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Backbone 1H, 13C and 15N Chemical Shift Assignments for the alpha chain of human haemoglobin bound to alpha-haemoglobin stabilizing protein (AHSP)
Authors
Dickson, C.F., Gell, D.A.
Assembly
alpha-haemoglobin:AHSP protein complex
Entity
1. HBA1 (polymer, Thiol state: all free), 141 monomers, 15126.15 Da Detail

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


2. AHSP (polymer, Thiol state: not present), 102 monomers, 11840.26 Da Detail

MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS


Total weight
26966.41 Da
Max. entity weight
15126.15 Da
Source organism
Homo sapiens
Exptl. method
SOLUTION NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 49.0 %, Completeness: 14.4 %, Completeness (bb): 25.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All14.4 % (409 of 2833)10.0 % (146 of 1456)13.0 % (146 of 1120)45.5 % (117 of 257)
Backbone25.6 % (364 of 1421)24.4 % (115 of 472)18.5 % (133 of 720)50.7 % (116 of 229)
Sidechain 3.6 % (59 of 1646) 3.2 % (31 of 984) 4.3 % (27 of 634) 3.6 % (1 of 28)
Aromatic 0.0 % (0 of 248) 0.0 % (0 of 124) 0.0 % (0 of 122) 0.0 % (0 of 2)
Methyl 7.8 % (23 of 294) 6.1 % (9 of 147) 9.5 % (14 of 147)

1. HBA1

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

2. AHSP

MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS

Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0


#NameIsotope labelingTypeConcentration
1HBA1[U-98% 13C; U-98% 15N]0.6 ~ 1.0 mM
2AHSPnatural abundance0.6 ~ 1.0 mM
3D2Onatural abundance7 %
4DSSnatural abundance40 uM
5H2Onatural abundance93 %
6sodium phosphatenatural abundance20 mM

Release date
2010-05-26
Citation
α-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy-α-hemoglobin and weakens the iron-oxygen bond
Dickson, C.F., Rich, A.M., Collins, W.M.H., Lowry, D.A.T., Mollan, J.A., Khandros, T.L., Olson, E., Weiss, J.S., Mackay, M.J., Lay, J.P., Gell, P.A.
J. Biol. Chem. (2013), 288, 19986-20001, PubMed 23696640 , DOI 10.1074/jbc.M112.437509 ,
Related entities 1. HBA1, : 3 : 5 entities Detail
Related entities 2. AHSP, : 1 : 1 : 7 : 2 entities Detail
Interaction partners 2. AHSP, : 6 interactors Detail
Experiments performed 4 experiments Detail