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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: 83.9 %, Completeness: 78.4 %, Completeness (bb): 87.6 % Detail

Polymer type: polypeptide(L)

Total15N
All78.4 % (120 of 153)78.4 % (120 of 153)
Backbone87.6 % (120 of 137)87.6 % (120 of 137)
Sidechain 0.0 % (0 of 16) 0.0 % (0 of 16)
Aromatic 0.0 % (0 of 1) 0.0 % (0 of 1)

1. micrococcal nuclease

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

Sample

Temperature 318 K, pH 5.5



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 10.1021/bi00118a039 ,
Related entities 1. micrococcal nuclease, : 1 : 7 : 43 : 73 entities Detail
Experiments performed 1 experiments Detail