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Open data
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Basic information
Entry | Database: PDB / ID: 4axz | ||||||
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Title | Borrelia burgdorferi outer surface lipoprotein BBA73 | ||||||
![]() | PUTATIVE ANTIGEN P35 | ||||||
![]() | MEMBRANE PROTEIN / LIPID BINDING PROTEIN / OUTER SURFACE LIPOPROTEIN | ||||||
Function / homology | Bbcrasp-1 / Bbcrasp-1 / Borrelia lipoprotein paralogus family 54/60 / Borrelia Bbcrasp-1 domain containing protein / Orthogonal Bundle / Mainly Alpha / membrane / Antigen P35![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Brangulis, K. / Petrovskis, I. / Kazaks, A. / Ranka, R. / Baumanis, V. / Tars, K. | ||||||
![]() | ![]() Title: Structural Characterization of the Borrelia Burgdorferi Outer Surface Protein Bba73 Implicates Dimerization as a Functional Mechanism. Authors: Brangulis, K. / Petrovskis, I. / Kazaks, A. / Baumanis, V. / Tars, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 59.8 KB | Display | ![]() |
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PDB format | ![]() | 42.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426 KB | Display | ![]() |
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Full document | ![]() | 426.7 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 14.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4b2fC ![]() 4alyS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 31712.143 Da / Num. of mol.: 1 / Fragment: RESIDUES 28-296 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: B31 / Plasmid: PETM-11 / Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41 % / Description: NONE |
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Crystal grow | pH: 7 / Details: 0.1M HEPES, PH 7.0, 14% PEG 3350, 0.05M NAH2PO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 19, 2012 / Details: RH-COATED TOROIDAL SI MIRROR |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.08→40.13 Å / Num. obs: 15649 / % possible obs: 99.9 % / Observed criterion σ(I): 2.1 / Redundancy: 13.8 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.3 |
Reflection shell | Resolution: 2.09→2.2 Å / Redundancy: 12.2 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4ALY Resolution: 2.09→40.15 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.935 / SU B: 4.653 / SU ML: 0.127 / Cross valid method: THROUGHOUT / ESU R: 0.231 / ESU R Free: 0.185 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.051 Å2
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Refinement step | Cycle: LAST / Resolution: 2.09→40.15 Å
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Refine LS restraints |
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