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Open data
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Basic information
Entry | Database: PDB / ID: 6d5z | ||||||
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Title | Cis form of Hemolysin II C-terminal domain | ||||||
![]() | Hemolysin II | ||||||
![]() | TOXIN / pore-forming toxin / proline isomerization / conformational heterogeneity | ||||||
Function / homology | Bi-component toxin, staphylococci / Leukocidin/Hemolysin toxin / Leukocidin/Hemolysin toxin family / Leukocidin/porin MspA superfamily / cytolysis in another organism / extracellular region / Hemolysin II![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Kaplan, A.R. / Alexandrescu, A.T. / Olson, R. | ||||||
![]() | ![]() Title: Trans form of HemolysinII c-terminal domain Authors: Kaplan, A.R. / Alexandrescu, A.T. / Olson, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 703.3 KB | Display | ![]() |
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PDB format | ![]() | 588.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 403.6 KB | Display | ![]() |
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Full document | ![]() | 591.9 KB | Display | |
Data in XML | ![]() | 55.4 KB | Display | |
Data in CIF | ![]() | 86.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6d53C C: citing same article ( |
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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: 10841.098 Da / Num. of mol.: 1 / Fragment: residues 319-412 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711 Gene: BC_3523 / Plasmid: pET28b Production host: ![]() ![]() Strain (production host): BL21-Gold(DE3)pLysS AG / References: UniProt: Q81AN8 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 0 M / Label: 1 / pH: 6.0 / Pressure: 1 atm / Temperature: 310 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: molecular dynamics / Software ordinal: 5 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 25 |