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Yorodumi- PDB-1aal: STRUCTURAL EFFECTS INDUCED BY MUTAGENESIS AFFECTED BY CRYSTAL PAC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1aal | ||||||
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Title | STRUCTURAL EFFECTS INDUCED BY MUTAGENESIS AFFECTED BY CRYSTAL PACKING FACTORS: THE STRUCTURE OF A 30-51 DISULFIDE MUTANT OF BASIC PANCREATIC TRYPSIN INHIBITOR | ||||||
Components | BOVINE PANCREATIC TRYPSIN INHIBITOR | ||||||
Keywords | SERINE PROTEASE INHIBITOR | ||||||
Function / homology | Function and homology information trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / zymogen binding / serine protease inhibitor complex / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / serine-type endopeptidase inhibitor activity ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / zymogen binding / serine protease inhibitor complex / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / serine-type endopeptidase inhibitor activity / protease binding / calcium ion binding / extracellular space Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.6 Å | ||||||
Authors | Eigenbrot, C. / Randal, M. / Kossiakoff, A.A. | ||||||
Citation | Journal: Proteins / Year: 1992 Title: Structural effects induced by mutagenesis affected by crystal packing factors: the structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor. Authors: Eigenbrot, C. / Randal, M. / Kossiakoff, A.A. #1: Journal: Protein Eng. / Year: 1990 Title: Structural Effects Induced by Removal of a Disulfide Bridge: The X-Ray Structure of the C30A(Slash)C51A Mutant of Basic Pancreatic Trypsin Inhibitor at 1.6 Angstroms Authors: Eigenbrot, C. / Randal, M. / Kossiakoff, A.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1aal.cif.gz | 35 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1aal.ent.gz | 27.1 KB | Display | PDB format |
PDBx/mmJSON format | 1aal.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1aal_validation.pdf.gz | 438 KB | Display | wwPDB validaton report |
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Full document | 1aal_full_validation.pdf.gz | 448.4 KB | Display | |
Data in XML | 1aal_validation.xml.gz | 9.9 KB | Display | |
Data in CIF | 1aal_validation.cif.gz | 13.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aa/1aal ftp://data.pdbj.org/pub/pdb/validation_reports/aa/1aal | HTTPS FTP |
-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: THE FOLLOWING RESIDUES MODELLED WITH 2 SIDE CHAIN CONFORMATIONS: GLU A 7, ARG A 17, ARG A 39, GLU A 49, ASP B 3, ARG B 17, ARG B 39, ARG B 42, GLU B 49. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.785512, -0.594349, -0.172394), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL GENERATE APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO CHAIN A. | |
-Components
#1: Protein | Mass: 6491.490 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P00974 #2: Chemical | ChemComp-PO4 / | #3: Water | ChemComp-HOH / | Compound details | THERE IS A UNIQUE SALT-BRIDGE BETWEEN THE N AND C TERMINALS OF MOLECULES WITH RESIDUE NUMBERS 1 - ...THERE IS A UNIQUE SALT-BRIDGE BETWEEN THE N AND C TERMINALS OF MOLECULES WITH RESIDUE NUMBERS 1 - 58, WHICH HAS BEEN SEEN IN SOLUTION (NMR) BUT NEVER CRYSTALLOG | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.57 % |
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Crystal grow | *PLUS pH: 10 / Method: vapor diffusion, hanging drop |
Components of the solutions | *PLUS Conc.: 0.7 M / Chemical formula: NaKPO4 |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 8 Å / Num. obs: 16638 / Rmerge(I) obs: 0.131 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.6→8 Å / σ(I): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.6→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 8 Å / Num. reflection obs: 15473 / σ(I): 1 / Rfactor obs: 0.179 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |