The Solution Structure of the CBM4-2 Carbohydrate Binding Module from a Thermostable Rhodothermus marinus Xylanase.
Second family 4 carbohydrate binding module (CBM4-2)(Residues 211-373)
MLVANINGGFESTPAGVVTDLAEGVEGWDLNVGSSVTNPPVFEVLETSDAPEGNKVLAVTVNGVGNNPWDIEATAFPVNV RPGVTYTYTIWARAEQDGAVVSFTVGNQSFQEYGRLHEQQITTEWQPFTFEFTVSDQETVIRAPIHFGYAANVGNTIYID GLAIASQP
1K45 CONTAINS THE MINIMIZED AVERAGE STRUCTURE FOR THIS PROTEIN
structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy
The final set of restraints contained 1654 non-redundant unambiguous NOEs and 17 ambiguous NOEs, 93 dihedral angle restraints, 72 chi1 and 1 chi2 restraint, and 65 pairs of hydrogen bond restraints, plus 177 backbone dihedral restraints based on 13C shifts from TALOS.
hybrid distance geometry/simulated annealing using XPLOR
1.5 mM CBM4-2 15N-labelled, and 13C,15N double labelled protein; 50 mM CaCl2, 50 mM sodium acetate-d3, pH 6.0, 10% D2O, 10 mM sodium azide, 0.1 mM sodium trimethylsilylpropionate (TSP)
beta-sandwich formed by 11 strands. Binding-site cleft. Solvent exposed aromatics (Trp69, Phe110) in binding cleft. Two helical twists. Two calcium binding sites., Hydrolase
LVANINGGFESTPAGVVTDLAEGVEGWDLNVGSSVTNPPVFEVLETSDAPEGNKVLAVTVNGVGNNPWDIEATAFPVNVR PGVTYTYTIWARAEQDGAVVSFTVGNQSFQEYGRLHEQQITTEWQPFTFEFTVSDQETVIRAPIHFGYAANVGNTIYIDG LAI