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Yorodumi- PDB-1txe: Solution structure of the active-centre mutant Ile14Ala of the hi... -
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-Basic information
Entry | Database: PDB / ID: 1txe | ||||||
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Title | Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus | ||||||
Components | Phosphocarrier protein HPr | ||||||
Keywords | TRANSPORT PROTEIN / open-faced beta-sandwich / Structural Proteomics in Europe / SPINE / Structural Genomics | ||||||
Function / homology | Function and homology information phosphoenolpyruvate-dependent sugar phosphotransferase system / cytoplasm Similarity search - Function | ||||||
Biological species | Staphylococcus carnosus (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Moeglich, A. / Koch, B. / Hengstenberg, W. / Brunner, E. / Kalbitzer, H.R. / Structural Proteomics in Europe (SPINE) | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 2004 Title: Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus Authors: Moeglich, A. / Koch, B. / Gronwald, W. / Hengstenberg, W. / Brunner, E. / Kalbitzer, H.R. #1: Journal: Protein Sci. / Year: 2000 Title: 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure Authors: Kalbitzer, H.R. / Goerler, A. / Li, H. / Dubovskii, P.V. / Hengstenberg, W. / Kowolik, C. / Yamada, H. / Akasaka, K. #2: Journal: APPL.MAGN.RESON. / Year: 1999 Title: Solution Structure of the Histidine-Containing Phosphocarrier Protein from Staphylococcus carnosus Authors: Goerler, A. / Hengstenberg, W. / Kravanja, M. / Beneicke, W. / Maurer, T. / Kalbitzer, H.R. #3: Journal: J.Am.Chem.Soc. / Year: 2003 Title: NMR-spectroscopic mapping of an engineered cavity in the I14A mutant of HPr from Staphylococcus carnosus using xenon Authors: Groeger, C. / Moeglich, A. / Pons, M. / Koch, B. / Hengstenberg, W. / Kalbitzer, H.R. / Brunner, E. #4: Journal: Proteins / Year: 2004 Title: DRESS: a database of REfined solution NMR structures Authors: Nabuurs, S.B. / Nederveen, A.J. / Vranken, W. / Doreleijers, J.F. / Bonvin, A.M.J.J. / Vuister, G.W. / Vriend, G. / Spronk, C.A.E.M. #5: Journal: Proteins / Year: 2003 Title: Refinement of protein structures in explicit solvent Authors: Linge, J.P. / Williams, M.A. / Spronk, C.A.E.M. / Bonvin, A.M.J.J. / Nilges, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1txe.cif.gz | 260.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1txe.ent.gz | 216.2 KB | Display | PDB format |
PDBx/mmJSON format | 1txe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1txe_validation.pdf.gz | 337.6 KB | Display | wwPDB validaton report |
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Full document | 1txe_full_validation.pdf.gz | 392.8 KB | Display | |
Data in XML | 1txe_validation.xml.gz | 15.1 KB | Display | |
Data in CIF | 1txe_validation.cif.gz | 25.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tx/1txe ftp://data.pdbj.org/pub/pdb/validation_reports/tx/1txe | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9476.568 Da / Num. of mol.: 1 / Mutation: I14A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus carnosus (bacteria) / Plasmid: pET11 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P23534 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Residual dipolar couplings for the amide bond (HN-N) as well as between the atoms HA and HN have also been used as restraints for structure determination. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0.12 / pH: 7.14 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: TOTAL NUMBER OF NOES USED FOR THE CALCULATION: 1268, NUMBER OF INTRA-RESIDUE NOES USED FOR THE CALCULATION: 637, NUMBER OF SHORT RANGE NOES (I,J, I < J < I+5) USED FOR THE CALCULATION: 365, ...Details: TOTAL NUMBER OF NOES USED FOR THE CALCULATION: 1268, NUMBER OF INTRA-RESIDUE NOES USED FOR THE CALCULATION: 637, NUMBER OF SHORT RANGE NOES (I,J, I < J < I+5) USED FOR THE CALCULATION: 365, NUMBER OF LONG RANGE (I,J, J > I+4) NOES USED FOR THE CALCULATION: 266, NUMBER OF DIHEDRAL ANGLES RESTRAINTS USED FOR THE CALCULATION: 44, NUMBER OF HYDROGEN BOND RESTRAINTS USED FOR THE CALCULATION: 20, NUMBER OF 1HN/15NH RESIDUAL DIPOLAR COUPLINGS USED FOR THE CALCULATION: 49, NUMBER OF 1HN/1HA RESIDUAL DIPOLAR COUPLINGS USED FOR THE CALCULATION: 25 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 300 / Conformers submitted total number: 10 |