+Open data
-Basic information
Entry | Database: PDB / ID: 1qpx | ||||||
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Title | CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS | ||||||
Components | PAPD CHAPERONE | ||||||
Keywords | CHAPERONE / BETA BARREL / IMMUNOGLOBULIN FOLD | ||||||
Function / homology | Function and homology information chaperone-mediated protein folding / cell wall organization / outer membrane-bounded periplasmic space Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Hung, D.L. / Pinkner, J.S. / Knight, S.D. / Hultgren, S.J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 Title: Structural basis of chaperone self-capping in P pilus biogenesis. Authors: Hung, D.L. / Pinkner, J.S. / Knight, S.D. / Hultgren, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qpx.cif.gz | 86.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qpx.ent.gz | 69.9 KB | Display | PDB format |
PDBx/mmJSON format | 1qpx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qpx_validation.pdf.gz | 368.7 KB | Display | wwPDB validaton report |
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Full document | 1qpx_full_validation.pdf.gz | 376.9 KB | Display | |
Data in XML | 1qpx_validation.xml.gz | 9.9 KB | Display | |
Data in CIF | 1qpx_validation.cif.gz | 14.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qp/1qpx ftp://data.pdbj.org/pub/pdb/validation_reports/qp/1qpx | 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: 24536.859 Da / Num. of mol.: 2 / Mutation: Q108C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P15319 #2: 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: 2.35 Å3/Da / Density % sol: 47.61 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.2 Details: PEG 4000, isopropanol, acetate buffer, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.5 Details: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5412 |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Aug 25, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5412 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. all: 18542 / Num. obs: 18542 / % possible obs: 99.3 % / Observed criterion σ(F): -999 / Observed criterion σ(I): -999 / Redundancy: 5.8 % / Biso Wilson estimate: 43.245 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 16.7 |
Reflection shell | Resolution: 2.4→2.44 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.27 / Num. unique all: 863 / % possible all: 93.8 |
Reflection | *PLUS Num. measured all: 107688 |
Reflection shell | *PLUS % possible obs: 93.8 % / Mean I/σ(I) obs: 4.1 |
-Processing
Software |
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Refinement | Resolution: 2.4→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||
Refine LS restraints | *PLUS
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