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- PDB-1yub: SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONF... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yub | ||||||
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Title | SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
![]() | RRNA METHYLTRANSFERASE | ||||||
![]() | METHYLTRANSFERASE / ERM / ERMAM / MLS ANTIBIOTICS / RRNA | ||||||
Function / homology | ![]() 23S rRNA (adenine2085-N6)-dimethyltransferase / 23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity / rRNA (adenine-N6,N6-)-dimethyltransferase activity / response to antibiotic / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / DG, SA | ||||||
![]() | Yu, L. / Petros, A.M. / Schnuchel, A. / Zhong, P. / Severin, J.M. / Walter, K. / Holzman, T.F. / Fesik, S.W. | ||||||
![]() | ![]() Title: Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Authors: Yu, L. / Petros, A.M. / Schnuchel, A. / Zhong, P. / Severin, J.M. / Walter, K. / Holzman, T.F. / Fesik, S.W. #1: ![]() Title: Erratum. Solution Structure of an Rrna Methyltransferase (Ermam) that Confers Macrolide-Lincosamide-Streptogramin Antibiotic Resistance Authors: Yu, L. / Petros, A.M. / Schnuchel, A. / Zhong, P. / Severin, J.M. / Walter, K. / Holzman, T.F. / Fesik, S.W. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 102.5 KB | Display | ![]() |
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PDB format | ![]() | 80.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 248.9 KB | Display | ![]() |
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Full document | ![]() | 248.6 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 14.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 28862.568 Da / Num. of mol.: 1 / Mutation: I75T, S100N, H118R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 5728, A CLINICAL ISOLATE FROM ABBOTT CULTURE COLLECTION Cell line: BL21 / Gene: ERM / Plasmid: PET-24(+) / Species (production host): Escherichia coli / Gene (production host): ERM / 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
Sample conditions | Ionic strength: 50 mM SODIUM PHOSPHATE, 100 mM NACL / pH: 6.5 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
Software |
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NMR software |
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Refinement | Method: DG, SA / Software ordinal: 1 Details: THE TOTAL NUMBER OF DISTANCE RESTRAINTS USED WAS 3259. THE TOTAL NUMBER OF TORSIONAL RESTRAINTS USED WAS 63. | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY AND LEAST RESTRAINT VIOLATION Conformers calculated total number: 17 / Conformers submitted total number: 1 |