Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-124 |
Sentence |
denotes |
Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding. |
T1 |
0-124 |
Sentence |
denotes |
Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding. |
T1 |
0-124 |
Sentence |
denotes |
Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding. |
TextSentencer_T2 |
125-280 |
Sentence |
denotes |
Starch-branching enzyme catalyzes the cleavage of α-1, 4-linkages and the subsequent transfer of α-1,4 glucan to form an α-1,6 branch point in amylopectin. |
T2 |
125-280 |
Sentence |
denotes |
Starch-branching enzyme catalyzes the cleavage of α-1, 4-linkages and the subsequent transfer of α-1,4 glucan to form an α-1,6 branch point in amylopectin. |
T2 |
125-280 |
Sentence |
denotes |
Starch-branching enzyme catalyzes the cleavage of α-1, 4-linkages and the subsequent transfer of α-1,4 glucan to form an α-1,6 branch point in amylopectin. |
TextSentencer_T3 |
281-504 |
Sentence |
denotes |
Sequence analysis of the rice-branching enzyme I (BEI) indicated a modular structure in which the central α-amylase domain is flanked on each side by the N-terminal carbohydrate-binding module 48 and the α-amylase C-domain. |
T3 |
281-504 |
Sentence |
denotes |
Sequence analysis of the rice-branching enzyme I (BEI) indicated a modular structure in which the central α-amylase domain is flanked on each side by the N-terminal carbohydrate-binding module 48 and the α-amylase C-domain. |
T3 |
281-504 |
Sentence |
denotes |
Sequence analysis of the rice-branching enzyme I (BEI) indicated a modular structure in which the central α-amylase domain is flanked on each side by the N-terminal carbohydrate-binding module 48 and the α-amylase C-domain. |
TextSentencer_T4 |
505-655 |
Sentence |
denotes |
We determined the crystal structure of BEI at a resolution of 1.9 Å by molecular replacement using the Escherichia coli glycogen BE as a search model. |
T4 |
505-655 |
Sentence |
denotes |
We determined the crystal structure of BEI at a resolution of 1.9 Å by molecular replacement using the Escherichia coli glycogen BE as a search model. |
T4 |
505-655 |
Sentence |
denotes |
We determined the crystal structure of BEI at a resolution of 1.9 Å by molecular replacement using the Escherichia coli glycogen BE as a search model. |
TextSentencer_T5 |
656-841 |
Sentence |
denotes |
Despite three modular structures, BEI is roughly ellipsoidal in shape with two globular domains that form a prominent groove which is proposed to serve as the α-polyglucan-binding site. |
T5 |
656-841 |
Sentence |
denotes |
Despite three modular structures, BEI is roughly ellipsoidal in shape with two globular domains that form a prominent groove which is proposed to serve as the α-polyglucan-binding site. |
T5 |
656-841 |
Sentence |
denotes |
Despite three modular structures, BEI is roughly ellipsoidal in shape with two globular domains that form a prominent groove which is proposed to serve as the α-polyglucan-binding site. |
TextSentencer_T6 |
842-1042 |
Sentence |
denotes |
Amino acid residues Asp344 and Glu399, which are postulated to play an essential role in catalysis as a nucleophile and a general acid/base, respectively, are located at a central cleft in the groove. |
T6 |
842-1042 |
Sentence |
denotes |
Amino acid residues Asp344 and Glu399, which are postulated to play an essential role in catalysis as a nucleophile and a general acid/base, respectively, are located at a central cleft in the groove. |
T6 |
842-1042 |
Sentence |
denotes |
Amino acid residues Asp344 and Glu399, which are postulated to play an essential role in catalysis as a nucleophile and a general acid/base, respectively, are located at a central cleft in the groove. |
TextSentencer_T7 |
1043-1295 |
Sentence |
denotes |
Moreover, structural comparison revealed that in BEI, extended loop structures cause a narrowing of the substrate-binding site, whereas shortened loop structures make a larger space at the corresponding subsite in the Klebsiella pneumoniae pullulanase. |
T7 |
1043-1295 |
Sentence |
denotes |
Moreover, structural comparison revealed that in BEI, extended loop structures cause a narrowing of the substrate-binding site, whereas shortened loop structures make a larger space at the corresponding subsite in the Klebsiella pneumoniae pullulanase. |
T7 |
1043-1295 |
Sentence |
denotes |
Moreover, structural comparison revealed that in BEI, extended loop structures cause a narrowing of the substrate-binding site, whereas shortened loop structures make a larger space at the corresponding subsite in the Klebsiella pneumoniae pullulanase. |
TextSentencer_T8 |
1296-1448 |
Sentence |
denotes |
This structural difference might be attributed to distinct catalytic reactions, transglycosylation and hydrolysis, respectively, by BEI and pullulanase. |
T8 |
1296-1448 |
Sentence |
denotes |
This structural difference might be attributed to distinct catalytic reactions, transglycosylation and hydrolysis, respectively, by BEI and pullulanase. |
T8 |
1296-1448 |
Sentence |
denotes |
This structural difference might be attributed to distinct catalytic reactions, transglycosylation and hydrolysis, respectively, by BEI and pullulanase. |