BMRB Entry 16898
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16898
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 1H, 13C and 15N Chemical Shift Assignments for the alpha chain of human haemoglobin bound to alpha-haemoglobin stabilizing protein (AHSP) PubMed: 23696640
Deposition date: 2010-04-23 Original release date: 2010-05-27
Authors: Dickson, Claire; Gell, David
Citation: Dickson, Claire; Rich, Anne; Collins, William; Lowry, Daniel; Mollan, Jason; Khandros, Todd; Olson, Eugene; Weiss, John; Mackay, Mitchell; Lay, Joel; Gell, Peter. "-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy--hemoglobin and weakens the iron-oxygen bond." J. Biol. Chem. 288, 19986-20001 (2013).
Assembly members:
HBA1, polymer, 141 residues, Formula weight is not available
AHSP, polymer, 102 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HBA1: VLSPADKTNVKAAWGKVGAH
AGEYGAEALERMFLSFPTTK
TYFPHFDLSHGSAQVKGHGK
KVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKL
LSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKY
R
AHSP: MALLKANKDLISAGLKEFSV
LLNQQVFNDPLVSEEDMVTV
VEDWMNFYINYYRQQVTGEP
QERDKALQELRQELNTLANP
FLAKYRDFLKSHELPSHPPP
SS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 120 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 112 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alpha globin polypeptide | 1 |
| 2 | AHSP polypeptide | 2 |
Entities:
Entity 1, alpha globin polypeptide 141 residues - Formula weight is not available
| 1 | VAL | LEU | SER | PRO | ALA | ASP | LYS | THR | ASN | VAL | ||||
| 2 | LYS | ALA | ALA | TRP | GLY | LYS | VAL | GLY | ALA | HIS | ||||
| 3 | ALA | GLY | GLU | TYR | GLY | ALA | GLU | ALA | LEU | GLU | ||||
| 4 | ARG | MET | PHE | LEU | SER | PHE | PRO | THR | THR | LYS | ||||
| 5 | THR | TYR | PHE | PRO | HIS | PHE | ASP | LEU | SER | HIS | ||||
| 6 | GLY | SER | ALA | GLN | VAL | LYS | GLY | HIS | GLY | LYS | ||||
| 7 | LYS | VAL | ALA | ASP | ALA | LEU | THR | ASN | ALA | VAL | ||||
| 8 | ALA | HIS | VAL | ASP | ASP | MET | PRO | ASN | ALA | LEU | ||||
| 9 | SER | ALA | LEU | SER | ASP | LEU | HIS | ALA | HIS | LYS | ||||
| 10 | LEU | ARG | VAL | ASP | PRO | VAL | ASN | PHE | LYS | LEU | ||||
| 11 | LEU | SER | HIS | CYS | LEU | LEU | VAL | THR | LEU | ALA | ||||
| 12 | ALA | HIS | LEU | PRO | ALA | GLU | PHE | THR | PRO | ALA | ||||
| 13 | VAL | HIS | ALA | SER | LEU | ASP | LYS | PHE | LEU | ALA | ||||
| 14 | SER | VAL | SER | THR | VAL | LEU | THR | SER | LYS | TYR | ||||
| 15 | ARG |
Entity 2, AHSP polypeptide 102 residues - Formula weight is not available
| 1 | MET | ALA | LEU | LEU | LYS | ALA | ASN | LYS | ASP | LEU | ||||
| 2 | ILE | SER | ALA | GLY | LEU | LYS | GLU | PHE | SER | VAL | ||||
| 3 | LEU | LEU | ASN | GLN | GLN | VAL | PHE | ASN | ASP | PRO | ||||
| 4 | LEU | VAL | SER | GLU | GLU | ASP | MET | VAL | THR | VAL | ||||
| 5 | VAL | GLU | ASP | TRP | MET | ASN | PHE | TYR | ILE | ASN | ||||
| 6 | TYR | TYR | ARG | GLN | GLN | VAL | THR | GLY | GLU | PRO | ||||
| 7 | GLN | GLU | ARG | ASP | LYS | ALA | LEU | GLN | GLU | LEU | ||||
| 8 | ARG | GLN | GLU | LEU | ASN | THR | LEU | ALA | ASN | PRO | ||||
| 9 | PHE | LEU | ALA | LYS | TYR | ARG | ASP | PHE | LEU | LYS | ||||
| 10 | SER | HIS | GLU | LEU | PRO | SER | HIS | PRO | PRO | PRO | ||||
| 11 | SER | SER |
Samples:
sample_1: HBA1, [U-98% 13C; U-98% 15N], 0.6 – 1 mM; AHSP0.6 – 1 mM; D2O 7%; DSS 40 uM; H2O 93%; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin, Goddard - chemical shift assignment, collection
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts