| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-131 |
Sentence |
denotes |
Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases. |
| T2 |
132-378 |
Sentence |
denotes |
The crystal structure of the 32-kDa catalytic domain of the Streptomyces lividans xylanase A was solved by molecular isomorphous replacement methods and subsequently refined at 2.6-A resolution to a conventional crystallographic R factor of 0.21. |
| T3 |
379-490 |
Sentence |
denotes |
This is the first successful structure determination of a member of the F family of endo-beta-1,4-D-glycanases. |
| T4 |
491-562 |
Sentence |
denotes |
Unlike the recently determined xylanases of the G family (Wakarchuk, W. |
| T5 |
563-579 |
Sentence |
denotes |
W., Campbell, R. |
| T6 |
580-592 |
Sentence |
denotes |
L., Sung, W. |
| T7 |
593-645 |
Sentence |
denotes |
L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. |
| T8 |
646-876 |
Sentence |
denotes |
3, 467-475), where the catalytic domains have a unique beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is folded into a complete (alpha/beta)8 barrel, the first such fold observed among beta-1,4-D-glycanases. |
| T9 |
877-943 |
Sentence |
denotes |
The active site is located at the carbonyl end of the beta barrel. |
| T10 |
944-1146 |
Sentence |
denotes |
The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. |
| T11 |
1147-1161 |
Sentence |
denotes |
J., in press). |
| T1 |
0-131 |
Sentence |
denotes |
Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases. |
| T2 |
132-378 |
Sentence |
denotes |
The crystal structure of the 32-kDa catalytic domain of the Streptomyces lividans xylanase A was solved by molecular isomorphous replacement methods and subsequently refined at 2.6-A resolution to a conventional crystallographic R factor of 0.21. |
| T3 |
379-490 |
Sentence |
denotes |
This is the first successful structure determination of a member of the F family of endo-beta-1,4-D-glycanases. |
| T4 |
491-562 |
Sentence |
denotes |
Unlike the recently determined xylanases of the G family (Wakarchuk, W. |
| T5 |
563-579 |
Sentence |
denotes |
W., Campbell, R. |
| T6 |
580-592 |
Sentence |
denotes |
L., Sung, W. |
| T7 |
593-645 |
Sentence |
denotes |
L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. |
| T8 |
646-876 |
Sentence |
denotes |
3, 467-475), where the catalytic domains have a unique beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is folded into a complete (alpha/beta)8 barrel, the first such fold observed among beta-1,4-D-glycanases. |
| T9 |
877-943 |
Sentence |
denotes |
The active site is located at the carbonyl end of the beta barrel. |
| T10 |
944-1146 |
Sentence |
denotes |
The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. |
| T11 |
1147-1161 |
Sentence |
denotes |
J., in press). |