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- PDB-2wxz: Crystal structure of rat angiotensinogen in C2 space group -

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Basic information

Entry
Database: PDB / ID: 2wxz
TitleCrystal structure of rat angiotensinogen in C2 space group
Components(ANGIOTENSINOGEN) x 2
KeywordsHORMONE / ANGIOTENSINOGEN / RENIN / ANGIOTENSIN / HYPERTENSION / GLYCOPROTEIN / VASOCONSTRICTOR / VASOACTIVE
Function / homology
Function and homology information


renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure / negative regulation of tissue remodeling / uterine smooth muscle contraction / positive regulation of L-lysine import across plasma membrane / establishment of blood-nerve barrier / positive regulation of L-arginine import across plasma membrane / aldosterone secretion / smooth muscle cell proliferation / regulation of systemic arterial blood pressure by circulatory renin-angiotensin / brain renin-angiotensin system ...renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure / negative regulation of tissue remodeling / uterine smooth muscle contraction / positive regulation of L-lysine import across plasma membrane / establishment of blood-nerve barrier / positive regulation of L-arginine import across plasma membrane / aldosterone secretion / smooth muscle cell proliferation / regulation of systemic arterial blood pressure by circulatory renin-angiotensin / brain renin-angiotensin system / ovarian follicle rupture / regulation of transmission of nerve impulse / response to muscle activity involved in regulation of muscle adaptation / : / type 2 angiotensin receptor binding / Metabolism of Angiotensinogen to Angiotensins / maintenance of blood vessel diameter homeostasis by renin-angiotensin / positive regulation of extracellular matrix constituent secretion / negative regulation of neurotrophin TRK receptor signaling pathway / Peptide ligand-binding receptors / vasopressin secretion / cell growth involved in cardiac muscle cell development / operant conditioning / regulation of extracellular matrix assembly / vascular associated smooth muscle cell proliferation / regulation of renal output by angiotensin / regulation of norepinephrine secretion / artery smooth muscle contraction / renal system process / renin-angiotensin regulation of aldosterone production / angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure / drinking behavior / peristalsis / positive regulation of organ growth / positive regulation of branching involved in ureteric bud morphogenesis / positive regulation of extracellular matrix assembly / smooth muscle cell differentiation / positive regulation of macrophage derived foam cell differentiation / positive regulation of fatty acid biosynthetic process / positive regulation of blood pressure / positive regulation of multicellular organism growth / vasoconstriction / intracellular sodium ion homeostasis / hormone metabolic process / type 1 angiotensin receptor binding / positive regulation of extrinsic apoptotic signaling pathway / G alpha (q) signalling events / cellular response to angiotensin / response to angiotensin / positive regulation of vascular associated smooth muscle cell migration / G alpha (i) signalling events / positive regulation of epidermal growth factor receptor signaling pathway / organ growth / branching involved in ureteric bud morphogenesis / positive regulation of cardiac muscle hypertrophy / blood vessel development / positive regulation of cardiac muscle cell apoptotic process / angiotensin-mediated drinking behavior / negative regulation of vascular associated smooth muscle cell proliferation / associative learning / regulation of calcium ion transport / positive regulation of gap junction assembly / regulation of cardiac conduction / positive regulation of epithelial to mesenchymal transition / response to mechanical stimulus / positive regulation of insulin receptor signaling pathway / stress-activated MAPK cascade / positive regulation of vascular associated smooth muscle cell proliferation / response to salt stress / positive regulation of protein metabolic process / ERK1 and ERK2 cascade / regulation of heart rate / response to cold / positive regulation of endothelial cell migration / negative regulation of angiogenesis / extracellular matrix organization / cell-matrix adhesion / positive regulation of superoxide anion generation / kidney development / positive regulation of cytokine production / astrocyte activation / angiotensin-activated signaling pathway / female pregnancy / negative regulation of smooth muscle cell proliferation / regulation of long-term neuronal synaptic plasticity / serine-type endopeptidase inhibitor activity / hormone activity / negative regulation of cell growth / regulation of blood pressure / positive regulation of neuron projection development / positive regulation of miRNA transcription / cellular response to mechanical stimulus / vasodilation / protein import into nucleus / MAPK cascade / positive regulation of nitric oxide biosynthetic process / positive regulation of fibroblast proliferation / positive regulation of peptidyl-serine phosphorylation / response to estradiol / positive regulation of cytosolic calcium ion concentration
Similarity search - Function
Angiotensinogen, serpin domain / Angiotensinogen / Antithrombin; Chain I, domain 2 / Antithrombin, subunit I, domain 2 / Alpha-1-antitrypsin; domain 1 / Alpha-1-antitrypsin, domain 1 / Serpin superfamily, domain 2 / Serpin family / Serpin domain / Serpin superfamily ...Angiotensinogen, serpin domain / Angiotensinogen / Antithrombin; Chain I, domain 2 / Antithrombin, subunit I, domain 2 / Alpha-1-antitrypsin; domain 1 / Alpha-1-antitrypsin, domain 1 / Serpin superfamily, domain 2 / Serpin family / Serpin domain / Serpin superfamily / Serpin superfamily, domain 1 / Serpin (serine protease inhibitor) / SERine Proteinase INhibitors / Roll / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Biological speciesRATTUS NORVEGICUS (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.8 Å
AuthorsZhou, A. / Wei, Z. / Carrell, R.W. / Read, R.J.
CitationJournal: Nature / Year: 2010
Title: A Redox Switch in Angiotensinogen Modulates Angiotensin Release.
Authors: Zhou, A. / Carrell, R.W. / Murphy, M.P. / Wei, Z. / Yan, Y. / Stanley, P.L. / Stein, P.E. / Pipkin, F.B. / Read, R.J.
History
DepositionNov 11, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 20, 2010Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ANGIOTENSINOGEN
C: ANGIOTENSINOGEN


