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1H Chemical Shift Assignments for the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin
Authors
Tran, A.T., Kolczak, U., La Mar, G.N.
Assembly
human hemglobin A
Entity
1. human adult hemoglobin (polymer, Thiol state: all free), 146 monomers, 15867.00 × 4 Da Detail

VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK EFTPPVQAAY QKVVAGVANA LAHKYH


2. PROTOPORPHYRIN IX CONTAINING FE (non-polymer), 1 monomers, na Da
3. CYANIDE ION (non-polymer), 26.017 Da
Total weight
63494.016 Da
Max. entity weight
15867.0 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 74.0 %, Completeness: 49.2 %, Completeness (bb): 71.6 % Detail

Polymer type: polypeptide(L)

Total1H
All49.2 % (421 of 855)49.2 % (421 of 855)
Backbone71.6 % (204 of 285)71.6 % (204 of 285)
Sidechain38.1 % (217 of 570)38.1 % (217 of 570)
Aromatic30.5 % (25 of 82)30.5 % (25 of 82)
Methyl58.5 % (55 of 94)58.5 % (55 of 94)

1. human adult hemoglobin

VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK EFTPPVQAAY QKVVAGVANA LAHKYH

Sample

Temperature 303 (±1) K, Details Human Hb A was isolated and purified from human blood, and subunit separation were carried out following standard procedures. Cyanomet complexes were prepared by oxidizing the the oxyhemoglobin with potassium ferricyanide, followed by chromatography.


#NameIsotope labelingTypeConcentration
1human adult hemoglobin2 mM

Chem. Shift Complete2
Sequence coverage: 6.8 %, Completeness: 26.9 %, Completeness (bb): 39.3 % Detail

Polymer type: polypeptide(L)

Total1H
All26.9 % (460 of 1710)26.9 % (460 of 1710)
Backbone39.3 % (224 of 570)39.3 % (224 of 570)
Sidechain20.8 % (237 of 1140)20.8 % (237 of 1140)
Aromatic15.2 % (25 of 164)15.2 % (25 of 164)
Methyl31.9 % (60 of 188)31.9 % (60 of 188)

1. human adult hemoglobin

VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK EFTPPVQAAY QKVVAGVANA LAHKYH

Sample

Temperature 303 (±1) K, Details Human Hb A was isolated and purified from human blood, and subunit separation were carried out following standard procedures. Cyanomet complexes were prepared by oxidizing the the oxyhemoglobin with potassium ferricyanide, followed by chromatography.


#NameIsotope labelingTypeConcentration
1human adult hemoglobin2 mM

Chem. Shift Complete3
Sequence coverage: 74.7 %, Completeness: 33.9 %, Completeness (bb): 50.3 % Detail

Polymer type: polypeptide(L)

Total1H
All33.9 % (869 of 2565)33.9 % (869 of 2565)
Backbone50.3 % (430 of 855)50.3 % (430 of 855)
Sidechain25.7 % (440 of 1710)25.7 % (440 of 1710)
Aromatic19.9 % (49 of 246)19.9 % (49 of 246)
Methyl40.8 % (115 of 282)40.8 % (115 of 282)

1. human adult hemoglobin

VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK EFTPPVQAAY QKVVAGVANA LAHKYH

Sample

Temperature 303 (±1) K, Details Human Hb A was isolated and purified from human blood, and subunit separation were carried out following standard procedures. Cyanomet complexes were prepared by oxidizing the the oxyhemoglobin with potassium ferricyanide, followed by chromatography.


#NameIsotope labelingTypeConcentration
1human adult hemoglobin2 mM

Chem. Shift Complete4
Sequence coverage: 3.4 %, Completeness: 25.8 %, Completeness (bb): 38.5 % Detail

Polymer type: polypeptide(L)

Total1H
All25.8 % (884 of 3420)25.8 % (884 of 3420)
Backbone38.5 % (439 of 1140)38.5 % (439 of 1140)
Sidechain19.6 % (446 of 2280)19.6 % (446 of 2280)
Aromatic14.9 % (49 of 328)14.9 % (49 of 328)
Methyl30.9 % (116 of 376)30.9 % (116 of 376)

1. human adult hemoglobin

VHLTPEEKSA VTALWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLST PDAVMGNPKV KAHGKKVLGA FSDGLAHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGK EFTPPVQAAY QKVVAGVANA LAHKYH

Sample

Temperature 303 (±1) K, Details Human Hb A was isolated and purified from human blood, and subunit separation were carried out following standard procedures. Cyanomet complexes were prepared by oxidizing the the oxyhemoglobin with potassium ferricyanide, followed by chromatography.


#NameIsotope labelingTypeConcentration
1human adult hemoglobin2 mM

Release date
2004-06-10
Citation
Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin
Tran, A.T., Kolczak, U., La Mar, G.N.
Biochim. Biophys. Acta (2004), 1701, 75-87, PubMed 15450177 , DOI 10.1016/j.bbapap.2004.06.003 ,
Related entities 1. human adult hemoglobin, : 1 : 102 : 1 : 6 : 98 entities Detail
Interaction partners 1. human adult hemoglobin, : 11 interactors Detail
Experiments performed 4 experiments Detail
Keywords NMR, b-chain, contact shift, dipolar shift, hemoglobin A, magnetic axes