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Open data
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Basic information
| Entry | Database: PDB / ID: 1t7w | |||||||||
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| Title | Zn-alpha-2-glycoprotein; CHO-ZAG PEG 400 | |||||||||
Components | Zinc-alpha-2-glycoprotein | |||||||||
Keywords | LIPID BINDING PROTEIN / MHC class I homolog | |||||||||
| Function / homology | Function and homology informationMiscellaneous transport and binding events / detection of chemical stimulus involved in sensory perception of bitter taste / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / protein transmembrane transporter activity / RNA nuclease activity / positive regulation of T cell mediated cytotoxicity / : / cell adhesion / immune response ...Miscellaneous transport and binding events / detection of chemical stimulus involved in sensory perception of bitter taste / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / protein transmembrane transporter activity / RNA nuclease activity / positive regulation of T cell mediated cytotoxicity / : / cell adhesion / immune response / negative regulation of cell population proliferation / external side of plasma membrane / extracellular space / extracellular exosome / extracellular region / nucleus Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.7 Å | |||||||||
Authors | Delker, S.L. / West Jr., A.P. / McDermott, L. / Kennedy, M.W. / Bjorkman, P.J. | |||||||||
Citation | Journal: J.Struct.Biol. / Year: 2004Title: Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein. Authors: Delker, S.L. / West Jr., A.P. / McDermott, L. / Kennedy, M.W. / Bjorkman, P.J. #1: Journal: Science / Year: 1999Title: Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules Authors: Sanchez, L.M. / Chirino, A.J. / Bjorkman, P.J. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1t7w.cif.gz | 68.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1t7w.ent.gz | 50.1 KB | Display | PDB format |
| PDBx/mmJSON format | 1t7w.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1t7w_validation.pdf.gz | 762.4 KB | Display | wwPDB validaton report |
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| Full document | 1t7w_full_validation.pdf.gz | 767.1 KB | Display | |
| Data in XML | 1t7w_validation.xml.gz | 12.5 KB | Display | |
| Data in CIF | 1t7w_validation.cif.gz | 15.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t7/1t7w ftp://data.pdbj.org/pub/pdb/validation_reports/t7/1t7w | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1t7vSC ![]() 1t7xC ![]() 1t7yC ![]() 1t7zC ![]() 1t80C S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 32185.953 Da / Num. of mol.: 1 / Mutation: N89K, N92T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AZGP1, ZAG, ZNGP1 / Plasmid: pBJ5-GS / Production host: ![]() |
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| #2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
| #3: Sugar | ChemComp-NAG / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 67.27 % |
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| Crystal grow | Temperature: 298 K / Method: microbatch / pH: 7.5 Details: Ammonium sulfate, PEG 400, HEPES, pH 7.5, Microbatch, temperature 298.0K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.1 Å |
| Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Dec 19, 2002 |
| Radiation | Monochromator: Double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
| Reflection | Resolution: 2.7→30 Å / Num. obs: 13782 / % possible obs: 98.5 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 12.1 |
| Reflection shell | Resolution: 2.7→2.8 Å / % possible obs: 96.9 % / Rmerge(I) obs: 0.456 / Mean I/σ(I) obs: 1.8 / % possible all: 95.6 |
-Phasing
| Phasing | Method: molecular replacement |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB Entry 1T7V Resolution: 2.7→20 Å / Rfactor Rfree error: 0.011 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
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| Solvent computation | Solvent model: CNS bulk solvent model used / Bsol: 30.8686 Å2 / ksol: 0.351417 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 178.93 Å2 / Biso mean: 51.21 Å2 / Biso min: 1.51 Å2
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| Refine analyze |
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| Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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| Refine LS restraints |
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION
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Homo sapiens (human)
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