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Open data
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Basic information
Entry | Database: PDB / ID: 2go2 | ||||||
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Title | Crystal structure of BbKI, a Kunitz-type kallikrein inhibitor | ||||||
![]() | Kunitz-type serine protease inhibitor BbKI | ||||||
![]() | PROTEIN BINDING / BETA-TREFOIL FOLD | ||||||
Function / homology | ![]() endopeptidase inhibitor activity / serine-type endopeptidase inhibitor activity / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Navarro, M.V.A.S. / Garratt, R.C. | ||||||
![]() | ![]() Title: The Crystal Structure of BbKI, a kunitz-type kallikrein inhibitor devoid of disulfide bridges Authors: Navarro, M.V.A.S. / Oliva, M.L.V. / Araujo, A.P.U. / Garratt, R.C. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2005 Title: Crystallization and preliminary X-ray analysis of a novel Kunitz-type kallikrein inhibitor from Bauhinia bauhinioides Authors: Navarro, M.V. / Vierira, D.F. / Nagem, R.A. / de Araujo, A.P. / Oliva, M.L. / Garratt, R.C. #2: Journal: Acta Crystallogr.,Sect.D / Year: 2005 Title: Getting the most out of X-ray home sources Authors: Nagem, R.A. / Ambrosio, A.L. / Rojas, A.L. / Navarro, M.V. / Golubev, A.M. / Garratt, R.C. / Polikarpov, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 49 KB | Display | ![]() |
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PDB format | ![]() | 35.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.7 KB | Display | ![]() |
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Full document | ![]() | 440.6 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 15.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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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Details | The asymmetric unit of the crystal contains a monomer, which represents the biological assembly |
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Components
#1: Protein | Mass: 17839.266 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.51 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 8%(w/v) PEG 4000, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Apr 10, 2004 / Details: mirrors |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.87→26.44 Å / Num. obs: 14628 / % possible obs: 95.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 8.5 % / Rmerge(I) obs: 0.044 / Net I/σ(I): 32.8 |
Reflection shell | Resolution: 1.87→1.97 Å / Redundancy: 8.4 % / Rmerge(I) obs: 0.207 / Mean I/σ(I) obs: 10.7 / % possible all: 91.7 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 14.291 Å2
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Refinement step | Cycle: LAST / Resolution: 1.87→19.73 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.87→1.918 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 42.901 Å / Origin y: 58.142 Å / Origin z: 7.866 Å
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Refinement TLS group |
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