A: INSULIN A CHAIN B: INSULIN B CHAIN C: INSULIN A CHAIN D: INSULIN B CHAIN E: INSULIN A CHAIN F: INSULIN B CHAIN G: INSULIN A CHAIN H: INSULIN B CHAIN I: INSULIN A CHAIN J: INSULIN B CHAIN K: INSULIN A CHAIN L: INSULIN B CHAIN hetero molecules
Mass: 2383.698 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P01308
#2: Protein/peptide
INSULINBCHAIN / NMEB25PHE-INSULIN
Mass: 3447.980 Da / Num. of mol.: 6 / Source method: obtained synthetically / Details: THE N-PEPTIDE ATOM OF PHE 25 IS METHYLATED / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P01308
Mass: 18.015 Da / Num. of mol.: 106 / Source method: isolated from a natural source / Formula: H2O
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Details
Sequence details
THIS IS A FULL LENGTH HUMAN INSULIN ANALOGUE WITH THE N-PEPTIDE ATOM OF BETA CHAIN RESIDUE 25 ...THIS IS A FULL LENGTH HUMAN INSULIN ANALOGUE WITH THE N-PEPTIDE ATOM OF BETA CHAIN RESIDUE 25 METHYLATED (MEA).
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.4 Å3/Da / Density % sol: 48 % / Description: NONE
Crystal grow
pH: 8.2 Details: 0.6 M NA2SO4, 0.3 M TRIS PH 8.2, 0.6 M ZN(AC)2, 0.06% PHENOL.
Resolution: 1.9→54.29 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.915 / SU B: 5.313 / SU ML: 0.152 / Cross valid method: THROUGHOUT / ESU R: 0.194 / ESU R Free: 0.183 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES REFINED INDIVIDUALLY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.28143
1205
5.2 %
RANDOM
Rwork
0.22341
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obs
0.22649
22062
94.59 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK