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Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex
Authors
Wang, J., 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: 88.8 %, Completeness: 51.1 %, Completeness (bb): 50.2 % Detail

Polymer type: polypeptide(L)

Total1H
All51.1 % (466 of 912)51.1 % (466 of 912)
Backbone50.2 % (145 of 289)50.2 % (145 of 289)
Sidechain51.5 % (321 of 623)51.5 % (321 of 623)
Aromatic90.9 % (50 of 55)90.9 % (50 of 55)
Methyl69.3 % (52 of 75)69.3 % (52 of 75)

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
Two-dimensional NMR studies of staphylococcal nuclease. 1. Sequence-specific assignments of hydrogen-1 signals and solution structure of the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex
Wang, J., LeMaster, D.M., Markley, J.L.
Biochemistry (1990), 29, 88-101, PubMed 2108720 , DOI: ,
Related entities 1. micrococcal nuclease, : 1 : 8 : 43 : 87 entities Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail