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- PDB-6bk7: 1.83 Angstrom Resolution Crystal Structure of N-terminal Fragment... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6bk7 | ||||||
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Title | 1.83 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-404) of Elongation Factor G from Enterococcus faecalis | ||||||
![]() | Elongation factor G | ||||||
![]() | RIBOSOMAL PROTEIN / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID / Elongation factor G | ||||||
Function / homology | ![]() translation elongation factor activity / GTPase activity / GTP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Minasov, G. / Shuvalova, L. / Dubrovska, I. / Cardona-Correa, A. / Grimshaw, S. / Kwon, K. / Anderson, W.F. / Satchell, K.J.F. / Joachimiak, A. / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
![]() | ![]() Title: Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria. Authors: Inniss, N.L. / Minasov, G. / Chang, C. / Tan, K. / Kim, Y. / Maltseva, N. / Stogios, P. / Filippova, E. / Michalska, K. / Osipiuk, J. / Jaroszewki, L. / Godzik, A. / Savchenko, A. / ...Authors: Inniss, N.L. / Minasov, G. / Chang, C. / Tan, K. / Kim, Y. / Maltseva, N. / Stogios, P. / Filippova, E. / Michalska, K. / Osipiuk, J. / Jaroszewki, L. / Godzik, A. / Savchenko, A. / Joachimiak, A. / Anderson, W.F. / Satchell, K.J.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 327 KB | Display | ![]() |
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PDB format | ![]() | 267.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5uswC ![]() 5usxC ![]() 5utxC ![]() 5uu6C ![]() 5uwyC ![]() 5ux9C ![]() 5wp0C ![]() 6aonC ![]() 6aooC ![]() 6aziC ![]() 6b5fC ![]() 6b8dC ![]() 6blbC ![]() 6c8qC ![]() 6pu9C ![]() 6puaC ![]() 6pxaC ![]() 6w2zC ![]() 5vh6S S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Other databases |
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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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Components
#1: Protein | Mass: 45440.992 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 700802 / V583 / Gene: fusA, EF_0200 / Plasmid: pMCSG53 / Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Has protein modification | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.8 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8.3 Details: 12.5 mg/mL protein in 0.5 sodium chloride, 0.01 M Tris, pH 8.3 against screen PEGs II (G6), 15% w/v PEG6000, 5% w/v glycerol, cryoprotectant: reservoir |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 2, 2017 / Details: C(111) |
Radiation | Monochromator: diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 1.83→30 Å / Num. obs: 69321 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 4.5 % / Biso Wilson estimate: 35.5 Å2 / Rmerge(I) obs: 0.046 / Rpim(I) all: 0.025 / Rrim(I) all: 0.052 / Rsym value: 0.046 / Χ2: 1.004 / Net I/σ(I): 28.8 |
Reflection shell | Resolution: 1.83→1.86 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.793 / Mean I/σ(I) obs: 2.05 / Num. unique obs: 3419 / CC1/2: 0.774 / Rpim(I) all: 0.423 / Rrim(I) all: 0.9 / Rsym value: 0.793 / Χ2: 1.006 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 5VH6 Resolution: 1.83→28.95 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.956 / SU B: 8.395 / SU ML: 0.122 / Cross valid method: THROUGHOUT / ESU R: 0.144 / ESU R Free: 0.127 / 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: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.832 Å2
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Refinement step | Cycle: 1 / Resolution: 1.83→28.95 Å
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Refine LS restraints |
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