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Yorodumi- PDB-7lrr: Co-bound crystal structure of the engineered cyt cb562 variant, D... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7lrr | |||||||||
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Title | Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in the presence of Cu(II) (M1) and Co(II) (M2) | |||||||||
Components | Soluble cytochrome b562 | |||||||||
Keywords | METAL BINDING PROTEIN / Metal selectivity / Irving-Williams series | |||||||||
Function / homology | Function and homology information electron transport chain / periplasmic space / electron transfer activity / iron ion binding / heme binding Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.89 Å | |||||||||
Authors | Choi, T.S. / Tezcan, F.A. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Nature / Year: 2022 Title: Overcoming universal restrictions on metal selectivity by protein design. Authors: Choi, T.S. / Tezcan, F.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7lrr.cif.gz | 71.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7lrr.ent.gz | 44.8 KB | Display | PDB format |
PDBx/mmJSON format | 7lrr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7lrr_validation.pdf.gz | 2 MB | Display | wwPDB validaton report |
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Full document | 7lrr_full_validation.pdf.gz | 2 MB | Display | |
Data in XML | 7lrr_validation.xml.gz | 12.8 KB | Display | |
Data in CIF | 7lrr_validation.cif.gz | 17.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lr/7lrr ftp://data.pdbj.org/pub/pdb/validation_reports/lr/7lrr | HTTPS FTP |
-Related structure data
Related structure data | 7lr5C 7lraC 7lrbC 7lrvC 7lv1C 7mk4C 7n4fC 7n4gC 2bc5S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 11915.375 Da / Num. of mol.: 2 / Mutation: D60H, I67H, Q71H, T96C, T97H, A100H, K104H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: cybC / Production host: Escherichia coli (E. coli) / References: UniProt: P0ABE7 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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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: 2.24 Å3/Da / Density % sol: 45.19 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: PEG1500 25%, NaCl 200 mM, pH 8 EPPS 100 mM |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 1.59 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 4, 2020 |
Radiation | Monochromator: Si(111) and Si(220) double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.59 Å / Relative weight: 1 |
Reflection | Resolution: 1.89→44.27 Å / Num. obs: 17578 / % possible obs: 98.54 % / Redundancy: 30.2 % / Biso Wilson estimate: 16.99 Å2 / CC1/2: 0.883 / CC star: 0.969 / Rmerge(I) obs: 0.8529 / Rpim(I) all: 0.156 / Rrim(I) all: 0.8678 / Net I/σ(I): 14.77 |
Reflection shell | Resolution: 1.89→1.958 Å / Redundancy: 19.4 % / Rmerge(I) obs: 0.9726 / Mean I/σ(I) obs: 3.3 / Num. unique obs: 1611 / CC1/2: 0.417 / CC star: 0.767 / Rpim(I) all: 0.156 / Rrim(I) all: 0.8678 / % possible all: 92.48 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2bc5 Resolution: 1.89→44.27 Å / SU ML: 0.2187 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 23.2246 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.43 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.89→44.27 Å
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Refine LS restraints |
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LS refinement shell |
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