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- PDB-2tec: MOLECULAR DYNAMICS REFINEMENT OF A THERMITASE-EGLIN-C COMPLEX AT ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2tec | ||||||
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Title | MOLECULAR DYNAMICS REFINEMENT OF A THERMITASE-EGLIN-C COMPLEX AT 1.98 ANGSTROMS RESOLUTION AND COMPARISON OF TWO CRYSTAL FORMS THAT DIFFER IN CALCIUM CONTENT | ||||||
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![]() | COMPLEX(SERINE PROTEINASE-INHIBITOR) | ||||||
Function / homology | ![]() thermitase / serine-type endopeptidase inhibitor activity / response to wounding / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Gros, P. / Betzel, C. / Dauter, Z. / Wilson, K.S. / Hol, W.G.J. | ||||||
![]() | ![]() Title: Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 A resolution and comparison of two crystal forms that differ in calcium content. Authors: Gros, P. / Betzel, C. / Dauter, Z. / Wilson, K.S. / Hol, W.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.1 KB | Display | ![]() |
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PDB format | ![]() | 54.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 381.6 KB | Display | ![]() |
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Full document | ![]() | 391.4 KB | Display | |
Data in XML | ![]() | 9.3 KB | Display | |
Data in CIF | ![]() | 14.8 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: RESIDUE PRO E 172 IS A CIS PROLINE. 2: THE BOND PRO E 214 - THR E 215 IS IN THE CIS CONFORMATION. |
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Components
#1: Protein | Mass: 28384.896 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
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#2: Protein | Mass: 8100.011 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | THERMITASE RESIDUE 199 IS A VALINE ACCORDING TO AMINO ACID SEQUENCE DETERMINATION BY MELOUN ET AL. ...THERMITASE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.69 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 19-21 ℃ / pH: 5.2 / Method: vapor diffusion, hanging drop / Details: half of the reservoirs contained 0.5 M NaCl | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 3.5 Å / Num. obs: 26664 / % possible obs: 93 % / Observed criterion σ(I): 3 / Rmerge(I) obs: 0.072 / Num. measured all: 94298 |
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Processing
Software | Name: GROMOS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor Rwork: 0.165 / Highest resolution: 1.98 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.98 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.98 Å / Rfactor obs: 0.165 / Lowest resolution: 8 Å / Num. reflection obs: 19730 / σ(F): 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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