+Open data
-Basic information
Entry | Database: PDB / ID: 1g9i | ||||||
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Title | CRYSTAL STRUCTURE OF BETA-TRYSIN COMPLEX IN CYCLOHEXANE | ||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / TRYPSIN-INHIBITOR COMPLEX / ORGANIC MEDIA / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information cap snatching / virion component / serine-type endopeptidase inhibitor activity / hydrolase activity / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / nucleotide binding / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Zhu, G. / Huang, Q. / Zhu, Y. / Li, Y. / Chi, C. / Tang, Y. | ||||||
Citation | |||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g9i.cif.gz | 64.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g9i.ent.gz | 45.6 KB | Display | PDB format |
PDBx/mmJSON format | 1g9i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1g9i_validation.pdf.gz | 433.3 KB | Display | wwPDB validaton report |
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Full document | 1g9i_full_validation.pdf.gz | 439.2 KB | Display | |
Data in XML | 1g9i_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | 1g9i_validation.cif.gz | 19.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g9/1g9i ftp://data.pdbj.org/pub/pdb/validation_reports/g9/1g9i | HTTPS FTP |
-Related structure data
Related structure data | 1smfS S: Starting model for refinement |
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Similar 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: 23324.287 Da / Num. of mol.: 1 / Fragment: BETA-TRYPSIN / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P00760, trypsin | ||
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#2: Protein/peptide | Mass: 2411.823 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This peptide was chemically synthesized. The sequence is based on mimic bean trypsin inhibitor. References: UniProt: P01062 | ||
#3: Chemical | ChemComp-CA / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.57 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 297 K / Method: vapor diffusion, hanging drop / pH: 6.4 Details: 2M ammonium sulphate, 0.2M phosphate buffer, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 297K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 24 ℃ / Details: Li, Y., (1994) J.Biochem.(Tokyo), 116, 18. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 1, 1998 |
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: 2.2→70 Å / Num. all: 14471 / Num. obs: 12041 / % possible obs: 83.2 % / Observed criterion σ(F): 1.5 / Observed criterion σ(I): 0.75 / Redundancy: 3.7 % / Biso Wilson estimate: 18.7 Å2 / Rmerge(I) obs: 0.093 / Net I/σ(I): 7 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2 % / Rmerge(I) obs: 0.217 / Mean I/σ(I) obs: 2 / % possible all: 62.3 |
Reflection shell | *PLUS % possible obs: 62.3 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1SMF Resolution: 2.2→7 Å / σ(F): 1.5 / σ(I): 0.75 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→7 Å
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Refine LS restraints |
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LS refinement shell |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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