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Yorodumi- PDB-1q10: Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1q10 | ||||||
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Title | Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G | ||||||
Components | Immunoglobulin G binding protein G | ||||||
Keywords | PROTEIN BINDING / GB1 / core mutants / domain-swapping / oligomerization | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Streptococcus sp. 'group G' (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Byeon, I.J. / Louis, J.M. / Gronenborn, A.M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: A Protein Contortionist: Core Mutations of GB1 that Induce Dimerization and Domain Swapping Authors: Byeon, I.J. / Louis, J.M. / Gronenborn, A.M. #1: Journal: Science / Year: 1991 Title: A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G Authors: Gronenborn, A.M. / Filpula, D.R. / Essig, N.Z. / Achari, A. / Whitlow, M. / Wingfield, P.T. / Clore, G.M. #2: Journal: Nat.Struct.Biol. / Year: 2002 Title: Core Mutations Switch Monomeric Protein GB1 Into an Intertwined Tetramer Authors: Frank, M.K. / Dyda, F. / Dobrodumov, A. / Gronenborn, A.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1q10.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1q10.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 1q10.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1q10_validation.pdf.gz | 355.7 KB | Display | wwPDB validaton report |
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Full document | 1q10_full_validation.pdf.gz | 810 KB | Display | |
Data in XML | 1q10_validation.xml.gz | 89.8 KB | Display | |
Data in CIF | 1q10_validation.cif.gz | 137 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q1/1q10 ftp://data.pdbj.org/pub/pdb/validation_reports/q1/1q10 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Antibody | Mass: 6226.835 Da / Num. of mol.: 2 / Fragment: B1 Domain / Mutation: T228Q,L231V,F256V,Y259F,A260F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus sp. 'group G' (bacteria) / Gene: SPG / Plasmid: pET11A / Production host: Escherichia coli (E. coli) / Strain (production host): HMS174(DE3) / References: UniProt: P06654 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50mM sodium phosphate buffer / pH: 5.5 / Pressure: ambient / Temperature: 298 K | ||||||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1311 constraints per monomeric subunit: 1035 NOE-derived distance constraints, 72 hydrogen bond distance constraints, 148 dihedral angle constraints, ...Details: The structures are based on a total of 1311 constraints per monomeric subunit: 1035 NOE-derived distance constraints, 72 hydrogen bond distance constraints, 148 dihedral angle constraints, and 56 residual N-H dipolar coupling constraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy,target function Conformers calculated total number: 100 / Conformers submitted total number: 40 |