+Open data
-Basic information
Entry | Database: PDB / ID: 4n4n | |||||||||
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Title | Nitrosomonas europea HAO | |||||||||
Components |
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Keywords | OXIDOREDUCTASE / C-type cytochrome | |||||||||
Function / homology | Function and homology information hydroxylamine dehydrogenase / hydroxylamine oxidase activity / hydroxylamine oxidase / anaerobic respiration, using ammonium as electron donor / hydroxylamine oxidoreductase activity / anammoxosome / protein homotrimerization / oxidoreductase activity / heme binding / identical protein binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Nitrosomonas europaea (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | |||||||||
Authors | Maalcke, W.J. / Dietl, A. / Marritt, S.J. / Butt, J.N. / Jetten, M.S.M. / Keltjens, J.T. / Barends, T.R.M.B. / Kartal, B. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2014 Title: Structural Basis of Biological NO Generation by Octaheme Oxidoreductases. Authors: Maalcke, W.J. / Dietl, A. / Marritt, S.J. / Butt, J.N. / Jetten, M.S. / Keltjens, J.T. / Barends, T.R. / Kartal, B. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4n4n.cif.gz | 388.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4n4n.ent.gz | 317.3 KB | Display | PDB format |
PDBx/mmJSON format | 4n4n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n4/4n4n ftp://data.pdbj.org/pub/pdb/validation_reports/n4/4n4n | HTTPS FTP |
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-Related structure data
Related structure data | 4n4jC 4n4kC 4n4lC 4n4mC 4n4oC 1fgjS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 2 types, 6 molecules ACEBDF
#1: Protein | Mass: 61720.473 Da / Num. of mol.: 3 / Fragment: UNP residues 25-528 / Source method: isolated from a natural source / Source: (natural) Nitrosomonas europaea (bacteria) / References: UniProt: Q50925, hydroxylamine dehydrogenase #2: Protein | Mass: 6182.173 Da / Num. of mol.: 3 / Fragment: UNP residues 28-84 / Source method: isolated from a natural source / Source: (natural) Nitrosomonas europaea (bacteria) / References: UniProt: Q82V11, hydroxylamine dehydrogenase |
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-Non-polymers , 4 types, 1120 molecules
#3: Chemical | ChemComp-HEC / #4: Chemical | ChemComp-K / | #5: Chemical | ChemComp-PO4 / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.82 % |
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Crystal grow | Temperature: 293 K / Method: microbatch under oil / pH: 7.5 Details: 42% v/v PEG400, 50 mM potassium nitrate, 100 mM MES/NaOH, pH 7.5, MICROBATCH UNDER OIL, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 0.9786 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Dec 1, 2012 Details: two horizontal deflecting and one vertical deflecting X-ray mirror |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9786 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50.4 Å / Num. all: 98124 / Num. obs: 98124 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.6 % / Rmerge(I) obs: 0.102 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 2.2→2.3 Å / Rmerge(I) obs: 0.588 / % possible all: 99.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FGJ Resolution: 2.2→50.4 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.931 / SU B: 3.594 / SU ML: 0.093 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.266 / ESU R Free: 0.192 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.017 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→50.4 Å
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Refine LS restraints |
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