+Open data
-Basic information
Entry | Database: PDB / ID: 3wmi | ||||||
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Title | Crystal structure of EIAV wild type gp45 | ||||||
Components | (EIAV gp45 wild type) x 2 | ||||||
Keywords | VIRAL PROTEIN / alpha-helix / virus fusion | ||||||
Function / homology | Function and homology information viral envelope / host cell plasma membrane / virion membrane / structural molecule activity / plasma membrane Similarity search - Function | ||||||
Biological species | Equine (horse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Liu, X. / Du, J. / Qiao, W. | ||||||
Citation | Journal: To be Published Title: A mutation associated with EIAV vaccine strain within heptad repeat of EIAV gp45 provides insight into vaccine development for HIV Authors: Liu, X. / Du, J. / Qiao, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3wmi.cif.gz | 34.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3wmi.ent.gz | 23.7 KB | Display | PDB format |
PDBx/mmJSON format | 3wmi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wm/3wmi ftp://data.pdbj.org/pub/pdb/validation_reports/wm/3wmi | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 6578.155 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Equine (horse) / Production host: Escherichia coli (E. coli) / References: UniProt: E2E2L9*PLUS |
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#2: Protein/peptide | Mass: 4450.874 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Equine (horse) / Production host: Escherichia coli (E. coli) / References: UniProt: E2E2L9*PLUS |
#3: Water | ChemComp-HOH / |
Sequence details | THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEBASE DATABASE (UNIPROTKB) AT ...THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEB |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.95 Å3/Da / Density % sol: 58.34 % |
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Crystal grow | Temperature: 293 K / Method: evaporation / pH: 5.5 Details: 0.1M Bis-Tris, 2M NaCl, pH 5.5, EVAPORATION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9794 Å |
Detector | Type: ENRAF-NONIUS / Detector: CCD / Date: May 9, 2011 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→31.824 Å / Num. obs: 10074 / % possible obs: 11 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2.9 |
Reflection shell | Resolution: 1.9→1.93 Å / % possible all: 95 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→31.824 Å / SU ML: 0.24 / σ(F): 1.4 / Phase error: 23.41 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→31.824 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 3
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