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- PDB-5d54: In meso X-ray crystallography structure of insulin at 100 K -

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Basic information

Entry
Database: PDB / ID: 5d54
TitleIn meso X-ray crystallography structure of insulin at 100 K
Components
  • Insulin A chain
  • Insulin B chain
KeywordsHORMONE
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 / negative regulation of glycogen catabolic process / alpha-beta T cell activation ...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 / negative regulation of glycogen catabolic process / alpha-beta T cell activation / regulation of cellular amino acid metabolic 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 / negative regulation of acute inflammatory response / positive regulation of dendritic spine maintenance / fatty acid homeostasis / positive regulation of glycogen biosynthetic process / regulation of protein localization to plasma membrane / negative regulation of reactive oxygen species biosynthetic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of protein secretion / negative regulation of lipid catabolic process / 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 / positive regulation of mitotic nuclear division / regulation of transmembrane transporter activity / activation of protein kinase B activity / positive regulation of cytokine production / positive regulation of glucose import / acute-phase response / hormone activity / negative regulation of proteolysis / negative regulation of protein catabolic process / insulin receptor signaling pathway / insulin receptor binding / positive regulation of protein localization to nucleus / vasodilation / glucose metabolic process / glucose homeostasis / wound healing / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of phosphatidylinositol 3-kinase signaling / positive regulation of MAPK cascade / protease binding / positive regulation of protein kinase B signaling / positive regulation of NF-kappaB transcription factor activity / G protein-coupled receptor signaling pathway / positive regulation of cell migration / positive regulation of cell population proliferation / extracellular space / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin-like superfamily / Insulin family signature.
Similarity search - Domain/homology
PHOSPHATE ION / Insulin
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsHuang, C.-Y. / Olieric, V. / Wang, M. / Caffrey, M.
Funding support Ireland, 1items
OrganizationGrant numberCountry
Science Foundation Ireland12/IA/1255 Ireland
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2016
Title: In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures.
Authors: Huang, C.Y. / Olieric, V. / Ma, P. / Howe, N. / Vogeley, L. / Liu, X. / Warshamanage, R. / Weinert, T. / Panepucci, E. / Kobilka, B. / Diederichs, K. / Wang, M. / Caffrey, M.
History
DepositionAug 10, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jan 13, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 2, 2016Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Insulin B chain
B: Insulin A chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)6,3765
Polymers5,7882
Non-polymers5883
Water70339
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2100 Å2
ΔGint-15 kcal/mol
Surface area3630 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)77.510, 77.510, 77.510
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-102-

PO4

21B-102-

PO4

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Components

#1: Protein/peptide Insulin B chain


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


Mass: 3403.927 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P01315
#3: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#4: Chemical ChemComp-PE5 / 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL / 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, POLYETHYLENE GLYCOL PEG400 / Polyethylene glycol


Mass: 398.489 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H38O9 / Comment: precipitant*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 39 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.35 Å3/Da / Density % sol: 63.31 %
Crystal growTemperature: 293 K / Method: lipidic cubic phase
Details: 0.1-0.2 M sodium phosphate, pH 5.5-6.1, and 33-38 %(w/v) PEG400
PH range: pH 5.5-6.1

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1.03321 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 18, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03321 Å / Relative weight: 1
ReflectionResolution: 1.5→50 Å / Num. obs: 12580 / % possible obs: 99.9 % / Redundancy: 6.46 % / Net I/σ(I): 15.45
Reflection shellResolution: 1.5→1.54 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 1.49 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.9_1690refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 9ins
Resolution: 1.5→38.755 Å / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 23.48 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1883 634 5.04 %
Rwork0.1775 --
obs0.1781 12580 99.83 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.5→38.755 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms403 0 21 39 463
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.006446
X-RAY DIFFRACTIONf_angle_d0.92602
X-RAY DIFFRACTIONf_dihedral_angle_d14.337156
X-RAY DIFFRACTIONf_chiral_restr0.04266
X-RAY DIFFRACTIONf_plane_restr0.00475
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.5-1.61590.25771220.27232370X-RAY DIFFRACTION100
1.6159-1.77850.23921250.22552356X-RAY DIFFRACTION100
1.7785-2.03580.22471270.20272384X-RAY DIFFRACTION100
2.0358-2.56480.1621250.18032386X-RAY DIFFRACTION100
2.5648-38.76790.18171350.15912450X-RAY DIFFRACTION100

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