+Open data
-Basic information
Entry | Database: PDB / ID: 3kza | ||||||
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Title | Crystal structure of Gyuba, a patched chimera of b-lactglobulin | ||||||
Components | Beta-lactoglobulin | ||||||
Keywords | TRANSPORT PROTEIN / artificial protein / chimera protein / Disulfide bond / Milk protein / Retinol-binding / Secreted / Transport | ||||||
Function / homology | Function and homology information retinol binding / long-chain fatty acid binding / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Equus caballus (horse) Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Tsuge, H. / Ohtomo, H. / Utsunomiya, H. / Konuma, T. / Ikeguchi, M. | ||||||
Citation | Journal: Protein Sci. / Year: 2011 Title: Structure and stability of Gyuba, a patched chimera of b-lactoglobulin Authors: Ohtomo, H. / Konuma, T. / Utsunoiya, H. / Tsuge, H. / Ikeguchi, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3kza.cif.gz | 72.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3kza.ent.gz | 58.4 KB | Display | PDB format |
PDBx/mmJSON format | 3kza.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kz/3kza ftp://data.pdbj.org/pub/pdb/validation_reports/kz/3kza | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 18310.939 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: AN ARTIFICIAL CHIMERA PROTEIN OF BOS-TAURAS AND EQUINE B-LACTOGLOBULIN. THE RESIDUES 1-16, 28-41, 50, 51, 63-65, 74-49, 87, 88, 96-101, 109-116, 125-129, 139-144, 154-162 ARE FROM EQUINE, ...Details: AN ARTIFICIAL CHIMERA PROTEIN OF BOS-TAURAS AND EQUINE B-LACTOGLOBULIN. THE RESIDUES 1-16, 28-41, 50, 51, 63-65, 74-49, 87, 88, 96-101, 109-116, 125-129, 139-144, 154-162 ARE FROM EQUINE, THE RESIDUES 17-27, 42-49, 52-62, 66-73, 80-86, 89-95, 102-108, 117-124, 130-138, 145-153 ARE FROM BOS-TAURAS. Source: (gene. exp.) Equus caballus (horse), (gene. exp.) Bos taurus (cattle) Gene: LGB1 / Plasmid: pET3c / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P02758, UniProt: P02754 #2: Water | ChemComp-HOH / | Sequence details | THIS IS AN ARTIFICIAL | |
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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: 2.84 Å3/Da / Density % sol: 56.67 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 2.0M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2→59.66 Å / Num. obs: 27566 / % possible obs: 99.8 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 10.9 % / Rsym value: 0.066 / Net I/σ(I): 15.2 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 9.6 % / Num. unique all: 2741 / Rsym value: 0.314 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→59.66 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.91 / SU B: 4.16 / SU ML: 0.121 / Cross valid method: THROUGHOUT / ESU R: 0.193 / ESU R Free: 0.182 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.665 Å2
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Refinement step | Cycle: LAST / Resolution: 2→59.66 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.998→2.05 Å / Total num. of bins used: 20
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