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Yorodumi- PDB-1htr: CRYSTAL AND MOLECULAR STRUCTURES OF HUMAN PROGASTRICSIN AT 1.62 A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1htr | ||||||
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Title | CRYSTAL AND MOLECULAR STRUCTURES OF HUMAN PROGASTRICSIN AT 1.62 ANGSTROMS RESOLUTION | ||||||
Components |
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Keywords | ASPARTYL PROTEASE | ||||||
Function / homology | Function and homology information gastricsin / positive regulation of antibacterial peptide production / digestion / aspartic-type endopeptidase activity / proteolysis / extracellular space Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.62 Å | ||||||
Authors | Moore, S.A. / Sielecki, A.R. / James, M.N.G. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Crystal and molecular structures of human progastricsin at 1.62 A resolution. Authors: Moore, S.A. / Sielecki, A.R. / Chernaia, M.M. / Tarasova, N.I. / James, M.N. #1: Journal: Biochim.Biophys.Acta / Year: 1990 Title: Isolation, Crystallization and Preliminary X-Ray Diffraction Data of Human Progastricsin Authors: Ivanov, P.K. / Chernaia, M. / Gustchina, A.E. / Pechik, I.V. / Nikonov, S.V. / Tarasova, N.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1htr.cif.gz | 84.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1htr.ent.gz | 68.3 KB | Display | PDB format |
PDBx/mmJSON format | 1htr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ht/1htr ftp://data.pdbj.org/pub/pdb/validation_reports/ht/1htr | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO B 23 |
-Components
#1: Protein/peptide | Mass: 5137.138 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: GASTRIC MUCOSA CELL: CHIEF CELLS / Organ: STOMACH / References: UniProt: P20142, gastricsin |
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#2: Protein | Mass: 35464.930 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: GASTRIC MUCOSA CELL: CHIEF CELLS / Organ: STOMACH / References: UniProt: P20142, gastricsin |
#3: Water | ChemComp-HOH / |
Compound details | COMPND THE MOLECULE IS SYNTHESIZED IN THE STOMACH IN THIS INACTIVE ZYMOGEN FORM. AFTER ACTIVATION ...COMPND THE MOLECULE IS SYNTHESIZE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.82 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: seeding / PH range low: 6.5 / PH range high: 6 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 50353 / % possible obs: 96 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 1.62 Å / Rmerge(I) obs: 0.059 |
-Processing
Software |
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Refinement | Resolution: 1.62→20 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 27.75 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.62→20 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ/TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 50353 / Rfactor all: 0.179 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |