+Open data
-Basic information
Entry | Database: PDB / ID: 2uux | ||||||
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Title | Structure of the tryptase inhibitor TdPI from a tick | ||||||
Components | TRYPTASE INHIBITOR | ||||||
Keywords | INHIBITOR / TRYPTASE INHIBITOR | ||||||
Function / homology | Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Pancreatic trypsin inhibitor Kunitz domain superfamily / serine-type endopeptidase inhibitor activity / Few Secondary Structures / Irregular / Tryptase inhibitor Function and homology information | ||||||
Biological species | RHIPICEPHALUS APPENDICULATUS (arthropod) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.4 Å | ||||||
Authors | Siebold, C. / Paesen, G.C. / Harlos, K. / Peacey, M.F. / Nuttall, P.A. / Stuart, D.I. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: A Tick Protein with a Modified Kunitz Fold Inhibits Human Tryptase. Authors: Paesen, G.C. / Siebold, C. / Harlos, K. / Peacey, M.F. / Nuttall, P.A. / Stuart, D.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2uux.cif.gz | 33.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2uux.ent.gz | 26.3 KB | Display | PDB format |
PDBx/mmJSON format | 2uux.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2uux_validation.pdf.gz | 424 KB | Display | wwPDB validaton report |
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Full document | 2uux_full_validation.pdf.gz | 424.2 KB | Display | |
Data in XML | 2uux_validation.xml.gz | 5.7 KB | Display | |
Data in CIF | 2uux_validation.cif.gz | 7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uu/2uux ftp://data.pdbj.org/pub/pdb/validation_reports/uu/2uux | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 6049.021 Da / Num. of mol.: 1 / Fragment: RESIDUES 44-96 / Source method: isolated from a natural source / Source: (natural) RHIPICEPHALUS APPENDICULATUS (arthropod) / References: UniProt: Q1EG59 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.58 Å3/Da / Density % sol: 35.56 % |
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Crystal grow | Details: 2.4 M AMMONIUM SULFATE 0.1 M TRIS-HCL, PH 8 20% MPD |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.934 |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→20 Å / Num. obs: 10942 / % possible obs: 91 % / Observed criterion σ(I): 1.5 / Redundancy: 8.8 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 21 |
Reflection shell | Resolution: 1.4→1.5 Å / Redundancy: 4 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 1.6 / % possible all: 72 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.4→19.57 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.932 / SU B: 2.504 / SU ML: 0.045 / Cross valid method: THROUGHOUT / ESU R: 0.09 / ESU R Free: 0.08 / 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: 13.35 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→19.57 Å
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Refine LS restraints |
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