+Open data
-Basic information
Entry | Database: PDB / ID: 2jjw | ||||||
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Title | Structure of human signal regulatory protein (sirp) gamma | ||||||
Components | SIGNAL REGULATORY PROTEIN GAMMA | ||||||
Keywords | CELL ADHESION / IMMUNOGLOBULIN DOMAIN / IMMUNOGLOBULIN SUPERFAMILY / SIRP / SIRPG / MEMBRANE / GLYCOPROTEIN / SIGNAL REGULATORY PROTEIN GAMMA / TRANSMEMBRANE / PAIRED RECEPTOR / ALTERNATIVE SPLICING | ||||||
Function / homology | Function and homology information positive regulation of cell-cell adhesion / Signal regulatory protein family interactions / positive regulation of phagocytosis / Cell surface interactions at the vascular wall / positive regulation of T cell activation / cell-cell signaling / cell adhesion / intracellular signal transduction / negative regulation of cell population proliferation / positive regulation of cell population proliferation ...positive regulation of cell-cell adhesion / Signal regulatory protein family interactions / positive regulation of phagocytosis / Cell surface interactions at the vascular wall / positive regulation of T cell activation / cell-cell signaling / cell adhesion / intracellular signal transduction / negative regulation of cell population proliferation / positive regulation of cell population proliferation / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Hatherley, D. / Graham, S.C. / Turner, J. / Harlos, K. / Stuart, D.I. / Barclay, A.N. | ||||||
Citation | Journal: Mol.Cell / Year: 2008 Title: Paired Receptor Specificity Explained by Structures of Signal Regulatory Proteins Alone and Complexed with Cd47. Authors: Hatherley, D. / Graham, S.C. / Turner, J. / Harlos, K. / Stuart, D.I. / Barclay, A.N. | ||||||
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. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jjw.cif.gz | 59.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jjw.ent.gz | 43.2 KB | Display | PDB format |
PDBx/mmJSON format | 2jjw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jjw_validation.pdf.gz | 427.1 KB | Display | wwPDB validaton report |
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Full document | 2jjw_full_validation.pdf.gz | 428.5 KB | Display | |
Data in XML | 2jjw_validation.xml.gz | 7.1 KB | Display | |
Data in CIF | 2jjw_validation.cif.gz | 9.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jj/2jjw ftp://data.pdbj.org/pub/pdb/validation_reports/jj/2jjw | HTTPS FTP |
-Related structure data
Related structure data | 2jjsC 2jjtC 2jjuC 2jjvC 2vscC 2uv3S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Antibody | Mass: 14213.292 Da / Num. of mol.: 1 / Fragment: N-TERMINAL ECTODOMAIN, RESIDUES 29-147 Source method: isolated from a genetically manipulated source Details: ISOFORM 4 / Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PEE14 / Cell line (production host): CHO / Production host: CRICETULUS GRISEUS (Chinese hamster) / Variant (production host): LEC3.2.8.1 / References: UniProt: Q9P1W8 |
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#2: Water | ChemComp-HOH / |
Sequence details | RESIDUE NUMBERING IS FOR THE MATURE PROTEIN (LACKING N- TERMINAL 28 AMINO ACID SIGNAL SEQUENCE). C- ...RESIDUE NUMBERING IS FOR THE MATURE PROTEIN (LACKING N- TERMINAL 28 AMINO ACID SIGNAL SEQUENCE). C-TERMINAL PURIFICATI |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.1 % / Description: NONE |
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Crystal grow | pH: 6.5 Details: 300 NL 11.5 MG/ML SIRP GAMMA PLUS 50 NL RESERVOIR (2.0 M AMMONIUM SULPHATE, 0.1 M BIS-TRIS PH 6.5) EQUILIBRATED AGAINST 95 UL OF RESERVOIR AT 20.5 C. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.933 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 16, 2007 / Details: MIRRORS |
Radiation | Monochromator: SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→38.2 Å / Num. obs: 14652 / % possible obs: 95.2 % / Observed criterion σ(I): -3 / Redundancy: 32.3 % / Biso Wilson estimate: 29.3 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 43.9 |
Reflection shell | Resolution: 1.7→1.8 Å / Redundancy: 33.4 % / Rmerge(I) obs: 0.73 / Mean I/σ(I) obs: 7 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2UV3 CHAIN A Resolution: 1.7→38.21 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.94 / SU B: 6.453 / SU ML: 0.106 / Cross valid method: THROUGHOUT / ESU R: 0.122 / ESU R Free: 0.122 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. B VALUES INCLUDE TLS CONTRIBUTIONS.
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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: 30.98 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→38.21 Å
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Refine LS restraints |
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