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Yorodumi- PDB-2uz5: Solution structure of the fkbp-domain of Legionella pneumophila Mip -
+Open data
-Basic information
Entry | Database: PDB / ID: 2uz5 | ||||||
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Title | Solution structure of the fkbp-domain of Legionella pneumophila Mip | ||||||
Components | MACROPHAGE INFECTIVITY POTENTIATOR | ||||||
Keywords | ISOMERASE / FKBP / LEGIONELLA PNEUMOPHILA / PPIASE / LEGIONNAIRES DISEASE | ||||||
Function / homology | Function and homology information peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / cell outer membrane / protein folding Similarity search - Function | ||||||
Biological species | LEGIONELLA PNEUMOPHILA (bacteria) | ||||||
Method | SOLUTION NMR / ARIA | ||||||
Authors | Ceymann, A. / Horstmann, M. / Ehses, P. / Schweimer, K. / Steinert, M. / Kamphausen, T. / Fischer, G. / Hacker, J. / Rosch, P. / Faber, C. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Domain Motions of the Mip Protein from Legionella Pneumophila Authors: Horstmann, M. / Ehses, P. / Schweimer, K. / Steinert, M. / Kamphausen, T. / Fischer, G. / Hacker, J. / Rosch, P. / Faber, C. #1: Journal: J.Biomol.NMR / Year: 2005 Title: 1H, 13C, 15N Backbone and Sidechain Resonance Assignment of Mip(77-213) the Ppiase Domain of the Legionella Pneumophila Mip Protein Authors: Horstmann, M. / Kamphausen, T. / Schweimer, K. / Steinert, M. / Hacker, J. / Haase, A. / Rosch, P. / Schweimer, G. / Faber, C. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2uz5.cif.gz | 448.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2uz5.ent.gz | 378.9 KB | Display | PDB format |
PDBx/mmJSON format | 2uz5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/2uz5 ftp://data.pdbj.org/pub/pdb/validation_reports/uz/2uz5 | HTTPS FTP |
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-Related structure data
Similar structure data |
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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: 14667.702 Da / Num. of mol.: 1 / Fragment: FKBP DOMAIN, RESIDUES 97-233 / Source method: isolated from a natural source / Details: SURFACE EXPOSED PROTEIN / Source: (natural) LEGIONELLA PNEUMOPHILA (bacteria) References: UniProt: Q933L8, UniProt: Q5ZXE0*PLUS, peptidylprolyl isomerase |
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Sequence details | ONLY RESIDUES 97-233 INCLUDED |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: VARIOUS |
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED MIP AND UNLABELLED RAPAMYCIN. THE STRUCTURES ARE SORTED BY ENERGY |
-Sample preparation
Details | Contents: 90% WATER/10% D2O |
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Sample conditions | pH: 6.5 / Temperature: 298.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker AM / Manufacturer: Bruker / Model: AM / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: ARIA / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY / Conformers calculated total number: 40 / Conformers submitted total number: 10 |