Mass: 2383.698 Da / Num. of mol.: 1 / Fragment: Insulin A chain, residues 90-110 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: INS / Plasmid: pBR322 / Production host: Escherichia coli (E. coli) / References: UniProt: P01308
#2: Protein/peptide
Insulin
Mass: 3410.894 Da / Num. of mol.: 1 / Fragment: Insulin B chain, residues 25-54 / Mutation: HIS10ASP, GLU21DGL, PRO28LYS, LYS29PRO Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: INS / Plasmid: pBR322 / Production host: Escherichia coli (E. coli) / References: UniProt: P01308
Compound details
INSULIN B-CHAIN MADE VIA SEMI-SYNTHESIS: EXPRESSED INSULIN B-CHAIN WAS DIGEST THEN MERGED WITH ...INSULIN B-CHAIN MADE VIA SEMI-SYNTHESIS: EXPRESSED INSULIN B-CHAIN WAS DIGEST THEN MERGED WITH ORGANIC SYNTHESIZED PART OF B-CHAIN (CONTAINED B21-D-GLU).
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D TOCSY
1
2
1
NOESY
1
3
1
COSY
NMR details
Text: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR NMR TECHNIQUES.
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Sample preparation
Details
Contents: 0.5 mM INSULIN A CHAIN, 0.5 mM INSULIN B CHAIN, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)
Component
Solution-ID
0.5mM
INSULIN A CHAIN-1
1
0.5mM
INSULIN B CHAIN-2
1
Sample conditions
Conditions-ID
Ionic strength
pH
Pressure (kPa)
Temperature (K)
1
0.1
7.0
1bar
298K
2
0.1
2.0
1bar
298K
3
0.1
7.6
1bar
305K
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NMR measurement
NMR spectrometer
Type: BRUKER DRX / Manufacturer: Bruker / Model: DRX / Field strength: 700 MHz
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Processing
NMR software
Name
Version
Developer
Classification
X-PLOR
3.85
BRUNGER
refinement
XwinNMR
3.5
BrukerBiospin
structuresolution
Refinement
Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 Details: RMSD VALUES FOR ALL 20 STRUCTURES VERSUS GEOMETRIC AVERAGE: (BACKBONE, A2-A20, B4-B24) 0.42 ANGSTROM
NMR representative
Selection criteria: closest to the average
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 20
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