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Assignments of Backbone 1H, 13C, 15N Resonances and Secondary Structure of Ribonuclease H from Escherichia coli by Heteronuclear Three-Dimensional NMR Spectroscopy
Authors
Yamazaki, T., Yoshida, M., Kanaya, S., Nakamura, H., Nagayama, K.
Assembly
ribonuclease H
Entity
1. ribonuclease H (polymer), 155 monomers, 17596.78 Da Detail

MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV


Formula weight
17596.78 Da
Source organism
Escherichia coli
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 39.7 %, Completeness (bb): 67.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All39.7 % (725 of 1825)41.4 % (392 of 947)26.3 % (183 of 697)82.9 % (150 of 181)
Backbone67.2 % (609 of 906)99.3 % (303 of 305)35.0 % (158 of 451)98.7 % (148 of 150)
Sidechain12.7 % (135 of 1060)13.9 % (89 of 642)11.4 % (44 of 387) 6.5 % (2 of 31)
Aromatic 0.0 % (0 of 152) 0.0 % (0 of 76) 0.0 % (0 of 70) 0.0 % (0 of 6)
Methyl13.8 % (22 of 160)13.8 % (11 of 80)13.8 % (11 of 80)

1. ribonuclease H

MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV

Sample

Temperature 300 K, pH 5.5



Release date
1995-07-30
Citation
Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy
Yamazaki, T., Yoshida, M., Kanaya, S., Nakamura, H., Nagayama, K.
Biochemistry (1991), 30, 6036-6047, PubMed 1646006 , DOI 10.1021/bi00238a030 ,
Related entities 1. ribonuclease H, : 1 : 4 : 7 : 22 : 155 entities Detail
Interaction partners 1. ribonuclease H, : 5 interactors Detail
Experiments performed 1 experiments Detail