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Open data
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Basic information
Entry | Database: PDB / ID: 5awl | ||||||
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Title | CRYSTAL STRUCTURE OF A MUTANT OF CHIGNOLIN, CLN025 | ||||||
![]() | A mutant of Chignolin, CLN025 | ||||||
![]() | DE NOVO PROTEIN / BETA-HAIRPIN / MINI-PROTEIN / MINIATURE PROTEIN | ||||||
Biological species | synthetic construct (others) | ||||||
Method | ![]() | ||||||
![]() | Akiba, T. / Ishimura, M. / Odahara, T. / Harata, K. / Honda, S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Crystal structure of a ten-amino acid protein Authors: Honda, S. / Akiba, T. / Kato, Y.S. / Sawada, Y. / Sekijima, M. / Ishimura, M. / Ooishi, A. / Watanabe, H. / Odahara, T. / Harata, K. #1: ![]() Title: 10 residue folded peptide designed by segment statistics. Authors: Honda, S. / Yamasaki, K. / Sawada, Y. / Morii, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 14.7 KB | Display | ![]() |
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PDB format | ![]() | 8.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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: 1294.322 Da / Num. of mol.: 1 / Mutation: G1Y G10Y / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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#2: 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: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.4 Å3/Da / Density % sol: 14.1 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 5 Details: using 2 uL drop of protein at 5 mg/mL in a solution of 35.7 mM sodium citrate-citric acid buffer (pH 5.0) containing 14.5% saturated ammonium sulfate against a crystallization well solution ...Details: using 2 uL drop of protein at 5 mg/mL in a solution of 35.7 mM sodium citrate-citric acid buffer (pH 5.0) containing 14.5% saturated ammonium sulfate against a crystallization well solution of 71.4 mM sodium citrate-citric acid buffer (pH 5.0) containing 29% saturated ammonium sulfate. PH range: 5 |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() |
Detector | Type: BRUKER SMART 6000 / Detector: CCD / Date: Dec 9, 2005 / Details: OSMIC CONFOCAL MAX-FLUX |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.11→16.8 Å / Num. obs: 3094 / % possible obs: 95.9 % / Redundancy: 6.5 % / Rmerge(I) obs: 0.057 / Net I/σ(I): 26.4 |
Reflection shell | Resolution: 1.11→1.71 Å / Redundancy: 4 % / Rmerge(I) obs: 0.203 / Mean I/σ(I) obs: 5 / % possible all: 88.9 |
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Processing
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Refinement | Method to determine structure: AB INITIO PHASING / Resolution: 1.11→16.8 Å / Num. parameters: 940 / Num. restraintsaints: 1193 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 73 / Occupancy sum non hydrogen: 103.5 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.11→16.8 Å
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Refine LS restraints |
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