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Yorodumi- PDB-3m9c: Crystal structure of the membrane domain of respiratory complex I... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3m9c | ||||||
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Title | Crystal structure of the membrane domain of respiratory complex I from Escherichia coli | ||||||
Components |
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Keywords | OXIDOREDUCTASE / MEMBRANE PROTEIN / COMPLEX I / ELECTRON TRANSPORT / RESPIRATORY CHAIN | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 3.9 Å | ||||||
Authors | Efremov, R.G. / Baradaran, R. / Sazanov, L.A. | ||||||
Citation | Journal: Nature / Year: 2010 Title: The architecture of respiratory complex I Authors: Efremov, R.G. / Baradaran, R. / Sazanov, L.A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3m9c.cif.gz | 110.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3m9c.ent.gz | 81.6 KB | Display | PDB format |
PDBx/mmJSON format | 3m9c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3m9c_validation.pdf.gz | 352 KB | Display | wwPDB validaton report |
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Full document | 3m9c_full_validation.pdf.gz | 359.4 KB | Display | |
Data in XML | 3m9c_validation.xml.gz | 3.1 KB | Display | |
Data in CIF | 3m9c_validation.cif.gz | 14.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m9/3m9c ftp://data.pdbj.org/pub/pdb/validation_reports/m9/3m9c | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 40357.742 Da / Num. of mol.: 1 / Fragment: Membrane domain / Mutation: Subunit NuoH is missing / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: BL21 / References: NADH:ubiquinone reductase (H+-translocating) |
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#2: Protein | Mass: 33293.949 Da / Num. of mol.: 1 / Fragment: Membrane domain / Mutation: Subunit NuoH is missing / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: BL21 / References: NADH:ubiquinone reductase (H+-translocating) |
#3: Protein | Mass: 32187.574 Da / Num. of mol.: 1 / Fragment: Membrane domain / Mutation: Subunit NuoH is missing / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: BL21 / References: NADH:ubiquinone reductase (H+-translocating) |
#4: Protein | Mass: 23932.375 Da / Num. of mol.: 1 / Fragment: Membrane domain / Mutation: Subunit NuoH is missing / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: BL21 / References: NADH:ubiquinone reductase (H+-translocating) |
Compound details | THE LONG C-N BONDS ARE BECAUSE OF THE LOOPS NOT BEING MODELED. |
Sequence details | THE ACTUAL SEQUENCE FOR CHAIN L: MNMLALTIILPLIGFVLLAFSRGRWSENVSAIVGVGSVGLAALVTAFIGVDFFANGEQTYSQPLW ...THE ACTUAL SEQUENCE FOR CHAIN L: MNMLALTIIL |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 7.42 Å3/Da / Density % sol: 73 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, sitting drop / pH: 4.8 Details: 9% PEG4000, 0.1 M sodium acetate, 1.0 M sodium formate, pH 4.8, VAPOR DIFFUSION, SITTING DROP, temperature 283K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 21, 2009 / Details: Mirrors |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 3.9→30 Å / Num. all: 34983 / Num. obs: 34983 / % possible obs: 97.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 82.3 Å2 / Rmerge(I) obs: 0.205 / Net I/σ(I): 4 |
Reflection shell | Resolution: 3.9→4.11 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.846 / Mean I/σ(I) obs: 1.5 / Num. unique all: 5022 / % possible all: 97.4 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 3.9→30 Å / Num. reflection all: 34983 / Num. reflection obs: 34983 Details: This is not refined backbone model. The directionality of alpha-helices is not known. For the optimal calculation of electron density the data should be anisotropically scaled. | ||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.9→30 Å
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