+Open data
-Basic information
Entry | Database: PDB / ID: 1bg8 | ||||||
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Title | HDEA FROM ESCHERICHIA COLI | ||||||
Components | HDEA | ||||||
Keywords | PERIPLASMIC / HDEA | ||||||
Function / homology | Function and homology information cellular stress response to acidic pH / cellular response to acidic pH / chaperone-mediated protein folding / protein folding chaperone / unfolded protein binding / protein-folding chaperone binding / outer membrane-bounded periplasmic space / protein homodimerization activity / identical protein binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.2 Å | ||||||
Authors | Yang, F. / Gustafson, K.R. / Boyd, M.R. / Wlodawer, A. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1998 Title: Crystal structure of Escherichia coli HdeA. Authors: Yang, F. / Gustafson, K.R. / Boyd, M.R. / Wlodawer, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bg8.cif.gz | 54.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bg8.ent.gz | 43.8 KB | Display | PDB format |
PDBx/mmJSON format | 1bg8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bg8_validation.pdf.gz | 440.9 KB | Display | wwPDB validaton report |
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Full document | 1bg8_full_validation.pdf.gz | 447.9 KB | Display | |
Data in XML | 1bg8_validation.xml.gz | 13.8 KB | Display | |
Data in CIF | 1bg8_validation.cif.gz | 19.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bg/1bg8 ftp://data.pdbj.org/pub/pdb/validation_reports/bg/1bg8 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS oper:
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-Components
#1: Protein | Mass: 9752.882 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P26604, UniProt: P0AES9*PLUS #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: 2.2 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||
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Crystal grow | pH: 3.6 Details: 36% PEG400, 5% GLYCEROL, 50MM SODIUM CITRATE, PH 3.6 | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 16, 1998 / Details: MIRRORS |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→40 Å / Num. obs: 12863 / % possible obs: 97.2 % / Observed criterion σ(I): -3 / Redundancy: 3.6 % / Rsym value: 0.071 / Net I/σ(I): 8.4 |
Reflection shell | Resolution: 2.2→2.26 Å / Rsym value: 0.473 / % possible all: 94.8 |
Reflection | *PLUS Rmerge(I) obs: 0.071 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.2→10 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Cross valid method: FREE R / σ(F): 2
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Displacement parameters | Biso mean: 40.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell | Resolution: 2.2→2.3 Å / Total num. of bins used: 8
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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