BMRB: 1202

Characterization of Hydrophobic Cores in Apomyoglobin: A Proton NMR Spectroscopy Study

Authors

Cocco, M.J., Lecomte, J.T.J.

Assembly

myoglobin

Entity

1. myoglobin (polymer), 153 monomers, 16950.26 Da Detail

GLSDGEWQQV LNVWGKVEAD IAGHGQEVLI RLFTGHPETL EKFDKFKHLK TEAEMKASED LKKHGTVVLT ALGGILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISDA IIHVLHSKHP GNFGADAQGA MTKALELFRN DIAAKYKELG FQG

Formula weight

16950.26 Da

Source organism

Equus caballus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 17.0 %, Completeness: 10.8 %, Completeness (bb): 5.7 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	10.8 % (102 of 942)	10.8 % (102 of 942)
Backbone	5.7 % (18 of 317)	5.7 % (18 of 317)
Sidechain	13.4 % (84 of 625)	13.4 % (84 of 625)
Aromatic	54.5 % (42 of 77)	54.5 % (42 of 77)
Methyl	14.8 % (13 of 88)	14.8 % (13 of 88)

1. myoglobin

GLSDGEWQQV LNVWGKVEAD IAGHGQEVLI RLFTGHPETL EKFDKFKHLK TEAEMKASED LKKHGTVVLT ALGGILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISDA IIHVLHSKHP GNFGADAQGA MTKALELFRN DIAAKYKELG FQG

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Sample

Temperature 298 K, pH 5.7

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Release date

1995-07-30

Citation

Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study
Cocco, M.J., Lecomte, J.T.J.
Biochemistry (1990), 29, 11067-11072, PubMed 2176892 , DOI: , Abstract

Related entities 1. myoglobin, : 1 : 52 : 196 entities Detail

Interaction partners 1. myoglobin, : 2 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail