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    - PDB-1fha: SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEER... -

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    Basic information

    Entry
    Database: PDB / ID: 1fha
    TitleSOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS
    DescriptorFERRITIN (H-CHAIN) MUTANT (LYS 86 REPLACED BY GLN) (K86Q)
    KeywordsMETAL BINDING PROTEIN / IRON STORAGE
    Specimen sourceHomo sapiens / human
    MethodX-ray diffraction (2.4 A resolution)
    AuthorsArtymiuk, P.J. / Harrison, P.M.
    CitationNature, 1991, 349, 541-544

    Nature, 1991, 349, 541-544 StrPapers
    Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts.
    Lawson, D.M. / Artymiuk, P.J. / Yewdall, S.J. / Smith, J.M. / Livingstone, J.C. / Treffry, A. / Luzzago, A. / Levi, S. / Arosio, P. / Cesareni, G. / Thomas, C.D. / Shaw, W.V. / Harrison, P.M.

    DateDeposition: Dec 20, 1990 / Release: Jul 15, 1992 / Last modification: Feb 29, 2012

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    Assembly

    Deposited unit
    A: FERRITIN
    hetero molecules

    21.4 kDa, 4 molecules
    Theoretical massNumber of molelcules
    Total
    (without water)
    21,3914
    Polyers21,2551
    Non-polymers1363
    Water36020

    Omokage search
    #1
    A: FERRITIN
    hetero molecules
    x 24
    defined by author&software (PISA,PQS)
    Buried area (A2)90720
    Surface area (A2)137520
    ΔGint (kcal/M)-550
    / 513 kDa, 96 molecules
    Theoretical massNumber of molelcules
    Total
    (without water)
    513,37996
    Polyers510,11424
    Non-polymers3,26472
    Water43224
    / Symmetry operations: (identity)x1 + (crystal symmetry)x23
    Download / Omokage search

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    Components

    #1polypeptide(L) / FERRITIN / Source: Homo sapiens (gene. exp.) / References: UniProt: P02794
    #2ChemComp-FE / FE (III) ION
    #3ChemComp-CA / CALCIUM ION
    #4ChemComp-HOH / water

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    Experimental details

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    Experiment

    ExperimentMethod: X-RAY DIFFRACTION

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    Sample preparation

    CrystalDensity Matthews: 3.09 A3/Da / Density percent sol: 60.23 %

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    Data collection

    RadiationScattering type: x-ray
    Radiation wavelengthRelative weight: 1

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    Processing

    SoftwareName: PROLSQ / Classification: refinement
    ComputingStructure refinement: PROLSQ
    RefineDetails: THE STRUCTURE WAS SOLVED BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS FROM THE KNOWN STRUCTURE OF HORSE L CHAIN FERRITIN INTO HUMAN H CHAIN FERRITIN.
    Least-squares processR factor obs: 0.205 / Highest resolution: 2.4 A
    Refine hist #LASTHighest resolution: 2.4 A
    Number of atoms included #LASTProtein: 1338 / Nucleic acid: 0 / Ligand: 3 / Solvent: 20 / Total: 1361
    Refine LS restraints
    Refine idTypeDev idealDev ideal target
    X-RAY DIFFRACTIONp_bond_d0.020.02
    X-RAY DIFFRACTIONp_angle_d0.0360.025
    X-RAY DIFFRACTIONp_angle_deg
    X-RAY DIFFRACTIONp_planar_d0.0470.025
    X-RAY DIFFRACTIONp_hb_or_metal_coord
    X-RAY DIFFRACTIONp_mcbond_it
    X-RAY DIFFRACTIONp_mcangle_it
    X-RAY DIFFRACTIONp_scbond_it
    X-RAY DIFFRACTIONp_scangle_it
    X-RAY DIFFRACTIONp_plane_restr0.0110.02
    X-RAY DIFFRACTIONp_chiral_restr0.0380.2
    X-RAY DIFFRACTIONp_singtor_nbd0.210.5
    X-RAY DIFFRACTIONp_multtor_nbd0.1960.5
    X-RAY DIFFRACTIONp_xhyhbond_nbd0.1360.5
    X-RAY DIFFRACTIONp_xyhbond_nbd
    X-RAY DIFFRACTIONp_planar_tor
    X-RAY DIFFRACTIONp_staggered_tor
    X-RAY DIFFRACTIONp_orthonormal_tor
    X-RAY DIFFRACTIONp_transverse_tor
    X-RAY DIFFRACTIONp_special_tor

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