+Open data
-Basic information
Entry | Database: PDB / ID: 2frg | ||||||
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Title | Structure of the immunoglobulin-like domain of human TLT-1 | ||||||
Components | trem-like transcript-1 | ||||||
Keywords | IMMUNE SYSTEM / immunoglobulin-like / beta-sandwich / cell surface receptor / triggering receptor / TREM-like / platelet receptor / ITIM | ||||||
Function / homology | Function and homology information platelet alpha granule / calcium-mediated signaling / platelet activation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / nuclear speck / innate immune response / Golgi apparatus / cell surface / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.19 Å | ||||||
Authors | Gattis, J.L. / Lubkowski, J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: The structure of the extracellular domain of triggering receptor expressed on myeloid cells like transcript-1 and evidence for a naturally occurring soluble fragment. Authors: Gattis, J.L. / Washington, A.V. / Chisholm, M.M. / Quigley, L. / Szyk, A. / McVicar, D.W. / Lubkowski, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2frg.cif.gz | 59.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2frg.ent.gz | 42.5 KB | Display | PDB format |
PDBx/mmJSON format | 2frg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fr/2frg ftp://data.pdbj.org/pub/pdb/validation_reports/fr/2frg | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | Current biochemical and crystallographic evidence suggest that the biologically active form is monomeric. |
-Components
#1: Antibody | Mass: 11523.272 Da / Num. of mol.: 1 / Fragment: immunoglobulin-like domain 20-125 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TLT-1 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3RIL / References: UniProt: Q86YW5 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.57 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: Mother liquor contained 15-19% w/w PEG6000, 0.5M Na/K phosphate pH 5.6. Protein solution contained 10mg/ml TLT-1 in 20mM Tris pH 8. Protein and mother liquor were mixed in equal proportions ...Details: Mother liquor contained 15-19% w/w PEG6000, 0.5M Na/K phosphate pH 5.6. Protein solution contained 10mg/ml TLT-1 in 20mM Tris pH 8. Protein and mother liquor were mixed in equal proportions at 15 C, and hanging drops were suspended over mother liquor., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.19→30 Å / Num. all: 32052 / Num. obs: 31487 / % possible obs: 98.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.4 % / Rsym value: 0.064 / Net I/σ(I): 25.9 | ||||||||||||||||||
Reflection shell | Resolution: 1.19→1.23 Å / Redundancy: 3.5 % / Mean I/σ(I) obs: 3.2 / Rsym value: 0.31 / % possible all: 87 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Hybrid model containing structurally conserved residues of TREM-1 (1SMO chain A), NKp44(1HKF), and D1 domain of polymeric immunoglobulin receptor (1XED chain E). Resolution: 1.19→30 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.954 / SU B: 1.156 / SU ML: 0.024 / Cross valid method: THROUGHOUT / ESU R: 0.046 / ESU R Free: 0.042 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.076 Å2
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Refine analyze | Luzzati coordinate error obs: 0.144 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.19→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.19→1.221 Å / Total num. of bins used: 20
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