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- PDB-2n2u: Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n2u | ||||||
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Title | Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358 | ||||||
![]() | OR358 | ||||||
![]() | Unknown Function / Structural Genomics / Protein NMR / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) / Target OR358 / PSI-Biology / Protein Structure Initiative | ||||||
Biological species | Synthetic construct (others) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, null | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Liu, G. / Lin, Y. / Koga, N. / Koga, R. / Xiao, R. / Janjua, H. / Hamilton, K. / Pederson, K. / Acton, T.B. / Kornhaber, G. ...Liu, G. / Lin, Y. / Koga, N. / Koga, R. / Xiao, R. / Janjua, H. / Hamilton, K. / Pederson, K. / Acton, T.B. / Kornhaber, G. / Everett, J.K. / Baker, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358 Authors: Liu, G. / Lin, Y. / Koga, N. / Koga, R. / Xiao, R. / Janjua, H. / Hamilton, K. / Pederson, K. / Acton, T.B. / Kornhaber, G. / Everett, J.K. / Baker, D. / Montelione, G.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 558.4 KB | Display | ![]() |
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PDB format | ![]() | 478.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 530 KB | Display | ![]() |
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Full document | ![]() | 684.7 KB | Display | |
Data in XML | ![]() | 40.4 KB | Display | |
Data in CIF | ![]() | 50.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 8898.082 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Synthetic construct (others) / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics, null Software ordinal: 1 / Details: null, null | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |