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Open data
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Basic information
Entry | Database: PDB / ID: 5i98 | ||||||
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Title | Structure of apo FKBP12(P104G) from C. albicans | ||||||
![]() | FK506-binding protein 1 | ||||||
![]() | ISOMERASE / FKBP12 / Self-catalysis | ||||||
Function / homology | ![]() regulation of homoserine biosynthetic process / fungal biofilm matrix / macrolide binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein folding / chromatin organization / extracellular region / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Schumacher, M.A. | ||||||
![]() | ![]() Title: Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function. Authors: Tonthat, N.K. / Juvvadi, P.R. / Zhang, H. / Lee, S.C. / Venters, R. / Spicer, L. / Steinbach, W.J. / Heitman, J. / Schumacher, M.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 99.3 KB | Display | ![]() |
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PDB format | ![]() | 77.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 431.5 KB | Display | ![]() |
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Full document | ![]() | 432.5 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 16.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ht1C ![]() 5htgC ![]() 5huaC ![]() 5hw6C ![]() 5hw7C ![]() 5hw8C ![]() 5hwbC ![]() 5hwcC ![]() 5j6eC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 12837.553 Da / Num. of mol.: 2 / Mutation: P104G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: SC5314 / ATCC MYA-2876 Gene: RBP1, RBP11, CaO19.11186, CaO19.3702, RBP2, RBP12, CaJ7.0299, CaO19.13810, CaO19.6452 Production host: Escherichia coli / References: UniProt: P28870, peptidylprolyl isomerase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.7 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 2 M Ammonium Sulfate 0.1 M CAPS/NaOH pH 10.5 0.2 M Lithium Sulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 3, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→50 Å / Num. obs: 15510 / % possible obs: 99 % / Redundancy: 3 % / Net I/σ(I): 20.5 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 112.66 Å2 / Biso mean: 42.14 Å2 / Biso min: 27.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.999→45.345 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 11
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