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- PDB-1b2g: PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN... -

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Basic information

Entry
Database: PDB / ID: 1b2g
TitlePH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 9.00 COORDINATES)
Components
  • PROTEIN (INSULIN a chain)
  • PROTEIN (INSULIN b chain)
KeywordsHORMONE/GROWTH FACTOR / HORMONE / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


glycoprotein biosynthetic process / lactate biosynthetic process / positive regulation of lipoprotein lipase activity / positive regulation of fatty acid biosynthetic process / response to L-arginine / lipoprotein biosynthetic process / positive regulation of glucose metabolic process / lipid biosynthetic process / alpha-beta T cell activation / negative regulation of glycogen catabolic process ...glycoprotein biosynthetic process / lactate biosynthetic process / positive regulation of lipoprotein lipase activity / positive regulation of fatty acid biosynthetic process / response to L-arginine / lipoprotein biosynthetic process / positive regulation of glucose metabolic process / lipid biosynthetic process / alpha-beta T cell activation / negative regulation of glycogen catabolic process / 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 / positive regulation of respiratory burst / negative regulation of respiratory burst involved in inflammatory response / negative regulation of gluconeogenesis / regulation of cellular amino acid metabolic process / negative regulation of acute inflammatory response / negative regulation of reactive oxygen species biosynthetic process / regulation of protein localization to plasma membrane / positive regulation of dendritic spine maintenance / positive regulation of glycogen biosynthetic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of protein secretion / negative regulation of lipid catabolic process / fatty acid homeostasis / positive regulation of insulin receptor signaling pathway / neuron projection maintenance / insulin-like growth factor receptor binding / positive regulation of DNA replication / positive regulation of protein autophosphorylation / positive regulation of glycolytic process / regulation of transmembrane transporter activity / positive regulation of mitotic nuclear division / positive regulation of cytokine production / acute-phase response / activation of protein kinase B activity / positive regulation of glucose import / hormone activity / negative regulation of proteolysis / negative regulation of protein catabolic process / insulin receptor binding / positive regulation of protein localization to nucleus / insulin receptor signaling pathway / vasodilation / glucose metabolic process / glucose homeostasis / wound healing / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase signaling / protease binding / positive regulation of NF-kappaB transcription factor activity / positive regulation of protein kinase B signaling / positive regulation of cell migration / G protein-coupled receptor signaling pathway / positive regulation of cell population proliferation / extracellular space / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin-like superfamily / Insulin family signature.
Similarity search - Domain/homology
Biological speciesSus scrofa (pig)
MethodX-RAY DIFFRACTION / OTHER / Resolution: 1.8 Å
AuthorsDiao, J.S. / Caspar, D.L.D.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 2003
Title: Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding.
Authors: Diao, J.
#1: Journal: Biophys.J. / Year: 1992
Title: Conformational Changes in Cubic Insulin Crystals in the Ph Range 7-11
Authors: Gursky, O. / Badger, J. / Li, Y. / Caspar, D.L.
#2: Journal: Biophys.J. / Year: 1992
Title: Monovalent Cation Binding in Cubic Insulin Crystals
Authors: Gursky, O. / Li, Y. / Badger, J. / Caspar, D.L.
#3: Journal: Biophys.J. / Year: 1992
Title: Flexibility in Crystalline Insulins
Authors: Badger, J.
#4: Journal: Acta Crystallogr.,Sect.B / Year: 1991
Title: Structure of the Pig Insulin Dimer in the Cubic Crystal
Authors: Badger, J. / Harris, M.R. / Reynolds, C.D. / Evans, A.C. / Dodson, E.J. / Dodson, G.G. / North, A.C.T.
#5: Journal: Proc.Natl.Acad.Sci.USA / Year: 1991
Title: Water Structure in Cubic Insulin Crystals
Authors: Badger, J. / Caspar, D.L.
#6: Journal: J.Mol.Biol. / Year: 1978
Title: Zinc-Free Cubic Pig Insulin: Crystallization and Structure Determination
Authors: Dodson, E.J. / Dodson, G.G. / Lewitova, A. / Sabesan, M.
History
DepositionNov 26, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Apr 8, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (INSULIN a chain)
B: PROTEIN (INSULIN b chain)


Theoretical massNumber of molelcules
Total (without water)5,7882
Polymers5,7882
Non-polymers00
Water88349
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1550 Å2
ΔGint-14 kcal/mol
Surface area3420 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)78.870, 78.870, 78.870
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number199
Space group name H-MI213
Components on special symmetry positions
IDModelComponents
11B-60-

HOH

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Components

#1: Protein/peptide PROTEIN (INSULIN a chain)


Mass: 2383.698 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: PANCREAS / References: UniProt: P01315
#2: Protein/peptide PROTEIN (INSULIN b chain)


Mass: 3403.927 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: PANCREAS / References: UniProt: P01315
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 49 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.53 Å3/Da / Density % sol: 65 %
Crystal growpH: 9 / Details: pH 9.00
Components of the solutionsName: 1M SODIUM SULFATE SOLUTION AT PH 9.00
Crystal grow
*PLUS
pH: 9.2 / Method: microdialysis
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
10.05 Msodium phosphate11
20.001 Msodium EDTA11pH11
318 mg/mlprotein11
40.15 Msodium phosphate12
50.001 Msodium EDTA12pH9.2

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Data collection

DiffractionMean temperature: 287 K
Diffraction sourceWavelength: 1.5418
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.7→55 Å / Num. obs: 8672 / % possible obs: 94.8 % / Redundancy: 4 % / Biso Wilson estimate: 21.33 Å2 / Rsym value: 0.065
Reflection
*PLUS
Highest resolution: 1.8 Å / % possible obs: 94.85 % / Rmerge(I) obs: 0.065

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
X-PLORmodel building
X-PLOR3.843refinement
X-PLORphasing
RefinementMethod to determine structure: OTHER / Resolution: 1.8→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.226 719 9.38 %RANDOM
Rwork0.1995 ---
obs-7201 93.96 %-
Displacement parametersBiso mean: 23.81 Å2
Refinement stepCycle: LAST / Resolution: 1.8→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms409 0 0 49 458
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.006
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.15
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d22.57
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.06
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
LS refinement shellResolution: 1.8→1.84 Å / Total num. of bins used: 15
RfactorNum. reflection% reflection
Rfree0.369 42 8.66 %
Rwork0.3184 422 -
obs--95.67 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM19.SOLTOPH19.SOL
X-RAY DIFFRACTION3SO4.PARSO4.TOP
Refinement
*PLUS
Highest resolution: 1.8 Å / Lowest resolution: 10 Å / Rfactor Rfree: 0.224 / Rfactor Rwork: 0.2023
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg22.57
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.06

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