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- PDB-6qbz: Solution structure of the N-terminal domain of the Staphylococcus... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6qbz | ||||||
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Title | Solution structure of the N-terminal domain of the Staphylococcus aureus Hibernation Promoting Factor | ||||||
![]() | Ribosome hibernation promoting factor | ||||||
![]() | RIBOSOMAL PROTEIN / Hibernation promoting factor / Staphylococcus aureus / 100S ribosome | ||||||
Function / homology | ![]() negative regulation of translational elongation / ribosomal small subunit binding / cytosolic small ribosomal subunit Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Usachev, K.S. / Validov, S.Z. / Khusainov, I.S. / Klochkov, V.V. / Aganov, A.V. / Yusupov, M.M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Solution structure of the N-terminal domain of the Staphylococcus aureus hibernation promoting factor. Authors: Usachev, K.S. / Validov, S.Z. / Khusainov, I.S. / Varfolomeev, A.A. / Klochkov, V.V. / Aganov, A.V. / Yusupov, M.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 361.8 KB | Display | ![]() |
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PDB format | ![]() | 300.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 406.6 KB | Display | ![]() |
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Full document | ![]() | 480.1 KB | Display | |
Data in XML | ![]() | 23.6 KB | Display | |
Data in CIF | ![]() | 37.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 12930.717 Da / Num. of mol.: 1 / Fragment: N-terminal domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: hpf, raiA, BN1321_170086, BTN44_08780, C0J46_03720, C7Q89_05535, CSC83_13900, CSC87_08515, CV021_09125, EP54_02760, EQ90_03750, ERS072840_01629, HMPREF3211_01097, NCTC10654_00858, NCTC11940_ ...Gene: hpf, raiA, BN1321_170086, BTN44_08780, C0J46_03720, C7Q89_05535, CSC83_13900, CSC87_08515, CV021_09125, EP54_02760, EQ90_03750, ERS072840_01629, HMPREF3211_01097, NCTC10654_00858, NCTC11940_00726, NCTC13131_00825, NCTC13196_00432, NCTC13812_00784, NCTC6133_00902, NCTC7878_03405, NCTC9944_00832, RK64_04495, SAMEA1466939_00154, SAMEA1469870_00863, SAMEA1531701_00565, SAMEA1708664_00330, SAMEA1708674_00592 Plasmid: pGS21A / 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 |
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Sample |
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Sample conditions | Details: PBS buffer (90%H2O+10%D2O) at pH 7.6 with 200 mM NH4Cl concentration Ionic strength: 200 mM / Label: conditions_1 / pH: 7.6 / Pressure: 1 atm / Temperature: 308 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 700 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 2 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 10 |