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- PDB-1aep: MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTR... -

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Basic information

Entry
Database: PDB / ID: 1aep
TitleMOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION
ComponentsAPOLIPOPHORIN III
KeywordsLIPOPROTEIN
Function / homologyApolipoprotein / lipid transport / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / extracellular region / Mainly Alpha / Apolipophorin-3b
Function and homology information
Biological speciesLocusta migratoria (migratory locust)
MethodX-RAY DIFFRACTION / Resolution: 2.7 Å
AuthorsHolden, H.
CitationJournal: Biochemistry / Year: 1991
Title: Molecular structure of an apolipoprotein determined at 2.5-A resolution.
Authors: Breiter, D.R. / Kanost, M.R. / Benning, M.M. / Wesenberg, G. / Law, J.H. / Wells, M.A. / Rayment, I. / Holden, H.M.
History
DepositionNov 30, 1992Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: APOLIPOPHORIN III


Theoretical massNumber of molelcules
Total (without water)17,2281
Polymers17,2281
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)67.500, 67.500, 155.600
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522

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Components

#1: Protein APOLIPOPHORIN III


Mass: 17227.836 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Locusta migratoria (migratory locust) / References: UniProt: P10762

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.97 Å3/Da / Density % sol: 58.57 %
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop / pH: 7.4 / Details: referred to J.Biol.Chem. 263.3960-3962 1988
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
112 mg/mlprotein1drop
22.4 Mammonium sulfate1drop
350 mMphosphate1drop
42.8 Mammonium sulfate1reservoir
550 mMphosphate1reservoir

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 2.4 Å / Num. obs: 3927 / Num. measured all: 15665 / Rmerge(I) obs: 0.042

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Processing

SoftwareName: TNT / Classification: refinement
RefinementResolution: 2.7→30 Å / Rfactor obs: 0.21 / σ(F): 0
Refinement stepCycle: LAST / Resolution: 2.7→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1161 0 0 0 1161
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONt_bond_d0.014
X-RAY DIFFRACTIONt_angle_deg2.13
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes
X-RAY DIFFRACTIONt_it
X-RAY DIFFRACTIONt_nbd
Software
*PLUS
Name: TNT / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.7 Å / Lowest resolution: 30 Å / σ(F): 0 / Rfactor all: 0.21
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDType
X-RAY DIFFRACTIONt_angle_d
X-RAY DIFFRACTIONt_angle_deg

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