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Open data
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Basic information
Entry | Database: PDB / ID: 1ld5 | ||||||
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Title | STRUCTURE OF BPTI MUTANT A16V | ||||||
![]() | PANCREATIC TRYPSIN INHIBITOR | ||||||
![]() | Hydrolase Inhibitor / BPTI / Kunitz fold | ||||||
Function / homology | ![]() trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / serine protease inhibitor complex / serine-type endopeptidase inhibitor activity ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / serine protease inhibitor complex / serine-type endopeptidase inhibitor activity / protease binding / calcium ion binding / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
![]() | Cierpicki, T. / Otlewski, J. | ||||||
![]() | ![]() Title: NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability. Authors: Cierpicki, T. / Otlewski, J. #1: ![]() Title: Substitutions at the P1' position in BPTI strongly affect the association energy with serine proteinases Authors: Grzesiak, A. / Helland, R. / Smalas, A.O. / Krowarsch, D. / Dadlez, M. / Otlewski, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 177.9 KB | Display | ![]() |
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PDB format | ![]() | 153.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 339.7 KB | Display | ![]() |
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Full document | ![]() | 404.1 KB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 19.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6565.597 Da / Num. of mol.: 1 / Mutation: A16V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: Structure was determined based on homonuclear TOCSY/NOESY techniques using automatic assignment in NOAH/DYANA program |
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Sample preparation
Details | Contents: 4mM BPTI_A16V / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0 / pH: 3.1 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy,target function Conformers calculated total number: 48 / Conformers submitted total number: 10 |