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- PDB-6wa1: Dimeric form of the trans-stabilized Hemolysin II C-terminal domain -
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Open data
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Basic information
Entry | Database: PDB / ID: 6wa1 | ||||||
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Title | Dimeric form of the trans-stabilized Hemolysin II C-terminal domain | ||||||
![]() | Hemolysin II | ||||||
![]() | TOXIN / domain swapped dimer | ||||||
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 / simulated annealing | ||||||
![]() | Kaplan, A.R. / Alexandrescu, A.T. | ||||||
![]() | ![]() Title: Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states. Authors: Kaplan, A.R. / Olson, R. / Alexandrescu, A.T. #1: ![]() Title: NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold. Authors: Kaplan, A.R. / Kaus, K. / De, S. / Olson, R. / Alexandrescu, A.T. #2: Journal: Biomol.Nmr Assign. / Year: 2014 Title: NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain. Authors: Kaplan, A.R. / Maciejewski, M.W. / Olson, R. / Alexandrescu, A.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 | ![]() | 1.4 MB | Display | ![]() |
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PDB format | ![]() | 1.2 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 578 KB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 363.7 KB | Display | |
Data in CIF | ![]() | 340.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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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: 10461.706 Da / Num. of mol.: 2 / Fragment: C-terminal domain (UNP residues 319-412) / Mutation: P87M 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: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 0.8 mM [U-99% 13C; U-99% 15N] HlyIIC, 20 mM sodium phosphate, 1 mM EDTA, 0.05 % w/v sodium azide, 1 mM AEBSF protease inhibitor, 90% H2O/10% D2O Label: 13C_15N_P87M / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 M / Label: 13C_15N_P87M / pH: 6.5 / Pressure: 1 atm / Temperature: 303.15 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 8 | ||||||||||||||||||||||||||||||||||||
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 |