Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16026
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Citation: Hua, Q.; Xu, B.; Huang, K.; Hu, S.; Nakarawa, S.; Jia, W.; Wang, S.; Wittaker, J.; Katsoyannis, P.; Weiss, M.. "Enhancing the activity of a protein by stereospecific unfolding. The conformational life cycle of insulin and its evolutionary origins." J. Biol. Chem. 284, 14586-14596 (2009).
PubMed: 19321436
Assembly members:
INSULIN_A_CHAIN, polymer, 21 residues, 2383.700 Da.
INSULIN_B_CHAIN, polymer, 30 residues, 3334.823 Da.
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 Vector: pBR322
Entity Sequences (FASTA):
INSULIN_A_CHAIN: GIVEQCCTSICSLYQLENYC
N
INSULIN_B_CHAIN: FVNQHLCGSDLVEALYLVCG
ERGXFYTKPT
Data type | Count |
1H chemical shifts | 337 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | INSULIN A CHAIN | 1 |
2 | INSULIN B CHAIN | 2 |
Entity 1, INSULIN A CHAIN 21 residues - 2383.700 Da.
1 | GLY | ILE | VAL | GLU | GLN | CYS | CYS | THR | SER | ILE | ||||
2 | CYS | SER | LEU | TYR | GLN | LEU | GLU | ASN | TYR | CYS | ||||
3 | ASN |
Entity 2, INSULIN B CHAIN 30 residues - 3334.823 Da.
1 | PHE | VAL | ASN | GLN | HIS | LEU | CYS | GLY | SER | ASP | |
2 | LEU | VAL | GLU | ALA | LEU | TYR | LEU | VAL | CYS | GLY | |
3 | GLU | ARG | GLY | DAL | PHE | TYR | THR | LYS | PRO | THR |
sample: INSULIN A CHAIN 0.5-0.8 mM; INSULIN B CHAIN 0.5-0.8 mM; H2O 90%; D2O 10%; ACETIC ACID 20%
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D TOCSY | sample | isotropic | sample_conditions_1 |
NOESY | sample | isotropic | sample_conditions_1 |
COSY | sample | isotropic | sample_conditions_1 |
X-PLOR v3.85, BRUNGER, A.T. ET AL. - refinement
VNMR_6.1B v6.1B, Varian - structure solution