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- PDB-1tie: CRYSTAL STRUCTURE OF A KUNITZ-TYPE TRYPSIN INHIBITOR FROM ERYTHRI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tie | ||||||
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Title | CRYSTAL STRUCTURE OF A KUNITZ-TYPE TRYPSIN INHIBITOR FROM ERYTHRINA CAFFRA SEEDS | ||||||
![]() | ERYTHRINA TRYPSIN INHIBITOR | ||||||
![]() | PROTEINASE INHIBITOR (TRYPSIN) | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Onesti, S. / Brick, P. / Blow, D.M. | ||||||
![]() | ![]() Title: Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. Authors: Onesti, S. / Brick, P. / Blow, D.M. #1: ![]() Title: Crystallization and Preliminary Diffraction Studies of Erythrina Trypsin Inhibitor Authors: Onesti, S. / Lloyd, L.F. / Brick, P. / Blow, D.M. | ||||||
History |
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Remark 700 | SHEET ETI CONSISTS OF 12 ANTIPARALLEL BETA-STRANDS JOINED BY LONG LOOPS. SIX OF THE STRANDS FORM A ...SHEET ETI CONSISTS OF 12 ANTIPARALLEL BETA-STRANDS JOINED BY LONG LOOPS. SIX OF THE STRANDS FORM A SHORT BARREL WHICH IS CLOSED AT ONE END BY A "LID" CONSISTING OF THE OTHER SIX STRANDS COUPLED IN THREE PAIRS. THE MOLECULE SHOWS APPROXIMATE THREE-FOLD SYMMETRY ABOUT THE THE AXIS OF THE BARREL, WITH THE REPEATING UNIT CONSISTING OF FOUR SEQUENTIAL BETA-STRANDS AND THE CONNECTING LOOPS. THE SHEET PRESENTED AS *B1* ON SHEET RECORDS BELOW IS ACTUALLY THE SIX-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A SEVEN-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.9 KB | Display | ![]() |
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PDB format | ![]() | 31.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 407.1 KB | Display | ![]() |
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Full document | ![]() | 409.3 KB | Display | |
Data in XML | ![]() | 9.1 KB | Display | |
Data in CIF | ![]() | 11.9 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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Components
#1: Protein | Mass: 19296.578 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.29 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 3.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Num. obs: 7770 / % possible obs: 93.6 % / Num. measured all: 33533 / Rmerge(I) obs: 0.065 |
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Processing
Software | Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.5→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.208 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.64 Å / Total num. of bins used: 10 / Rfactor obs: 0.297 |