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- PDB-1ntp: USE OF THE NEUTRON DIFFRACTION H/D EXCHANGE TECHNIQUE TO DETERMIN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ntp | ||||||
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Title | USE OF THE NEUTRON DIFFRACTION H/D EXCHANGE TECHNIQUE TO DETERMINE THE CONFORMATIONAL DYNAMICS OF TRYPSIN | ||||||
![]() | BETA-TRYPSIN | ||||||
![]() | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | NEUTRON DIFFRACTION / Resolution: 1.8 Å | ||||||
![]() | Kossiakoff, A.A. | ||||||
![]() | ![]() Title: Use of the neutron diffraction--H/D exchange technique to determine the conformational dynamics of trypsin Authors: Kossiakoff, A.A. #1: ![]() Title: Protein Dynamics Investigated by the Neutron Diffraction-Hydrogen Exchange Technique Authors: Kossiakoff, A.A. #2: ![]() Title: Direct Determination of the Protonation States of Aspartic Acid-102 and Histidine-57 in the Tetrahedral Intermediate of the Serine Proteases. Neutron Structure of Trypsin Authors: Kossiakoff, A.A. / Spencer, S.A. #3: ![]() Title: Neutron Diffraction Identifies His 57 as the Catalytic Base in Trypsin Authors: Kossiakoff, A.A. / Spencer, S.A. #4: ![]() Title: The Accuracy of Refined Protein Structures, Comparison of Two Independently Refined Models of Bovine Trypsin Authors: Chambers, J.L. / Stroud, R.M. #5: ![]() Title: Difference-Fourier Refinement of the Structure of Dip-Trypsin at 1.5 Angstroms Using a Minicomputer Technique Authors: Chambers, J.L. / Stroud, R.M. #6: ![]() Title: Structure-Function Relationships in the Serine Proteases Authors: Stroud, R.M. / Krieger, M. / Koeppeii, R.E. / Kossiakoff, A.A. / Chambers, J.L. #7: ![]() Title: Silver Ion Inhibition of Serine Proteases, Crystallographic Study of Silver-Trypsin Authors: Chambers, J.L. / Christoph, G.G. / Krieger, M. / Kay, L. / Stroud, R.M. #8: ![]() Title: The Structure of Bovine Trypsin,Electron Density Maps of the Inhibited Enzyme at 5 Angstroms and at 2.7 Angstroms Resolution Authors: Stroud, R.M. / Kay, L.M. / Dickerson, R.E. #9: ![]() Title: Structure and Specific Binding of Trypsin, Comparison of Inhibited Derivatives and a Model for Substrate Binding Authors: Krieger, M. / Kay, L.M. / Stroud, R.M. #10: ![]() Title: The Crystal and Molecular Structure of Dip-Inhibited Bovine Trypsin at 2.7 Angstroms Resolution Authors: Stroud, R.M. / Kay, L.M. / Dickerson, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.3 KB | Display | ![]() |
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PDB format | ![]() | 65.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367.8 KB | Display | ![]() |
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Full document | ![]() | 377.2 KB | Display | |
Data in XML | ![]() | 7.4 KB | Display | |
Data in CIF | ![]() | 10.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. 2: AN OCCUPANCY OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP. |
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Components
#1: Protein | Mass: 23327.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-ISP / |
Nonpolymer details | THE ENZYME IS INHIBITED BY A MONOISOPROPYLPHOSPHORYL DERIVATIVE. THE REFINED STRUCTURE IN THIS ...THE ENZYME IS INHIBITED BY A MONOISOPRO |
-Experimental details
-Experiment
Experiment | Method: NEUTRON DIFFRACTION |
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-Data collection
Radiation | Scattering type: neutron |
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Radiation wavelength | Relative weight: 1 |
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Processing
Refinement | Rfactor Rwork: 0.187 / Highest resolution: 1.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
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Refine LS restraints |
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