|Entry||Database: PDB / ID: 2kq4|
|Title||Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy|
|Components||Immunoglobulin G-binding protein G|
|Keywords||IMMUNE SYSTEM / GB1 / TEDOR / Solid-State / Cell wall / IgG-binding protein / Peptidoglycan-anchor / Secreted / THERMOSTABLE|
|Function / homology|
Function and homology information
IgG binding / cell wall / : / extracellular region
Similarity search - Function
IgG-binding B / B domain / M protein-type anchor domain / GA-like domain / GA-like domain / Ubiquitin-like (UB roll) - #10 / Immunoglobulin/albumin-binding domain superfamily / YSIRK Gram-positive signal peptide / : / LPXTG cell wall anchor motif ...IgG-binding B / B domain / M protein-type anchor domain / GA-like domain / GA-like domain / Ubiquitin-like (UB roll) - #10 / Immunoglobulin/albumin-binding domain superfamily / YSIRK Gram-positive signal peptide / : / LPXTG cell wall anchor motif / Gram-positive cocci surface proteins LPxTG motif profile. / LPXTG cell wall anchor domain / Ubiquitin-like (UB roll) / Roll / Alpha Beta
Similarity search - Domain/homology
Immunoglobulin G-binding protein G
Similarity search - Component
|Biological species||Streptococcus sp. 'group G' (bacteria)|
|Method||SOLID-STATE NMR / DGSA-distance geometry simulated annealing, simulated annealing|
|Model details||lowest energy, model 4|
|Authors||Nieuwkoop, A.J. / Wylie, B.J. / Franks, W. / Shah, G.J. / Rienstra, C.M.|
|Citation||Journal: J.Chem.Phys. / Year: 2009|
Title: Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy
Authors: Nieuwkoop, A.J. / Wylie, B.J. / Franks, W.T. / Shah, G.J. / Rienstra, C.M.
|Structure viewer||Molecule: |
Downloads & links
X: Immunoglobulin G-binding protein G
|#1: Antibody|| |
Mass: 6228.809 Da / Num. of mol.: 1 / Fragment: UNP residues 303 to 357 / Mutation: T2Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus sp. 'group G' (bacteria) / Gene: spg / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P19909
|Experiment||Method: SOLID-STATE NMR|
|Sample conditions||Pressure: ambient / Temperature units: K|
|NMR spectrometer||Type: Varian Infinity Plus / Manufacturer: Varian / Model: Infinity Plus / Field strength: 500 MHz|
|Refinement||Method: DGSA-distance geometry simulated annealing, simulated annealing|
Software ordinal: 1
Details: DG sub-embed was used from initial extend geometry, Two steps of simulated annealing
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structures with the lowest energy|
Conformers calculated total number: 250 / Conformers submitted total number: 10
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