+Open data
-Basic information
Entry | Database: PDB / ID: 1p9i | ||||||
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Title | Coiled-coil X-ray structure at 1.17 A resolution | ||||||
Components | cortexillin I/GCN4 hybrid peptide | ||||||
Keywords | UNKNOWN FUNCTION / coiled-coil | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.17 Å | ||||||
Authors | Ivaninskii, S. | ||||||
Citation | Journal: Protein Sci. / Year: 2003 Title: Unique stabilizing interactions identified in the two-stranded alpha-helical coiled-coil: crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptide. Authors: Lee, D.L. / Ivaninskii, S. / Burkhard, P. / Hodges, R.S. | ||||||
History |
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Remark 999 | This peptide is a hybrid of two proteins: GCN4 and cortexillin I. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p9i.cif.gz | 19.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p9i.ent.gz | 14.2 KB | Display | PDB format |
PDBx/mmJSON format | 1p9i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p9/1p9i ftp://data.pdbj.org/pub/pdb/validation_reports/p9/1p9i | 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 on special symmetry positions |
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-Components
#1: Protein/peptide | Mass: 3400.935 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.73 Å3/Da / Density % sol: 29.01 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.17→20.77 Å / Num. all: 8174 / Num. obs: 8174 |
Reflection | *PLUS Num. obs: 8183 / % possible obs: 97.8 % / Num. measured all: 263880 / Rmerge(I) obs: 0.037 |
-Processing
Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.17→20 Å /
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Refinement step | Cycle: LAST / Resolution: 1.17→20 Å
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Refine LS restraints | *PLUS
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