Theoretical massNumber of molelcules
Total (without water)99,1442
Polymers99,1442
Non-polymers00
Water00
1
A: ANGIOTENSINOGEN


Theoretical massNumber of molelcules
Total (without water)49,5561
Polymers49,5561
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
C: ANGIOTENSINOGEN


Theoretical massNumber of molelcules
Total (without water)49,5881
Polymers49,5881
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)130.499, 49.539, 150.275
Angle α, β, γ (deg.)90.00, 90.84, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11C
21A

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114C4 - 20
2114A4 - 20
1214C91 - 96
2214A91 - 96
1312C97 - 230
2312A97 - 230
1414C231 - 238
2414A231 - 238
1512C239 - 401
2512A239 - 401
1616C402 - 421
2616A402 - 421
1712C422 - 455
2712A422 - 455
1812C21 - 90
2812A21 - 90

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Components

#1: Protein ANGIOTENSINOGEN / SERPIN A8


Mass: 49556.211 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Plasmid: PSUMO3-MANGT / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01015
#2: Protein ANGIOTENSINOGEN / SERPIN A8


Mass: 49588.277 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Plasmid: PSUMO3-MANGT / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01015

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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: 2.4 Å3/Da / Density % sol: 49 % / Description: NONE
Crystal growpH: 7.8 / Details: 20-25% PEG3350, 0.2M MGSO4, 0.1M TRIS -HCL, PH7.8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 1.045
DetectorType: ADSC CCD / Detector: CCD / Date: Jul 1, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.045 Å / Relative weight: 1
ReflectionResolution: 2.8→41.6 Å / Num. obs: 23736 / % possible obs: 98.5 % / Observed criterion σ(I): 2 / Redundancy: 4.7 % / Rmerge(I) obs: 0.22 / Net I/σ(I): 8
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 4.1 % / Rmerge(I) obs: 1.04 / Mean I/σ(I) obs: 1.2 / % possible all: 96.8

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Processing

Software
NameVersionClassification
REFMAC5.5.0099refinement
PHASERphasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 2.8→50 Å / Cor.coef. Fo:Fc: 0.883 / Cor.coef. Fo:Fc free: 0.868 / SU B: 60.573 / SU ML: 0.512 / Cross valid method: THROUGHOUT / ESU R Free: 0.478 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.31 1212 5.1 %RANDOM
Rwork0.282 ---
obs0.283 22489 98.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 23.2 Å2
Baniso -1Baniso -2Baniso -3
1-0.47 Å20 Å24.5 Å2
2---1.35 Å20 Å2
3---1.01 Å2
Refinement stepCycle: LAST / Resolution: 2.8→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6452 0 0 0 6452
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0226620
X-RAY DIFFRACTIONr_bond_other_d0.0040.024445
X-RAY DIFFRACTIONr_angle_refined_deg0.9291.9789014
X-RAY DIFFRACTIONr_angle_other_deg0.834310900
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4095831
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.15924.296277
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.61151088
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.5711536
X-RAY DIFFRACTIONr_chiral_restr0.0790.21056
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0217276
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021284
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2541.54177
X-RAY DIFFRACTIONr_mcbond_other0.0231.51668
X-RAY DIFFRACTIONr_mcangle_it0.46726763
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.34332443
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.6334.52248
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
2A2223tight positional0.010.05
1C2223tight positional0.010.05
2A3099medium positional0.040.5
1C3099medium positional0.040.5
2A42loose positional0.245
1C42loose positional0.245
2A2223tight thermal0.020.5
1C2223tight thermal0.020.5
2A3099medium thermal0.022
1C3099medium thermal0.022
2A42loose thermal0.0310
1C42loose thermal0.0310
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.436 73 -
Rwork0.4 1485 -
obs--89.39 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.6972-0.0043-1.48651.6493-0.45193.5969-0.1059-0.4427-0.104-0.03640.0102-0.12710.10350.33330.09570.33630.04550.01230.1544-0.02130.2542-38.243533.270121.4122
25.0108-1.1411-2.31721.7290.40733.42660.19080.41850.0539-0.1145-0.11170.0976-0.19860.233-0.07910.0603-0.0079-0.0670.11250.00040.109-18.114719.499458.5557
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1C6 - 450
2X-RAY DIFFRACTION2A6 - 450

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