |
Other databases |
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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: 18237.443 Da / Num. of mol.: 1 / Fragment: UNP residues 695-874 / Mutation: A180T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9ZFH0, Isomerases; Racemases and epimerases; Acting on carbohydrates and derivatives |
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#2: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Structure of the third R-module of AlgE6 from Azotobacter vinelandii | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | pH: 6.9 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2146 / NOE intraresidue total count: 889 / NOE long range total count: 553 / NOE medium range total count: 98 / NOE sequential total count: 606 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 51 / Protein psi angle constraints total count: 51 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |