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Yorodumi- PDB-2rui: Solution Structure of the Bacillus anthracis Sortase A-substrate ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2rui | |||||||||
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Title | Solution Structure of the Bacillus anthracis Sortase A-substrate Complex | |||||||||
Components |
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Keywords | HYDROLASE/HYDROLASE SUBSTRATE / Sortase / SrtA / Transpeptidase / HYDROLASE-HYDROLASE SUBSTRATE complex | |||||||||
Function / homology | Function and homology information cysteine-type peptidase activity / membrane => GO:0016020 / proteolysis / membrane Similarity search - Function | |||||||||
Biological species | Bacillus anthracis str. Sterne (bacteria) synthetic (others) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Model details | lowest energy, model1 | |||||||||
Authors | Chan, A.H. / Yi, S. / Jung, M.E. / Clubb, R.T. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2015 Title: Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS. Authors: Chan, A.H. / Yi, S.W. / Terwilliger, A.L. / Maresso, A.W. / Jung, M.E. / Clubb, R.T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rui.cif.gz | 971.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rui.ent.gz | 815.5 KB | Display | PDB format |
PDBx/mmJSON format | 2rui.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rui_validation.pdf.gz | 421.1 KB | Display | wwPDB validaton report |
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Full document | 2rui_full_validation.pdf.gz | 660.6 KB | Display | |
Data in XML | 2rui_validation.xml.gz | 79.8 KB | Display | |
Data in CIF | 2rui_validation.cif.gz | 100.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ru/2rui ftp://data.pdbj.org/pub/pdb/validation_reports/ru/2rui | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17110.387 Da / Num. of mol.: 1 / Fragment: UNP residues 57-210 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus anthracis str. Sterne (bacteria) Gene: BAS0654, srtA / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q6I399, UniProt: Q81V16*PLUS |
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#2: Protein/peptide | |
-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: 50 / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1861 / NOE intraresidue total count: 368 / NOE long range total count: 808 / NOE medium range total count: 235 / NOE sequential total count: 449 / Hydrogen bond constraints total count: 47 / Protein chi angle constraints total count: 24 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 150 / Protein psi angle constraints total count: 144 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.031 Å / Distance rms dev error: 0.002 Å |