+Open data
-Basic information
Entry | Database: PDB / ID: 1orm | ||||||
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Title | NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES | ||||||
Components | Outer membrane protein X | ||||||
Keywords | MEMBRANE PROTEIN / OMPX / TROSY / DHPC / DETERGENTS / LIPIDS / MICELLES | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS (DYANA) | ||||||
Authors | Fernandez, C. / Adeishvili, K. / Wuthrich, K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2001 Title: TRANSVERSE RELAXATION-OPTIMIZED NMR SPECTROSCOPY WITH THE OUTER MEMBRANE PROTEIN OMPX IN DIHEXANOYL PHOSPHATIDYLCHOLINE MICELLES Authors: FERNANDEZ, C. / ADEISHVILI, K. / WUTHRICH, K. #1: Journal: FEBS Lett. / Year: 2001 Title: SOLUTION NMR STUDIES OF THE INTERGRAL MEMBRANE PROTEINS OMPX AND OMPA FROM ESCHERICHIA COLI Authors: FERNANDEZ, C. / HILTY, C. / BONJOUR, S. / ADEISHVILI, K. / PERVUSHIN, K. / WUTHRICH, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1orm.cif.gz | 881.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1orm.ent.gz | 734 KB | Display | PDB format |
PDBx/mmJSON format | 1orm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1orm_validation.pdf.gz | 344.3 KB | Display | wwPDB validaton report |
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Full document | 1orm_full_validation.pdf.gz | 532.5 KB | Display | |
Data in XML | 1orm_validation.xml.gz | 61 KB | Display | |
Data in CIF | 1orm_validation.cif.gz | 75.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/or/1orm ftp://data.pdbj.org/pub/pdb/validation_reports/or/1orm | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16371.768 Da / Num. of mol.: 1 / Mutation: H100N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: OMPX / Plasmid: pET3B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P0A917 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2mM OMPX U-15N,13C,2H Solvent system: 300 mM DIHEXANOYL PHOSPHATIDYLCHOLINE (DHPC), 20mM PHOSPHATE BUFFER, 100mM NaCl, 95% H2O, 5% D2O |
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Sample conditions | Ionic strength: 20mM SODIUM PHOSPHATE, 100mM NaCl / pH: 6.5 / Pressure: ambient / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 750 MHz |
-Processing
NMR software |
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Refinement | Method: TORSION ANGLE DYNAMICS (DYANA) / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |