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- PDB-1a7l: DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1a7l | |||||||||
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Title | DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN | |||||||||
![]() | MALE-B363 | |||||||||
![]() | TRANSPORT / PRES2 / ![]() ![]() | |||||||||
Function / homology | ![]() detection of maltose stimulus / ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | synthetic construct (others) | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Saul, F.A. / Vulliez-Lenormand, B. / Lema, F. / Bentley, G.A. | |||||||||
![]() | ![]() Title: Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein. Authors: Saul, F.A. / Vulliez-le Normand, B. / Lema, F. / Bentley, G.A. #1: ![]() Title: Maltodextrin-Binding Protein Hybrids Carrying Epitopes from the Pres2 Region of Hepatitis B Virus: Expression, Antibody-Binding and Preliminary Crystallographic Studies Authors: Vulliez-Le Normand, B. / Saul, F.A. / Martineau, P. / Lema, F. / Hofnung, M. / Bentley, G.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 220.5 KB | Display | ![]() |
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PDB format | ![]() | 178.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS THREE INDEPENDENT MOLECULES OF MALE-B363. EACH IS ASSOCIATED WITH A BOUND MOLECULE OF MALTOSE SUBSTRATE. THE FOLLOWING CHAIN IDENTIFIERS ARE USED: CHAIN A, MALE-B363 MOLECULE 1; CHAIN B, MALE-B363 MOLECULE 2; CHAIN C, MALE-B363 MOLECULE 3; CHAIN D, HET GROUP ASSOCIATED WITH MOLECULE 1; CHAIN E, HET GROUP ASSOCIATED WITH MOLECULE 2; CHAIN F, HET GROUP ASSOCIATED WITH MOLECULE 3; CHAIN X, SOLVENTS ASSOCIATED WITH MOLECULE 1; CHAIN Y, SOLVENTS ASSOCIATED WITH MOLECULE 2; CHAIN Z, SOLVENTS ASSOCIATED WITH MOLECULE 3. |
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Components
#1: Protein | Mass: 42650.176 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Strain: ED9 / Gene: MBP MUTANT / Plasmid: PPD91-(DERIVATIVE) / Gene (production host): MBP MUTANT / Production host: ![]() ![]() ![]() #2: Polysaccharide | #3: Water | ChemComp-HOH / | ![]() Compound details | MALE-B363 IS AN INSERTION/DELETION MUTANT OF THE E. COLI MALTODEXTRIN-BINDING PROTEIN (MBP) ...MALE-B363 IS AN INSERTION/DELETION MUTANT OF THE E. COLI MALTODEXTR | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 42 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 8.5 Details: PROTEIN CONCENTRATION 3.0MG/ML, BUFFER 0.1M TRIS-HCL PH 8.5 WITH 0.2 M MGCL2, 1 MM MALTOSE, 26% PEG 4000. | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Vulliez-Le Normand, B., (1997) Protein Eng., 10, 175. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1994 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.9→15 Å / Num. obs: 24492 / % possible obs: 98 % / Observed criterion σ(I): 1 / Redundancy: 3.6 % / Rmerge(I) obs: 0.119 / Net I/σ(I): 14.3 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 3 % / Rmerge(I) obs: 0.419 / Mean I/σ(I) obs: 2.7 / % possible all: 90 |
Reflection | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 15 Å / % possible obs: 98 % / Observed criterion σ(I): 1 / Redundancy: 3.6 % |
Reflection shell | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 3 Å / % possible obs: 90 % / Redundancy: 3 % / Num. unique obs: 2146 / Mean I/σ(I) obs: 2.7 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: MBP RESIDUES 4 - 362 (PDB ENTRY 1ANF) Resolution: 2.9→10 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / σ(F): 1
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Displacement parameters | Biso mean: 26.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→10 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.9→3.03 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.357 / Rfactor Rwork: 0.248 |