the complex of Glycoside Hydrolase 5 Lichenase from Caldicellulosiruptor sp. F32 E188Q mutant and cellotetraose

Structural insights into the substrate specificity of a glycoside hydrolase family 5 lichenase from Caldicellulosiruptor sp. F32

MRGSHHHHHHGMASLNRESSNRAKIPEIKIASRKIPNNAALKFVKDMKIGWNLGNTFDAAFENPSFDDELLYETAWCGVK
TTKQMIDTVKKAGFNTIRIPVSWHNHVTGSNFTISKRWLDRVQQVVDYAMKNKMYVIINIHHDIMPGYYYPNSQHLQTSI
KYVKSIWTQVATRFKNYNDHLIFEAVNQPRLTGSRFEWWLDMNNPECRDAVEAINKLNQVFVDTVRSTGGNNVSRYLMVP
GYAAAPEYVLIDEFKIPKDSSKYKNRIIISVHAYRPYNFALQAPNESGSVSEWSVNSEESRRDIDYFMDKLYDKFVSKGI
PVVIGEFGARDKNGNLQSRVEFAAYYVRAARARGITCCWWDNNAFYGNGENFGLLDRKTLKWVYPEIVSAMMKYAR

0.2 M ammonium sulfate, 0.1 M Tris, 25% PEG3350

chain 'A' and (resid 22 through 68 )

chain 'A' and (resid 69 through 91 )

chain 'A' and (resid 92 through 152 )

chain 'A' and (resid 153 through 173 )

chain 'A' and (resid 174 through 204 )

chain 'A' and (resid 205 through 228 )

chain 'A' and (resid 229 through 260 )

chain 'A' and (resid 261 through 280 )

chain 'A' and (resid 281 through 371 )

chain 'A' and (resid 372 through 396 )

Glycoside Hydrolase 5 Lichenase, HYDROLASE

SSNRAKIPEIKIASRKIPNNAALKFVKDMKIGWNLGNTFDAAFENPSFDDELLYETAWCGVKTTKQMIDTVKKAGFNTIR
IPVSWHNHVTGSNFTISKRWLDRVQQVVDYAMKNKMYVIINIHHDIMPGYYYPNSQHLQTSIKYVKSIWTQVATRFKNYN
DHLIFEAVNEPRLTGSRFEWWLDMNNPECRDAVEAINKLNQVFVDTVRSTGGNNVSRYLMVPGYAAAPEYVLIDEFKIPK
DSSKYKNRIIISVHAYRPYNFALQAPNESGSVSEWSVNSEESRRDIDYFMDKLYDKFVSKGIPVVIGEFGARDKNGNLQS
RVEFAAYYVRAARARGITCCWWDNNAFYGNGENFGLLDRKTLKWVYPEIVSAMMKYAR