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- PDB-3zs2: TyrB25,NMePheB26,LysB28,ProB29-insulin analogue crystal structure -
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Open data
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Basic information
Entry | Database: PDB / ID: 3zs2 | |||||||||
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Title | TyrB25,NMePheB26,LysB28,ProB29-insulin analogue crystal structure | |||||||||
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Function / homology | ![]() Signaling by Insulin receptor / negative regulation of glycogen catabolic process / alpha-beta T cell activation / regulation of cellular amino acid metabolic process / IRS activation / Insulin processing / Insulin receptor recycling / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of fatty acid metabolic process ...Signaling by Insulin receptor / negative regulation of glycogen catabolic process / alpha-beta T cell activation / regulation of cellular amino acid metabolic process / IRS activation / Insulin processing / Insulin receptor recycling / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Antolikova, E. / Zakova, L. / Turkenburg, J.P. / Watson, C.J. / Hanclova, I. / Sanda, M. / Cooper, A. / Kraus, T. / Brzozowski, A.M. / Jiracek, J.A. | |||||||||
![]() | ![]() Title: Non-Equivalent Role of Inter- and Intramolecular Hydrogen Bonds in the Insulin Dimer Interface. Authors: Antolikova, E. / Zakova, L. / Turkenburg, J.P. / Watson, C.J. / Hanclova, I. / Sanda, M. / Cooper, A. / Kraus, T. / Brzozowski, A.M. / Jiracek, J.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.4 KB | Display | ![]() |
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PDB format | ![]() | 61.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 399.7 KB | Display | ![]() |
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Full document | ![]() | 760.9 KB | Display | |
Data in XML | ![]() | 69.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3zqrC ![]() 1ms0S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein/peptide , 2 types, 12 molecules ACEGIKBDFHJL
#1: Protein/peptide | Mass: 2383.698 Da / Num. of mol.: 6 / Mutation: YES / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #2: Protein/peptide | Mass: 3447.980 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
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-Non-polymers , 4 types, 160 molecules 






#3: Chemical | ChemComp-IPH / ![]() #4: Chemical | ![]() #5: Chemical | #6: Water | ChemComp-HOH / | ![]() |
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-Details
Sequence details | THE N-PEPTIDE ATOM OF B26PHE IS METHYLATED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48 % / Description: NONE |
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Crystal grow![]() | pH: 8.2 Details: 0.1 M NACITRATE, 0.3 M TRIS PH 8.2, 0.6 MM ZN(AC)2, 0.06% PHENOL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 3, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.97→50 Å / Num. obs: 18615 / % possible obs: 90.2 % / Observed criterion σ(I): 0 / Redundancy: 2.3 % / Biso Wilson estimate: 30.7 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 1.97→2.04 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 8.5 / % possible all: 61.7 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1MS0 Resolution: 1.97→53.68 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.921 / SU B: 4.412 / SU ML: 0.127 / Cross valid method: THROUGHOUT / ESU R: 0.21 / ESU R Free: 0.19 / 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
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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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.213 Å2
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Refinement step | Cycle: LAST / Resolution: 1.97→53.68 Å
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Refine LS restraints |
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