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NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease
Authors
Torchia, D.A., Sparks, S.W., Bax, A.
Assembly
micrococcal nuclease
Entity
1. micrococcal nuclease (polymer), 156 monomers, 17603.95 Da Detail

MDPTVYSATS TKKLHKEPAT LIKAIDGDTV KLMYKGQPMT FRLLLVDTPE TKHPKKGVEK YGPEASAFTK KMVENAKKIE VEFNKGQRTD KYGRGLAYIY ADGKMVNEAL VRQGLAKVAY VYKPNNTHEQ HLRKSEAQAK KEKLNIWSEN DADSGQ


Formula weight
17603.95 Da
Source organism
Staphylococcus aureus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 17.3 %, Completeness: 4.6 %, Completeness (bb): 11.7 % Detail

Polymer type: polypeptide(L)

Total1H15N
All 4.6 % (53 of 1148) 2.8 % (27 of 980)15.5 % (26 of 168)
Backbone11.7 % (53 of 454) 8.5 % (26 of 305)18.1 % (27 of 149)
Sidechain 0.1 % (1 of 694) 0.1 % (1 of 675) 0.0 % (0 of 19)
Aromatic 0.0 % (0 of 62) 0.0 % (0 of 61) 0.0 % (0 of 1)
Methyl 0.0 % (0 of 77) 0.0 % (0 of 77)

1. micrococcal nuclease

MDPTVYSATS TKKLHKEPAT LIKAIDGDTV KLMYKGQPMT FRLLLVDTPE TKHPKKGVEK YGPEASAFTK KMVENAKKIE VEFNKGQRTD KYGRGLAYIY ADGKMVNEAL VRQGLAKVAY VYKPNNTHEQ HLRKSEAQAK KEKLNIWSEN DADSGQ

Sample

Temperature 309 K, pH 7.6



Release date
1995-07-30
Citation
NMR signal assignments of amide protons in the alpha-helical domains of staphylococcal nuclease
Torchia, D.A., Sparks, S.W., Bax, A.
Biochemistry (1988), 27, 5135-5141, PubMed 2844251 , DOI 10.1021/bi00414a028 ,
Related entities 1. micrococcal nuclease, : 1 : 116 entities Detail