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Open data
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Basic information
Entry | Database: PDB / ID: 1h9i | ||||||
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Title | COMPLEX OF EETI-II MUTANT WITH PORCINE TRYPSIN | ||||||
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![]() | HYDROLASE/INHIBITOR / COMPLEX (SERINE PROTEASE-INHIBITOR) / TRYPSIN / SQUASH INHIBITOR / CYSTINE KNOT / HYDROLASE-INHIBITOR complex | ||||||
Function / homology | ![]() trypsin / digestion / serine-type endopeptidase inhibitor activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kraetzner, R. / Wentzel, A. / Kolmar, H. / Uson, I. | ||||||
![]() | ![]() Title: Structure of Ecballium Elaterium Trypsin Inhibitor II (Eeti-II): A Rigid Molecular Scaffold Authors: Kraetzner, R. / Debreczeni, J.E. / Pape, T. / Schneider, T.R. / Wentzel, A. / Kolmar, H. / Sheldrick, G.M. / Uson, I. #1: Journal: J.Biol.Chem. / Year: 1999 Title: Sequence Requirements of the Gpng Beta-Turn of the Ecballium Elaterium Trypsin Inhibitor II Explored by Combinatorial Library Screening Authors: Wentzel, A. / Christmann, A. / Kraetzner, R. / Kolmar, H. #2: Journal: Biochemistry / Year: 1999 Title: Min-21 and Min-23, the Smallest Peptides that Fold Like a Cystine-Stabilized Beta-Sheet Motif: Design, Solution Structure, and Thermal Stability Authors: Heitz, A. / Le-Nguyen, D. / Chiche, L. #3: ![]() Title: Use of Restrained Molecular Dynamics in Water to Determine Three-Dimensional Protein Structure: Prediction of the Three-Dimensional Structure of Ecballium Elaterium Trypsin Inhibitor II Authors: Chiche, L. / Gaboriaud, C. / Heitz, A. / Mornon, J.P. / Castro, B. / Kollman, P.A. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "B" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "B" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66.6 KB | Display | ![]() |
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PDB format | ![]() | 47.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1h9hC ![]() 1w7zC ![]() 1ldtS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23493.496 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SIGMA / Source: (natural) ![]() ![]() |
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#2: Protein/peptide | Mass: 4035.668 Da / Num. of mol.: 1 / Mutation: YES / Source method: obtained synthetically / Details: C-TERMINAL TAG OF 6 HISTIDINES / Source: (synth.) ![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Compound details | CHAIN I ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 56 % |
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Crystal grow | pH: 6.7 / Details: pH 6.70 |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 3, 2000 / Details: OSMIC MIRROR SYSTEM |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54187 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→15 Å / Num. obs: 26024 / % possible obs: 99.1 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.0683 / Rsym value: 0.0405 / Net I/σ(I): 17.84 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 6.31 % / Rmerge(I) obs: 0.2171 / Mean I/σ(I) obs: 8.89 / Rsym value: 0.1031 / % possible all: 97.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1LDT Resolution: 1.9→10 Å / Num. parameters: 8079 / Num. restraintsaints: 7813 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 13 / Occupancy sum hydrogen: 1741 / Occupancy sum non hydrogen: 1958 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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