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Open data
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Basic information
Entry | Database: PDB / ID: 2kid | |||||||||
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Title | Solution Structure of the S. Aureus Sortase A-substrate Complex | |||||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / SORTASE / EIGHT STRANDED BETA BARREL / TRANSPEPTIDASE / ENZYME-SUBSTRATE COMPLEX / HYDROLASE-HYDROLASE INHIBITOR complex | |||||||||
Function / homology | ![]() calcium-dependent cysteine-type endopeptidase activity / peptide binding / manganese ion binding / calcium ion binding / magnesium ion binding / proteolysis Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Model details | lowest energy, model 1 | |||||||||
![]() | Suree, N. / Liew, C.K. / Villareal, V.A. / Thieu, W. / Fadeev, E.A. / Clemens, J.J. / Jung, M.E. / Clubb, R.T. | |||||||||
![]() | ![]() Title: The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized. Authors: Suree, N. / Liew, C.K. / Villareal, V.A. / Thieu, W. / Fadeev, E.A. / Clemens, J.J. / Jung, M.E. / Clubb, R.T. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 954.1 KB | Display | ![]() |
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PDB format | ![]() | 790.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.3 KB | Display | ![]() |
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Full document | ![]() | 701.9 KB | Display | |
Data in XML | ![]() | 91.6 KB | Display | |
Data in CIF | ![]() | 116.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Similar structure data | |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 16753.000 Da / Num. of mol.: 1 / Fragment: Residues 62-206 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | ( |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 6 / Pressure: AMBIENT / Temperature: 302 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: SOFTWARE USED: PIPP, NMRPIPE, ATNOS/CANDID, REFINEMENT: Residual Dipolar Couplings (RDC) | |||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2454 / Protein chi angle constraints total count: 127 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry Conformers calculated total number: 400 / Conformers submitted total number: 20 |