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Open data
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Basic information
Entry | Database: PDB / ID: 9rmm | ||||||||||||
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Title | Crystal structure of outer membrane SilC | ||||||||||||
![]() | (Probable outer membrane lipoprotein SilC) x 2 | ||||||||||||
![]() | MEMBRANE PROTEIN / SilC / sil / outer membrane / silver resistance / cus / CusC / silver | ||||||||||||
Function / homology | RND efflux system, outer membrane lipoprotein, NodT / : / Outer membrane efflux protein / Outer membrane efflux protein / efflux transmembrane transporter activity / cell outer membrane / Prokaryotic membrane lipoprotein lipid attachment site profile. / Probable outer membrane lipoprotein SilC![]() | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Lithgo, R.M. / Carr, S.B. / Quigley, A.M. / Scott, D.J. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural characterisation of the outer membrane protein SilC, involved in bacterial silver resistance. Authors: Lithgo, R.M. / Carr, S.B. / Quigley, A.M. / Scott, D.J. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 615.8 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.8 KB | Display | ![]() |
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Full document | ![]() | 450.9 KB | Display | |
Data in XML | ![]() | 48.2 KB | Display | |
Data in CIF | ![]() | 74.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 51295.531 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: silC / Production host: ![]() ![]() #2: Protein | | Mass: 51433.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: silC / Production host: ![]() ![]() Has protein modification | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.56 Å3/Da / Density % sol: 65.4 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 0.1M Sodium Citrate pH 5 0.1M Magnesium Chloride hexahydrate 11% PEG 4000 20% Glycerol (Cryo) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jan 19, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.999 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→44.29 Å / Num. obs: 70140 / % possible obs: 99.35 % / Redundancy: 3.4 % / Biso Wilson estimate: 46.16 Å2 / CC1/2: 0.94 / Net I/σ(I): 3.5 |
Reflection shell | Resolution: 3.203→3.317 Å / Num. unique obs: 4668 / CC1/2: 0.418 |
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Processing
Software | Name: PHENIX / Version: 1.20.1_4487 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.72 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→44.29 Å
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Refine LS restraints |
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LS refinement shell |
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