+Open data
-Basic information
Entry | Database: PDB / ID: 7kmj | ||||||||||||
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Title | Hsa Siglec and Unique domains in complex with Sialyl Lewis C | ||||||||||||
Components | Streptococcal hemagglutinin | ||||||||||||
Keywords | CELL ADHESION / adhesin | ||||||||||||
Function / homology | Function and homology information surface biofilm formation / biofilm matrix assembly / cell adhesion / extracellular region Similarity search - Function | ||||||||||||
Biological species | Streptococcus gordonii str. Challis (bacteria) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.33 Å | ||||||||||||
Authors | Stubbs, H.E. / Iverson, T.M. | ||||||||||||
Funding support | 3items
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Citation | Journal: Nat Commun / Year: 2022 Title: Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation. Authors: Bensing, B.A. / Stubbs, H.E. / Agarwal, R. / Yamakawa, I. / Luong, K. / Solakyildirim, K. / Yu, H. / Hadadianpour, A. / Castro, M.A. / Fialkowski, K.P. / Morrison, K.M. / Wawrzak, Z. / Chen, ...Authors: Bensing, B.A. / Stubbs, H.E. / Agarwal, R. / Yamakawa, I. / Luong, K. / Solakyildirim, K. / Yu, H. / Hadadianpour, A. / Castro, M.A. / Fialkowski, K.P. / Morrison, K.M. / Wawrzak, Z. / Chen, X. / Lebrilla, C.B. / Baudry, J. / Smith, J.C. / Sullam, P.M. / Iverson, T.M. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7kmj.cif.gz | 145.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7kmj.ent.gz | 108.2 KB | Display | PDB format |
PDBx/mmJSON format | 7kmj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/km/7kmj ftp://data.pdbj.org/pub/pdb/validation_reports/km/7kmj | HTTPS FTP |
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-Related structure data
Related structure data | 6ef7C 6ef9C 6efaC 6efbC 6efcC 6efdC 6effC 6efiC 6x3kC 6x3qC 5eq2S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 25837.381 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus gordonii str. Challis (bacteria) Strain: Challis / Gene: hsa, SGO_0966 / Production host: Escherichia coli (E. coli) / References: UniProt: A8AWU7 | ||||
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#2: Polysaccharide | N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.99 Å3/Da / Density % sol: 38.32 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 21.6 mg/ml in 20 mM Tris-HCl, pH 7.2. Equilibrate 1 ul protein and 2 ul reservoir solution over 50 ul of reservoir solution (0.1 M Succinate/Phosphate/Glycine pH 10.0 and 25% PEG 3350). ...Details: 21.6 mg/ml in 20 mM Tris-HCl, pH 7.2. Equilibrate 1 ul protein and 2 ul reservoir solution over 50 ul of reservoir solution (0.1 M Succinate/Phosphate/Glycine pH 10.0 and 25% PEG 3350). Crystals were soaked in reservoir solution supplemented with 5 mM of sLec for 20 hr |
-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: 0.9795 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 21, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→50 Å / Num. obs: 1748709 / % possible obs: 99.7 % / Redundancy: 8 % / Biso Wilson estimate: 16.25 Å2 / CC1/2: 0.998 / Net I/σ(I): 40.5 |
Reflection shell | Resolution: 1.3→1.32 Å / Num. unique obs: 2468 / CC1/2: 0.891 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5EQ2 Resolution: 1.33→37.99 Å / SU ML: 0.1624 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.6886 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: 26 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.33→37.99 Å
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Refine LS restraints |
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LS refinement shell |
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