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Yorodumi- PDB-1lep: THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lep | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROTEIN CHAPERONIN-10 OF MYCOBACTERIUM LEPRAE | ||||||
Components | CHAPERONIN-10 | ||||||
Keywords | CHAPERONE / ANTIGEN / HEAT SHOCK | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Mycobacterium leprae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3.5 Å | ||||||
Authors | Mande, S.C. / Hol, W.G.J. | ||||||
Citation | Journal: Science / Year: 1996 Title: Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. Authors: Mande, S.C. / Mehra, V. / Bloom, B.R. / Hol, W.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lep.cif.gz | 27.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lep.ent.gz | 16.4 KB | Display | PDB format |
PDBx/mmJSON format | 1lep.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lep_validation.pdf.gz | 322.9 KB | Display | wwPDB validaton report |
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Full document | 1lep_full_validation.pdf.gz | 322.9 KB | Display | |
Data in XML | 1lep_validation.xml.gz | 720 B | Display | |
Data in CIF | 1lep_validation.cif.gz | 5.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/le/1lep ftp://data.pdbj.org/pub/pdb/validation_reports/le/1lep | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 10682.150 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) Mycobacterium leprae (bacteria) / References: UniProt: P24301 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Rmerge(I) obs: 0.088 |
Reflection | *PLUS Highest resolution: 3.5 Å / % possible obs: 98 % |
Reflection shell | *PLUS Highest resolution: 3.5 Å / Lowest resolution: 3.6 Å / % possible obs: 90 % |
-Processing
Software |
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Refinement | Resolution: 3.5→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 40 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.5→8 Å
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Refine LS restraints |
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