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- PDB-6o7p: Nitrogenase MoFeP mutant F99Y from Azotobacter vinelandii in the ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6o7p | |||||||||
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Title | Nitrogenase MoFeP mutant F99Y from Azotobacter vinelandii in the dithionite reduced state | |||||||||
![]() | (Nitrogenase molybdenum-iron protein ...) x 2 | |||||||||
![]() | OXIDOREDUCTASE / Nitrogenase / F99Y / MoFeP | |||||||||
Function / homology | ![]() molybdenum-iron nitrogenase complex / nitrogenase / : / nitrogenase activity / nitrogen fixation / iron-sulfur cluster binding / ATP binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Rutledge, H.L. / Williamson, L.M. / Tezcan, F.A. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Redox-Dependent Metastability of the Nitrogenase P-Cluster. Authors: Rutledge, H.L. / Rittle, J. / Williamson, L.M. / Xu, W.A. / Gagnon, D.M. / Tezcan, F.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 798.6 KB | Display | ![]() |
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PDB format | ![]() | 652.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 93.1 KB | Display | |
Data in CIF | ![]() | 144 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6o7lC ![]() 6o7mC ![]() 6o7nC ![]() 6o7oC ![]() 6o7qC ![]() 6o7rC ![]() 6o7sC ![]() 2minS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Nitrogenase molybdenum-iron protein ... , 2 types, 4 molecules ACBD
#1: Protein | Mass: 55363.043 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 59551.879 Da / Num. of mol.: 2 / Mutation: F99Y / Source method: isolated from a natural source Details: This protein was expressed from the natural source by modification of the chromosomal DNA rather than through and expression system with a plasmid Source: (natural) ![]() |
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-Non-polymers , 5 types, 2537 molecules ![](data/chem/img/HCA.gif)
![](data/chem/img/ICS.gif)
![](data/chem/img/CLF.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ICS.gif)
![](data/chem/img/CLF.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.48 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.3 Details: 22% PEG 8000, 100 mM Tris pH 8.3, 500 mM NaCl, 10 mM dithionite |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 29, 2018 / Details: Rh coated flat bent M0 |
Radiation | Monochromator: Si(111) and Si(220) double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→63.23 Å / Num. obs: 189177 / % possible obs: 87.5 % / Redundancy: 6.4 % / CC1/2: 0.987 / Rmerge(I) obs: 0.237 / Rpim(I) all: 0.154 / Rrim(I) all: 0.284 / Χ2: 0.95 / Net I/σ(I): 6.4 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 6.2 % / Rmerge(I) obs: 1.442 / Mean I/σ(I) obs: 1.5 / Num. unique obs: 10279 / CC1/2: 0.271 / Rpim(I) all: 0.937 / Rrim(I) all: 1.729 / Χ2: 0.97 / % possible all: 96.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2MIN Resolution: 1.7→46.652 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 20.53
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→46.652 Å
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Refine LS restraints |
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LS refinement shell |
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