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Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins
Authors
Nagai, K., La Mar, G.N., Jue, T., Bunn, H.FRANKLIN.
Assembly
hemoglobin A alpha chain
Entity
1. hemoglobin A alpha chain (polymer), 141 monomers, 15126.15 Da Detail

VLSPADKTNV KAAWGKVGAH AGEYGAEALE RMFLSFPTTK TYFPHFDLSH GSAQVKGHGK KVADALTNAV AHVDDMPNAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHLPAEFTPA VHASLDKFLA SVSTVLTSKY R


Formula weight
15126.15 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 3.5 %, Completeness: 2.1 %, Completeness (bb): 2.5 % Detail

Polymer type: polypeptide(L)

Total1H
All 2.1 % (17 of 804) 2.1 % (17 of 804)
Backbone 2.5 % (7 of 282) 2.5 % (7 of 282)
Sidechain 1.9 % (10 of 522) 1.9 % (10 of 522)
Aromatic 5.5 % (4 of 73) 5.5 % (4 of 73)
Methyl 0.0 % (0 of 92) 0.0 % (0 of 92)

1. hemoglobin A alpha chain

VLSPADKTNV KAAWGKVGAH AGEYGAEALE RMFLSFPTTK TYFPHFDLSH GSAQVKGHGK KVADALTNAV AHVDDMPNAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHLPAEFTPA VHASLDKFLA SVSTVLTSKY R

Sample

Temperature 298 K, pH 6.5



Release date
1995-07-30
Citation
Proton magnetic resonance investigation of the influence of quaternary structure on iron-histidine bonding in deoxyhemoglobins
Nagai, K., La Mar, G.N., Jue, T., Bunn, H.FRANKLIN.
Biochemistry (1982), 21, 842-847, PubMed 7074055 ,
Related entities 1. hemoglobin A alpha chain, : 1 : 101 : 1 : 6 : 150 entities Detail
Interaction partners 1. hemoglobin A alpha chain, : 32 interactors Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail