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Yorodumi- PDB-1o7t: Metal nanoclusters bound to the Ferric Binding Protein from Neiss... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1o7t | ||||||
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Title | Metal nanoclusters bound to the Ferric Binding Protein from Neisseria gonorrhoeae. | ||||||
Components | IRON BINDING PROTEINIron-binding proteins | ||||||
Keywords | METAL BINDING PROTEIN / METAL-BINDING PROTEIN / PERIPLASMIC FERRIC BINDING PROTEIN / HAFNIUM / METAL-OXO CLUSTER | ||||||
Function / homology | Function and homology information | ||||||
Biological species | NEISSERIA GONORRHOEAE (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Alexeev, D. / Zu, H. / Guo, M. / Zhong, W. / Hunter, D.J.B. / Yang, W. / Campopiano, D.J. / Sadler, P.J. | ||||||
Citation | Journal: Nat. Struct. Biol. / Year: 2003 Title: A novel protein-mineral interface. Authors: Alexeev, D. / Zhu, H. / Guo, M. / Zhong, W. / Hunter, D.J. / Yang, W. / Campopiano, D.J. / Sadler, P.J. | ||||||
History |
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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 | 1o7t.cif.gz | 572 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1o7t.ent.gz | 470.5 KB | Display | PDB format |
PDBx/mmJSON format | 1o7t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o7/1o7t ftp://data.pdbj.org/pub/pdb/validation_reports/o7/1o7t | HTTPS FTP |
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-Related structure data
Related structure data | 1d9yS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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5 |
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6 |
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7 |
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8 |
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9 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 33674.320 Da / Num. of mol.: 9 Source method: isolated from a genetically manipulated source Source: (gene. exp.) NEISSERIA GONORRHOEAE (bacteria) / Strain: FBPA / Plasmid: PTRC99A/FBP/NG / Production host: ESCHERICHIA COLI (E. coli) / Variant (production host): TOP10 / References: UniProt: Q50964 #2: Chemical | ChemComp-HF5 / #3: Chemical | ChemComp-HF3 / | #4: Chemical | #5: Water | ChemComp-HOH / | Nonpolymer details | HF5 - HFC LINKED TO OH OF TYR195 HF5 - HFA LINKED TO OH OF TYR196 HF3 - HFC LINKED TO OH OF TYR195 ...HF5 - HFC LINKED TO OH OF TYR195 HF5 - HFA LINKED TO OH OF TYR196 HF3 - HFC LINKED TO OH OF TYR195 HF3 - HFA LINKED TO OH OF TYR196 PHOSPHATE BRIDGES HFA-HFB-HFC PHF - HFC LINKED TO OH OF TYR195 PHF - HFA LINKED TO OH OF TYR196 PHOSPHATE BRIDGES HFA-HFD-HFE | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.1 % | ||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 4MG/ML PROTEIN IN 4MM PHOSPHATE, 25MM NAHCO3 PLUS 20% PEG 4000, 0.2M KCL, 0.4M IMIDAZOLE/MALATE BUFFER PH7.7, pH 7.40 | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 290 K / pH: 7.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 15, 2001 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. obs: 406392 / % possible obs: 100 % / Redundancy: 8.4 % / Biso Wilson estimate: 28.5 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 1.6→1.63 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.584 / Mean I/σ(I) obs: 1.8 / % possible all: 100 |
Reflection | *PLUS Lowest resolution: 30 Å / % possible obs: 100 % / Rmerge(I) obs: 0.08 |
Reflection shell | *PLUS % possible obs: 100 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1D9Y Resolution: 1.65→30 Å / Data cutoff high absF: 100000 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT / Bsol: 54 Å2 / ksol: 0.34 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.2 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→30 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 30 Å / % reflection Rfree: 7 % / Rfactor Rfree: 0.264 / Rfactor Rwork: 0.165 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.24 |