A: Insulin B chain,Insulin A chain B: Insulin B chain,Insulin A chain C: Insulin B chain,Insulin A chain D: Insulin B chain,Insulin A chain E: Insulin B chain,Insulin A chain F: Insulin B chain,Insulin A chain hetero molecules
Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: PHE / Beg label comp-ID: PHE / End auth comp-ID: ASN / End label comp-ID: ASN / Auth seq-ID: 1 - 49 / Label seq-ID: 1 - 49
Dom-ID
Selection details
Auth asym-ID
Label asym-ID
1
chainA
A
A
2
chainB
B
B
3
chainC
C
C
4
chainD
D
D
5
chainE
E
E
6
chainF
F
F
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Components
#1: Protein/peptide
InsulinBchain,InsulinAchain
Mass: 5601.417 Da / Num. of mol.: 6 Mutation: Residues corresponding to B chain amino acids 29-30 were deleted, and Pro-28 was mutated to Lys. This, in effect, is the equivalent of deleting only residues 28 and 30 of the wild-type B chain. Source method: obtained synthetically Details: This is a fusion protein consisting of a mutant insulin B chain followed by the insulin A chain. Six of these fusion chains are in the asymmetric unit Source: (synth.) Homo sapiens (human) / References: UniProt: P01308
Mass: 18.015 Da / Num. of mol.: 77 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interest
N
Sequence details
This construct contains a mutant of the naturally occurring insulin B chain and the wild-type ...This construct contains a mutant of the naturally occurring insulin B chain and the wild-type naturally occurring A chain fused together into one peptide chain.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 1.96 Å3/Da / Density % sol: 37.11 %
Crystal grow
Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 1:2.5 ratio of Zn2+ to protein monomer in 0.02M Tris-HCl, 0.05M sodium citrate, 5% acetone, 0.03% phenol, 0.01% zinc acetate, PH 8.0
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Data collection
Diffraction
Mean temperature: 100 K / Serial crystal experiment: N
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