|Entry||Database: PDB / ID: 1fcl|
|Title||DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF STREPTOCOCCAL PROTEIN G|
|Components||IMMUNOGLOBULIN G BINDING PROTEIN G|
|Keywords||PROTEIN BINDING / Designed Core Mutant / Streptococcal Protein G|
|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. (bacteria)|
|Method||SOLUTION NMR / Standard Distance Geometry, simulated Annealing Methods|
|Authors||Ross, S.A. / Sarisky, C.A. / Su, A. / Mayo, S.L.|
|Citation||Journal: Protein Sci. / Year: 2001|
Title: Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification.
Authors: Ross, S.A. / Sarisky, C.A. / Su, A. / Mayo, S.L.
|Structure viewer||Molecule: |
Downloads & links
A: IMMUNOGLOBULIN G BINDING PROTEIN G
|#1: Antibody|| |
Mass: 6216.819 Da / Num. of mol.: 1 / Fragment: GB1_DELTA1.5 / Mutation: Y3F, L7I, F30L, A34I, V39I, F52W
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus sp. (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P19909
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: none|
|Details||Contents: 1 mM unlabeled protein in 50 mM sodium phosphate, pH 6.0|
Solvent system: either D2O or 90:10 H2O:D2O
|Sample conditions||Ionic strength: 50 mM sodium phosphate / pH: 6.0 / Pressure: Atmospheric atm / Temperature: 298 K|
*PLUSMethod: other / Details: NMR
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|NMR spectrometer||Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz|
|Refinement||Method: Standard Distance Geometry, simulated Annealing Methods|
Software ordinal: 1
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: Structures with the Least Restraint Violations, Structures with the Lowest Energy|
Conformers calculated total number: 100 / Conformers submitted total number: 40
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