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- PDB-1u7m: Solution structure of a diiron protein model: Due Ferri(II) turn ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1u7m | ||||||
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Title | Solution structure of a diiron protein model: Due Ferri(II) turn mutant | ||||||
![]() | Four-helix bundle model | ||||||
![]() | DE NOVO PROTEIN / Diiron proteins / four-helix bundle / protein design / inter-helical loops | ||||||
Function / homology | Immunoglobulin FC, subunit C / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / Torsion Angle Dynamics, Simulated Annealing, Energy Restrained Minimization | ||||||
![]() | Maglio, O. / Nastri, F. / Calhoun, J.R. / Lahr, S. / Pavone, V. / DeGrado, W.F. / Lombardi, A. | ||||||
![]() | ![]() Title: Analysis and Design of Turns in alpha-Helical Hairpins Authors: Lahr, S.J. / Engel, D.E. / Stayrook, S.E. / Maglio, O. / North, B. / Geremia, S. / Lombardi, A. / Degrado, W.F. #1: ![]() Title: Solution characterization of diiron proteins containing two distinct types of inter-helical loops Authors: Maglio, O. / Nastri, F. / Calhoun, J.R. / Lahr, S. / Pavone, V. / DeGrado, W.F. / Lombardi, A. #2: Journal: Protein Sci. / Year: 2001 Title: Proton and metal ion-dependent assembly of a model diiron protein Authors: Pasternak, A. / Kaplan, J. / Lear, J.D. / DeGrado, W.F. #3: ![]() Title: Inaugural article: retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins Authors: Lombardi, A. / Summa, C.M. / Geremia, S. / Randaccio, L. / Pavone, V. / DeGrado, W.F. #4: ![]() Title: Preorganization of molecular binding sites in designed diiron proteins Authors: Maglio, O. / Nastri, F. / Pavone, V. / Lombardi, A. / DeGrado, W.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 714.3 KB | Display | ![]() |
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PDB format | ![]() | 598.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 369.1 KB | Display | ![]() |
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Full document | ![]() | 589.9 KB | Display | |
Data in XML | ![]() | 32.1 KB | Display | |
Data in CIF | ![]() | 56.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 6477.396 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear technique |
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Sample preparation
Details | Contents: 0.5mM protein concentration; 50mM phosphate buffer; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50mm phosphate buffer / pH: 6.1 / Pressure: Ambient / 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 | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: Torsion Angle Dynamics, Simulated Annealing, Energy Restrained Minimization Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 20 |