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- PDB-5fp2: Crystal structure of the siderophore receptor PirA from Pseudomon... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5fp2 | ||||||
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Title | Crystal structure of the siderophore receptor PirA from Pseudomonas aeruginosa | ||||||
![]() | (FERRIC ENTEROBACTIN RECEPTOR PIRA) x 2 | ||||||
![]() | METAL TRANSPORT / TONB-DEPENDENT RECEPTOR / SIDEROPHORE RECEPTOR / OUTER-MEMBRANE PROTEIN | ||||||
Function / homology | ![]() : / enterobactin transmembrane transporter activity / enterobactin transport / siderophore transmembrane transport / : / siderophore transport / siderophore uptake transmembrane transporter activity / signaling receptor activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Moynie, L. / Tortajada, A. / Naismith, J.H. | ||||||
![]() | ![]() Title: Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii. Authors: Moynie, L. / Luscher, A. / Rolo, D. / Pletzer, D. / Tortajada, A. / Weingart, H. / Braun, Y. / Page, M.G. / Naismith, J.H. / Kohler, T. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 22-STRANDED BARREL THIS IS REPRESENTED BY A 23-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 22-STRANDED BARREL THIS IS REPRESENTED BY A 23-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 422.6 KB | Display | ![]() |
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PDB format | ![]() | 352.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 484.3 KB | Display | ![]() |
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Full document | ![]() | 522.9 KB | Display | |
Data in XML | ![]() | 38.7 KB | Display | |
Data in CIF | ![]() | 52.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5fokC ![]() 5fp1C ![]() 5fr8C ![]() 1fepS C: citing same article ( S: Starting model for refinement |
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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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.6931, -0.3621, 0.6233), Vector: |
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Components
#1: Protein | Mass: 79460.445 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 869.063 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: PEPTIDE THOUGHT PART OF THE MAIN PROTEIN CHAIN BUT CANNOT BE CONFIRMED. Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57 % / Description: NONE |
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Crystal grow | pH: 7 / Details: 17% PEG 3350, 0.2 M MGCL2, 0.1 M TRIS PH 7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 13, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97625 Å / Relative weight: 1 |
Reflection | Resolution: 2.97→52.49 Å / Num. obs: 36861 / % possible obs: 98.8 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 11 |
Reflection shell | Resolution: 2.97→3.05 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 1.8 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FEP Resolution: 2.97→52.49 Å / Cor.coef. Fo:Fc: 0.896 / Cor.coef. Fo:Fc free: 0.853 / SU B: 59.586 / SU ML: 0.479 / Cross valid method: THROUGHOUT / ESU R: 1.508 / ESU R Free: 0.467 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 126.995 Å2
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Refinement step | Cycle: LAST / Resolution: 2.97→52.49 Å
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Refine LS restraints |
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