BMRB: 188

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: 7.1 %, Completeness: 2.6 %, Completeness (bb): 3.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	2.6 % (25 of 980)	2.6 % (25 of 980)
Backbone	3.2 % (10 of 315)	3.2 % (10 of 315)
Sidechain	2.3 % (15 of 665)	2.3 % (15 of 665)
Aromatic	0.0 % (0 of 61)	0.0 % (0 of 61)
Methyl	14.3 % (11 of 77)	14.3 % (11 of 77)

1. micrococcal nuclease

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

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Sample

Temperature 309 K, pH 7.6

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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 , Abstract

Related entities 1. micrococcal nuclease, : 1 : 129 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail