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- PDB-3ld7: Crystal structure of the Lin0431 protein from Listeria innocua, N... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3ld7 | ||||||
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Title | Crystal structure of the Lin0431 protein from Listeria innocua, Northeast Structural Genomics Consortium Target LkR112 | ||||||
![]() | Lin0431 protein | ||||||
![]() | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / Lin0431 / DUF1312 / PF07009 / LkR112 / NESG / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium | ||||||
Function / homology | N-utilization substance G protein NusG, insert domain / NusG, domain 2 / NusG, domain 2 superfamily / NusG domain II / mini-chromosome maintenance (MCM) complex, domain 2 / Sandwich / Mainly Beta / Lin0431 protein![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Vorobiev, S. / Chen, Y. / Lee, D. / Patel, D.J. / Ciccosanti, C. / Sahdev, S. / Acton, T.B. / Xiao, R. / Everett, J.K. / Montelione, G.T. ...Vorobiev, S. / Chen, Y. / Lee, D. / Patel, D.J. / Ciccosanti, C. / Sahdev, S. / Acton, T.B. / Xiao, R. / Everett, J.K. / Montelione, G.T. / Hunt, J.F. / Tong, L. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Crystal structure of the Lin0431 protein from Listeria innocua Authors: Vorobiev, S. / Chen, Y. / Lee, D. / Patel, D.J. / Ciccosanti, C. / Sahdev, S. / Acton, T.B. / Xiao, R. / Everett, J.K. / Montelione, G.T. / Hunt, J.F. / Tong, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 115.2 KB | Display | ![]() |
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PDB format | ![]() | 95.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 444.7 KB | Display | ![]() |
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Full document | ![]() | 447.2 KB | Display | |
Data in XML | ![]() | 15.2 KB | Display | |
Data in CIF | ![]() | 21.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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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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3 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Details | monomer according to gel filtration |
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Components
#1: Protein | Mass: 11537.740 Da / Num. of mol.: 3 / Fragment: sequence database residues 36-127 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.41 % |
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Crystal grow | Temperature: 291 K / Method: microbatch under paraffin oil / pH: 8.2 Details: 0.072M sodium phosphate monobasic, 1.728M potassium phosphate dibasic, pH 8.2, microbatch under paraffin oil, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jan 7, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97814 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→50 Å / Num. all: 84850 / Num. obs: 84087 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.4 % / Biso Wilson estimate: 19.53 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 34.3 |
Reflection shell | Highest resolution: 1.55 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.399 / Mean I/σ(I) obs: 3.4 / Num. unique all: 8496 / % possible all: 98.3 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 60.156 Å2 / ksol: 0.4 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.547→31.547 Å
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Refine LS restraints |
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LS refinement shell |
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