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1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers
Authors
Hauksson, J.B., La Mar, G.N., Pande, U., Pandey, R.K., Parish, D.W., Singh, J.P., Smith, K.M.
Assembly
myoglobin
Entity
1. myoglobin (polymer), 153 monomers, 17199.65 Da Detail

VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED LKKHGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP GDFGADAQGA MNKALELFRK DIAAKYKELG YQG


Formula weight
17199.65 Da
Source organism
Physeter catodon
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 5.9 %, Completeness: 2.9 %, Completeness (bb): 3.0 % Detail

Polymer type: polypeptide(L)

Total1H
All 2.9 % (28 of 953) 2.9 % (28 of 953)
Backbone 3.0 % (9 of 302) 3.0 % (9 of 302)
Sidechain 3.1 % (20 of 651) 3.1 % (20 of 651)
Aromatic 6.4 % (5 of 78) 6.4 % (5 of 78)
Methyl 6.5 % (6 of 92) 6.5 % (6 of 92)

1. myoglobin

VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED LKKHGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP GDFGADAQGA MNKALELFRK DIAAKYKELG YQG

Sample

Temperature 298 K, pH 8.6



Release date
1995-07-30
Citation
1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers
Hauksson, J.B., La Mar, G.N., Pande, U., Pandey, R.K., Parish, D.W., Singh, J.P., Smith, K.M.
Biochim. Biophys. Acta (1990), 1041, 186-194, PubMed 2265204 , DOI 10.1016/0167-4838(90)90064-m ,
Related entities 1. myoglobin, : 1 : 93 : 7 : 101 entities Detail
Interaction partners 1. myoglobin, : 2 interactors Detail
Experiments performed 1 experiments Detail