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- PDB-1oa6: The solution structure of bovine pancreatic trypsin inhibitor at ... -

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Basic information

Entry
Database: PDB / ID: 1oa6
TitleThe solution structure of bovine pancreatic trypsin inhibitor at high pressure
ComponentsPANCREATIC TRYPSIN INHIBITOR
KeywordsHYDROLASE INHIBITOR / 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 / 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 / potassium channel inhibitor activity / negative regulation of platelet aggregation / 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
Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Pancreatic trypsin inhibitor
Similarity search - Component
Biological speciesBOS TAURUS (cattle)
MethodSOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS
AuthorsWilliamson, M.P. / Akasaka, K. / Refaee, M.
CitationJournal: Protein Sci. / Year: 2003
Title: The Solution Structure of Bovine Pancreatic Trypsin Inhibitor at High Pressure
Authors: Williamson, M.P. / Akasaka, K. / Refaee, M.
History
DepositionJan 2, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 28, 2003Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
5: PANCREATIC TRYPSIN INHIBITOR


Theoretical massNumber of molelcules
Total (without water)6,5281
Polymers6,5281
Non-polymers00
Water724
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)3 / 3
Representative

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Components

#1: Protein PANCREATIC TRYPSIN INHIBITOR / BPTI / APROTININ / TRASYLOL / BASIC PROTEASE INHIBITOR


Mass: 6527.568 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) BOS TAURUS (cattle) / Organ: PANCREAS / References: UniProt: P00974
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
NMR detailsText: THE STRUCTURE CALCULATION IS A CHANGE BETWEEN 1 AND 2000 ATMOSPHERES, BASED ON CHEMICAL SHIFT RESTRAINTS.

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Sample preparation

DetailsContents: 200 MM SODIUM ACETATE, 10MM PROTEIN
Sample conditionsIonic strength: 0.2 M / pH: 4.6 / Pressure: 2000 atm / Temperature: 309 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
XPLORstructure solution
RefinementMethod: RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1
Details: THE ONLY RESTRAINTS USED WERE HOLONOMIC PLUS CHEMICAL SHIFT RESTRAINTS. THESE STRUCTURES WERE RESTRAINED USING THE EXPERIMENTAL CHANGES IN CHEMICAL SHIFT FROM 1 - 2000 ATM.
NMR ensembleConformers calculated total number: 3 / Conformers submitted total number: 3

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