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  • 1hc9.B99990003 01 PDF

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    Lavanya Priya Sathyan
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    This document contains a Ramachandran plot analysis of protein structure 1hc9.B99990003. The plot shows amino acid residues mapped to phi-psi dihedral angle space. 76.4% of residues fall in the most favored regions, with an additional 17.7% in allowed regions and the remaining 5.9% in outlier regions. A good quality protein structure model would be expected to have over 90% of residues in the most favored regions.

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    This document contains a Ramachandran plot analysis of protein structure 1hc9.B99990003. The plot shows amino acid residues mapped to phi-psi dihedral angle space. 76.4% of residues fall in the most favored regions, with an additional 17.7% in allowed regions and the remaining 5.9% in outlier regions. A good quality protein structure model would be expected to have over 90% of residues in the most favored regions.

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    4 visualizações1 página

    1hc9.B99990003 01 PDF

    Enviado por

    Lavanya Priya Sathyan
    This document contains a Ramachandran plot analysis of protein structure 1hc9.B99990003. The plot shows amino acid residues mapped to phi-psi dihedral angle space. 76.4% of residues fall in the most favored regions, with an additional 17.7% in allowed regions and the remaining 5.9% in outlier regions. A good quality protein structure model would be expected to have over 90% of residues in the most favored regions.

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    de 1

    PROCHECK

    Ramachandran Plot
    1hc9.B99990003
    180
    B ~bLEU
    HIS 199
    38
    b

    135 b ~b ASN 48
    TYR 46
    ~l
    GLN 53
    90
    l

    45 L
    Psi (degrees)

    a
    A
    0
    ~a

    TRP 18 ASP 150


    -45
    SER 76

    -90
    VAL 159GLU 237
    SER~b200 MET 45 ~p ASP 90
    -135
    b p
    ~b
    VAL
    SER 214
    239

    -180 -135 -90 -45 0 45 90 135 180


    Phi (degrees)
    Plot statistics
    Residues in most favoured regions [A,B,L] 194 76.4%
    Residues in additional allowed regions [a,b,l,p] 45 17.7%
    Residues in generously allowed regions [~a,~b,~l,~p] 10 3.9%
    Residues in disallowed regions 5 2.0%
    ---- ------
    Number of non-glycine and non-proline residues 254 100.0%
    Number of end-residues (excl. Gly and Pro) 2
    Number of glycine residues (shown as triangles) 11
    Number of proline residues 27
    ----
    Total number of residues 294

    Based on an analysis of 118 structures of resolution of at least 2.0 Angstroms


    and R-factor no greater than 20%, a good quality model would be expected
    to have over 90% in the most favoured regions.

    1hc9.B99990003_01.ps

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