+Open data
-Basic information
Entry | Database: PDB / ID: 1jvw | ||||||
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Title | TRYPANOSOMA CRUZI MACROPHAGE INFECTIVITY POTENTIATOR (TCMIP) | ||||||
Components | MACROPHAGE INFECTIVITY POTENTIATOR | ||||||
Keywords | ISOMERASE / Macrophage Infectivity Potentiator / Trypanosoma cruzi / Chagas disease / X-ray crystal structure / rotamase | ||||||
Function / homology | Function and homology information peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / extracellular region Similarity search - Function | ||||||
Biological species | Trypanosoma cruzi (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Pereira, P.J.B. / Vega, M.C. / Gonzalez-Rey, E. / Fernandez-Carazo, R. / Macedo-Ribeiro, S. / Gomis-Rueth, F.X. / Gonzalez, A. / Coll, M. | ||||||
Citation | Journal: EMBO Rep. / Year: 2002 Title: Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix. Authors: Pereira, P.J. / Vega, M.C. / Gonzalez-Rey, E. / Fernandez-Carazo, R. / Macedo-Ribeiro, S. / Gomis-Ruth, F.X. / Gonzalez, A. / Coll, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jvw.cif.gz | 50.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jvw.ent.gz | 35 KB | Display | PDB format |
PDBx/mmJSON format | 1jvw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jv/1jvw ftp://data.pdbj.org/pub/pdb/validation_reports/jv/1jvw | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18863.271 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma cruzi (eukaryote) / Production host: Escherichia coli (E. coli) / References: UniProt: Q09734, peptidylprolyl isomerase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.14 % | ||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: small tubes / pH: 7.5 Details: PMSF, Tris/HCl, pH 7.5, SMALL TUBES, temperature 277K | ||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: microdialysis | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.885 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 20, 1997 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.885 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→19.2 Å / Num. obs: 17009 / % possible obs: 95.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.7→1.79 Å / % possible all: 89.8 |
Reflection | *PLUS Highest resolution: 1.7 Å / Redundancy: 3.6 % / Num. measured all: 60547 / Rmerge(I) obs: 0.081 |
Reflection shell | *PLUS Highest resolution: 1.7 Å / % possible obs: 89.8 % / Rmerge(I) obs: 0.097 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→19 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→19 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 5 % / Rfactor all: 0.179 / Rfactor Rfree: 0.231 / Rfactor Rwork: 0.176 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |