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- PDB-1guj: Insulin at pH 2: structural analysis of the conditions promoting ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1guj | ||||||
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Title | Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation. | ||||||
![]() | (INSULIN![]() | ||||||
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Function / homology | ![]() Signaling by Insulin receptor / alpha-beta T cell activation / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / IRS activation / Insulin processing / negative regulation of NAD(P)H oxidase activity / Insulin receptor recycling / nitric oxide-cGMP-mediated signaling pathway / negative regulation of fatty acid metabolic process ...Signaling by Insulin receptor / alpha-beta T cell activation / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / IRS activation / Insulin processing / negative regulation of NAD(P)H oxidase activity / Insulin receptor recycling / nitric oxide-cGMP-mediated signaling pathway / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Whittingham, J.L. / Scott, D.J. / Chance, K. / Wilson, A. / Finch, J. / Brange, J. / Dodson, G.G. | ||||||
![]() | ![]() Title: Insulin at Ph2: Structural Analysis of the Conditions Promoting Insulin Fibre Formation Authors: Whittingham, J.L. / Scott, D.J. / Chance, K. / Wilson, A. / Finch, J. / Brange, J. / Dodson, G.G. #1: ![]() Title: Structure of an Insulin Dimer in an Orthorhombic Crystal: The Structure Analysis of a Human Insulin Mutant (B9 Ser to Glu) Authors: Yao, Z.-P. / Zeng, Z.-H. / Li, H.-M. / Zhang, Y. / Feng, Y.-M. / Wang, D.-C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.8 KB | Display | ![]() |
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PDB format | ![]() | 44.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 250 KB | Display | ![]() |
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Full document | ![]() | 250 KB | Display | |
Data in XML | ![]() | 3.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4insS ![]() 1vks 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99815, 0.00858, -0.06016), Vector: |
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Components
#1: Protein/peptide | ![]() Mass: 2383.698 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein/peptide | ![]() Mass: 3433.953 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #3: Chemical | ![]() #4: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 45 % | |||||||||||||||||||||
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Crystal grow![]() | Method: vapor diffusion, hanging drop / pH: 2.1 Details: HANGING DROP VAPOUR DIFFUSION METHOD PROTEIN SOL: 5 MG/ML HUMAN INSULIN IN SULPHURIC ACID PH 2.1 RESERVOIR SOL: SULPHURIC ACID PH 2.1,0.025 M SODIUM SULPHATE | |||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.63→20 Å / Num. obs: 13079 / % possible obs: 100 % / Redundancy: 5 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 36 |
Reflection shell | Resolution: 1.63→1.66 Å / Redundancy: 5 % / Rmerge(I) obs: 0.245 / Mean I/σ(I) obs: 9 / % possible all: 100 |
Reflection | *PLUS % possible obs: 91 % / Redundancy: 5.3 % |
Reflection shell | *PLUS % possible obs: 76.5 % / Rmerge(I) obs: 0.25 / Mean I/σ(I) obs: 9.2 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 4INS Resolution: 1.62→34.3 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.951 / SU B: 4.041 / SU ML: 0.058 / Cross valid method: THROUGHOUT / ESU R: 0.123 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.74 Å2
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Refinement step | Cycle: LAST / Resolution: 1.62→34.3 Å
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Refine LS restraints |
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