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- PDB-1sib: REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WIL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1sib | ||||||
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Title | REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES | ||||||
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![]() | SERINE PROTEASE/INHIBITOR COMPLEX / SERINE PROTEASE-INHIBITOR COMPLEX / SERINE PROTEASE-INHIBITOR COMPLEX complex | ||||||
Function / homology | ![]() subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase inhibitor activity / response to wounding / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Gruetter, M.G. / Heinz, D.W. / Priestle, J.P. | ||||||
![]() | ![]() Title: Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes. Authors: Heinz, D.W. / Priestle, J.P. / Rahuel, J. / Wilson, K.S. / Grutter, M.G. #1: ![]() Title: Refined 1.2 Angstroms Crystal Structure of the Complex Formed between Subtilisin Carlsberg and the Inhibitor Eglin C. Molecular Structure of Eglin and its Detailed Interaction with Subtilisin Authors: Bode, W. / Papamokos, E. / Musil, D. / Seemueller, U. / Fritz, H. #2: ![]() Title: Crystal and Molecular Structure of the Inhibitor Eglin from Leeches in Complex with Subtilisin Carlsberg Authors: Mcphalen, C.A. / Schnebli, H.P. / James, M.N.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 | ![]() | 81.1 KB | Display | ![]() |
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PDB format | ![]() | 60.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.3 KB | Display | ![]() |
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Full document | ![]() | 408.1 KB | Display | |
Data in XML | ![]() | 12.7 KB | Display | |
Data in CIF | ![]() | 18.8 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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Unit cell |
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Atom site foot note | 1: RESIDUE PRO E 168 IS A CIS PROLINE. |
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Components
#1: Protein | Mass: 27552.525 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||
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#2: Protein | Mass: 8071.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.7 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 24538 / Rmerge(I) obs: 0.097 / Num. measured all: 74306 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.4→5 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.4→5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 5 Å / Num. reflection obs: 11195 / σ(F): 0 / Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |