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Open data
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Basic information
Entry | Database: PDB / ID: 1mg1 | |||||||||
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Title | HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA | |||||||||
![]() | PROTEIN (HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA) | |||||||||
![]() | VIRAL PROTEIN / HUMAN T CELL LEUKEMIA VIRUS TYPE 1 / HTLV-1 / ENVELOPE PROTEIN / MEMBRANE FUSION / MALTOSE-BINDING PROTEIN CHIMERA | |||||||||
Function / homology | ![]() detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis ...detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / outer membrane-bounded periplasmic space / periplasmic space / DNA damage response / membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Kobe, B. / Center, R.J. / Kemp, B.E. / Poumbourios, P. | |||||||||
![]() | ![]() Title: Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins. Authors: Kobe, B. / Center, R.J. / Kemp, B.E. / Poumbourios, P. #1: ![]() Title: Crystallization of a Trimeric Human T Cell Leukemia Virus Type 1 Gp21 Ectodomain Fragment as a Chimera with Maltose-Binding Protein Authors: Center, R.J. / Kobe, B. / Wilson, K.A. / Teh, T. / Howlett, G.J. / Kemp, B.E. / Poumbourios, P. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.1 KB | Display | ![]() |
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PDB format | ![]() | 76.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 442.6 KB | Display | ![]() |
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Full document | ![]() | 460.4 KB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 17.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1anfS S: Starting model for refinement |
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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 on special symmetry positions |
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Components
#1: Protein | Mass: 49386.023 Da / Num. of mol.: 1 / Fragment: GP21 ECTODOMAIN (GP62 RESIDUES 338-425) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47 % | ||||||||||||||||||||
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Crystal grow | pH: 4.7 / Details: pH 4.7 | ||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 1998 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.29→99 Å / Num. obs: 19248 / % possible obs: 91 % / Redundancy: 7.8 % / Biso Wilson estimate: 60.4 Å2 / Rmerge(I) obs: 0.068 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 2.29→2.37 Å / Rmerge(I) obs: 0.364 / Mean I/σ(I) obs: 1.2 / % possible all: 65 |
Reflection | *PLUS Num. measured all: 150336 |
Reflection shell | *PLUS % possible obs: 65 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ANF Resolution: 2.5→40 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
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Displacement parameters | Biso mean: 65.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.59 Å / Rfactor Rfree error: 0.044 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.223 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.44 |