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- PDB-2jiy: PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M149 REPLACED WITH... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2jiy | ||||||
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Title | PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M149 REPLACED WITH TRP (CHAIN M, AM149W) | ||||||
![]() | (REACTION CENTER PROTEIN ...) x 3 | ||||||
![]() | PHOTOSYNTHESIS / MEMBRANE PROTEIN / ELECTRON TRANSPORT / BACTERIOCHLOROPHYLL / CHLOROPHYLL / METAL-BINDING / TRANSPORT / CHROMOPHORE | ||||||
Function / homology | ![]() plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthetic electron transport in photosystem II / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fyfe, P.K. / Potter, J.A. / Cheng, J. / Williams, C.M. / Watson, A.J. / Jones, M.R. | ||||||
![]() | ![]() Title: Structural Responses to Cavity-Creating Mutations in an Integral Membrane Protein. Authors: Fyfe, P.K. / Potter, J.A. / Cheng, J. / Williams, C.M. / Watson, A.J. / Jones, M.R. #1: Journal: Photosyn. Res. / Year: 2005 Title: On the Role of Basic Residues in Adapting the Purple Bacterial Reaction Centre-Lh1 Photosystem for Growth at Elevated Temperature Authors: Watson, A.J. / Hughes, A.V. / Fyfe, P.K. / Wakeham, M.C. / Holden-Dye, K. / Heathcote, P. / Jones, M.R. #2: ![]() Title: Structural Details of an Interaction between Cardiolipin and an Integral Membrane Protein. Authors: Mcauley, K.E. / Fyfe, P.K. / Ridge, J.P. / Isaacs, N.W. / Cogdell, R.J. / Jones, M.R. | ||||||
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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 211.7 KB | Display | ![]() |
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PDB format | ![]() | 163.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.8 MB | Display | ![]() |
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Full document | ![]() | 2.9 MB | Display | |
Data in XML | ![]() | 41.1 KB | Display | |
Data in CIF | ![]() | 56.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-REACTION CENTER PROTEIN ... , 3 types, 3 molecules HLM
#1: Protein | Mass: 28066.322 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 31346.389 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Protein | Mass: 34644.867 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Non-polymers , 11 types, 398 molecules ![](data/chem/img/LDA.gif)
![](data/chem/img/BCL.gif)
![](data/chem/img/BPH.gif)
![](data/chem/img/U10.gif)
![](data/chem/img/CDL.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/SPN.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/D12.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/BCL.gif)
![](data/chem/img/BPH.gif)
![](data/chem/img/U10.gif)
![](data/chem/img/CDL.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/SPN.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/D12.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | #5: Chemical | ChemComp-BCL / #6: Chemical | ChemComp-BPH / | #7: Chemical | #8: Chemical | ChemComp-CDL / | #9: Chemical | ChemComp-FE / | #10: Chemical | ChemComp-PO4 / | #11: Chemical | ChemComp-SPN / | #12: Chemical | ChemComp-CL / | #13: Chemical | ChemComp-D12 / | #14: Water | ChemComp-HOH / | |
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-Details
Compound details | ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.5 Å3/Da / Density % sol: 76 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.977 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→15.9 Å / Num. obs: 106556 / % possible obs: 98.6 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 2.2→2.25 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 2.7 / % possible all: 98.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: WILD-TYPE RHODOBACTER SPHAEROIDES COORDINATES UNPUBLISHED DATA Resolution: 2.2→15.97 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.944 / SU B: 7.663 / SU ML: 0.088 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.135 / ESU R Free: 0.128 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.95 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→15.97 Å
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Refine LS restraints |
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