BMRB: 1877

Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium

Authors

Wang, J., Hinck, A.P., Loh, S.N., LeMaster, D.M., Markley, J.L.

Assembly

micrococcal nuclease

Entity

1. micrococcal nuclease (polymer), 143 monomers, 16214.55 Da Detail

ATSTKKLHKE PATLIKAIDG DTVKLMYKGQ PMTFRLLLVD TPETKHPKKG VEKYGPEASA FTKKMVENAK KIEVEFDKGQ RTDKYGRGLA YIYADGKMVN EALVRQGLAK VAYVYKPNNT HEQLLRKSEA QAKKEKLNIW SED

Formula weight

16214.55 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 9.8 %, Completeness: 2.5 %, Completeness (bb): 5.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	2.5 % (23 of 912)	2.5 % (23 of 912)
Backbone	5.9 % (17 of 289)	5.9 % (17 of 289)
Sidechain	1.0 % (6 of 623)	1.0 % (6 of 623)
Aromatic	0.0 % (0 of 55)	0.0 % (0 of 55)
Methyl	1.3 % (1 of 75)	1.3 % (1 of 75)

1. micrococcal nuclease

ATSTKKLHKE PATLIKAIDG DTVKLMYKGQ PMTFRLLLVD TPETKHPKKG VEKYGPEASA FTKKMVENAK KIEVEFDKGQ RTDKYGRGLA YIYADGKMVN EALVRQGLAK VAYVYKPNNT HEQLLRKSEA QAKKEKLNIW SED

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Sample

Temperature 318 K, pH 5.1

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Release date

1995-07-30

Citation

Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary complex
Wang, J., Hinck, A.P., Loh, S.N., LeMaster, D.M., Markley, J.L.
Biochemistry (1992), 31, 921-936, PubMed 1731949 , DOI: , Abstract

Related entities 1. micrococcal nuclease, : 1 : 8 : 43 : 87 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail