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Yorodumi- PDB-1c94: REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1c94 | ||||||
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Title | REVERSING THE SEQUENCE OF THE GCN4 LEUCINE ZIPPER DOES NOT AFFECT ITS FOLD. | ||||||
Components | RETRO-GCN4 LEUCINE ZIPPER | ||||||
Keywords | GENE REGULATION / RETRO-COILED COIL / 4-ALPHA-HELIX-BUNDLE / PEPTIDE SYNTHESIS | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.08 Å | ||||||
Authors | Mittl, P.R.E. / Deillon, C.A. / Sargent, D. / Liu, N. / Klauser, S. / Thomas, R.M. / Gutte, B. / Gruetter, M.G. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2000 Title: The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure. Authors: Mittl, P.R. / Deillon, C. / Sargent, D. / Liu, N. / Klauser, S. / Thomas, R.M. / Gutte, B. / Grutter, M.G. #1: Journal: Science / Year: 1991 Title: X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil. Authors: O'Shea, E.K. / Klemm, J.D. / Kim, P.S. / Alber, T. #2: Journal: Science / Year: 1993 Title: A Switch Between Two-, Three-, and Four-Stranded Coiled Coils in GCN4 Leucine Zipper Mutants. Authors: Harbury, P.B. / Zhang, T. / Kim, P.S. / Alber, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c94.cif.gz | 26.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c94.ent.gz | 18.7 KB | Display | PDB format |
PDBx/mmJSON format | 1c94.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1c94_validation.pdf.gz | 370 KB | Display | wwPDB validaton report |
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Full document | 1c94_full_validation.pdf.gz | 374 KB | Display | |
Data in XML | 1c94_validation.xml.gz | 3.7 KB | Display | |
Data in CIF | 1c94_validation.cif.gz | 5.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c9/1c94 ftp://data.pdbj.org/pub/pdb/validation_reports/c9/1c94 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein/peptide | Mass: 4464.196 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED #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: 1.84 Å3/Da / Density % sol: 33.07 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 4.8 Details: 25% 2-METHYL-2,4-PENTANEDIOL, 100 MM SODIUM ACETATE, 200 MM SODIUM CHLORIDE., pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K | |||||||||||||||||||||||||
Crystal grow | *PLUS Details: drop contained 1:1 mixture of peptide and reservoir solution | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 | |||||||||||||||
Reflection | Resolution: 2.08→20 Å / Num. all: 4280 / Num. obs: 3740 / % possible obs: 87.4 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.035 | |||||||||||||||
Reflection shell | Resolution: 2→2.1 Å / Rmerge(I) obs: 0.11 / % possible all: 80.7 | |||||||||||||||
Reflection | *PLUS % possible obs: 87.2 % | |||||||||||||||
Reflection shell | *PLUS % possible obs: 80.7 % |
-Processing
Software |
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Refinement | Resolution: 2.08→20 Å / σ(F): 0 / σ(I): 0 Stereochemistry target values: CNS-TOPPAR PROTEIN_REP.PARAM CNS-TOPPAR WATER_REP.PARAM Details: PHASE SOLUTION FOUND THROUGH MOLECULAR REPLACEMENT.
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Refinement step | Cycle: LAST / Resolution: 2.08→20 Å
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Refine LS restraints |
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