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Open data
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Basic information
Entry | Database: PDB / ID: 1ewf | ||||||
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Title | THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI | ||||||
![]() | BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN | ||||||
![]() | ANTIBIOTIC / BACTERICIDAL / PERMEABILITY-INCREASING / LIPID-BINDING / LIPOPOLYSACCHARIDE-BINDING | ||||||
Function / homology | ![]() negative regulation of macrophage activation / Toll Like Receptor 4 (TLR4) Cascade / negative regulation of interleukin-8 production / Antimicrobial peptides / negative regulation of interleukin-6 production / negative regulation of tumor necrosis factor production / lipopolysaccharide-mediated signaling pathway / lipopolysaccharide binding / specific granule lumen / azurophil granule lumen ...negative regulation of macrophage activation / Toll Like Receptor 4 (TLR4) Cascade / negative regulation of interleukin-8 production / Antimicrobial peptides / negative regulation of interleukin-6 production / negative regulation of tumor necrosis factor production / lipopolysaccharide-mediated signaling pathway / lipopolysaccharide binding / specific granule lumen / azurophil granule lumen / defense response to Gram-negative bacterium / innate immune response / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kleiger, G. / Beamer, L.J. / Grothe, R. / Mallick, P. / Eisenberg, D. | ||||||
![]() | ![]() Title: The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold. Authors: Kleiger, G. / Beamer, L.J. / Grothe, R. / Mallick, P. / Eisenberg, D. #1: ![]() Title: Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution Authors: Beamer, L.J. / Carroll, S.F. / Eisenberg, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 110.1 KB | Display | ![]() |
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PDB format | ![]() | 89.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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
#1: Protein | Mass: 50703.625 Da / Num. of mol.: 1 / Mutation: S351A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: MAMMALIAN CHO CELLS USED FOR RECOMBINANT EXPRESSION OF THE PROTEIN Cell (production host): OVARY CELLS / Production host: ![]() ![]() | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | A NATURALLY OCCURRING POLYMORPHISM EXISTS AT RESIDUE 185 FOR HUMAN BPI. THE CLONE USED FOR ...A NATURALLY OCCURRING POLYMORPHI | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.78 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 12 % PEG 6000, 0.2 M Mg Acetate, 0.1 M Na Cacodylate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 16K | |||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 6, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.975 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→100 Å / Num. all: 47198 / Num. obs: 47198 / % possible obs: 94.2 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 2.3 % / Biso Wilson estimate: 24 Å2 / Rmerge(I) obs: 0.048 / Net I/σ(I): 16.7 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 1.3 % / Rmerge(I) obs: 0.201 / Num. unique all: 3300 / % possible all: 67 |
Reflection shell | *PLUS % possible obs: 67 % |
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Processing
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Refinement | Resolution: 1.7→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→50 Å
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Refine LS restraints |
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Software | *PLUS Name: 'CNS' / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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