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  • #2 Ligand

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    Kelly Eller
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    This document appears to be describing the 3D structure of a protein made up of amino acids. It shows the positions and interactions of various amino and carboxyl groups, nitrogen and oxygen atoms, and residues like aspartate, lysine and leucine that make up the tertiary structure. Bond distances are provided between some atoms in Angstroms. The overall structure seems to be stabilizing different regions of the folded peptide chain through hydrogen bonds, ionic interactions, and van der Waals contacts between the R groups of residues.

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    Original Title

    #2ligand

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    This document appears to be describing the 3D structure of a protein made up of amino acids. It shows the positions and interactions of various amino and carboxyl groups, nitrogen and oxygen atoms, and residues like aspartate, lysine and leucine that make up the tertiary structure. Bond distances are provided between some atoms in Angstroms. The overall structure seems to be stabilizing different regions of the folded peptide chain through hydrogen bonds, ionic interactions, and van der Waals contacts between the R groups of residues.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
    Flag for inappropriate content
    15 views1 page

    #2 Ligand

    Uploaded by

    Kelly Eller
    This document appears to be describing the 3D structure of a protein made up of amino acids. It shows the positions and interactions of various amino and carboxyl groups, nitrogen and oxygen atoms, and residues like aspartate, lysine and leucine that make up the tertiary structure. Bond distances are provided between some atoms in Angstroms. The overall structure seems to be stabilizing different regions of the folded peptide chain through hydrogen bonds, ionic interactions, and van der Waals contacts between the R groups of residues.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PDF, TXT or read online from Scribd
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    of 1

    O

    Ile 224(A)
    N C
    CA
    N
    O
    N6A CB
    CA

    Asp 223(A) CB
    Lys 228(A)
    C6A CG
    Nad 1377(A) N7A OD1
    CG
    N1A
    C8A OD2
    C5A
    C4A 3.49 CD
    C2A CE

    O2B Leu 200(A)


    N9A
    N3A C1B NZ
    3.61
    Gly 199(A) O4B C2B NH1
    C3B 2.84 NH2

    O3B
    CZ Asn 225(A)
    Thr 274(A) C4B
    NE
    N C5B
    Ile 269(A) CD
    CG1 O5B 3.11
    O CD1 CA
    2.79 CG
    His 51(A) CB
    C O1A PA O3
    C CB CB
    O1N
    CD2
    CG2 Arg 47(A)
    O PN CA O
    O2A
    CA NE2 3.24
    CG N
    O5D
    N ND1 2.76 O2N 2.79
    2.95 O3D C
    N
    3.12 NH1
    C5D N
    CE1
    O C3D Arg 369(A) CB
    3.08 CD
    CA
    CZ
    CG2 O2DC2D
    C4D N CA
    Val 268(A) C O4D
    NH2
    CG
    NE C
    CB
    Val 294(A) CG1
    CA
    O

    C1D C
    2.74 CG2
    N1N
    C2N Val 203(A)
    O
    CB OG N7N C6N CB Gly 201(A)
    Ser 48(A) C3N CG1
    O
    Gly 270(A) CA C5N
    C7N
    2.96 O7N
    N C4N
    C Leu 362(A)
    CG1
    O 3.05
    2.75
    Val 292(A) Gly 293(A)
    CB C
    N
    CG2
    C
    O
    CA
    O
    N C
    CA Cys 46(A)
    CB

    Ala 317(A) CA
    CD1
    Fxy 1378(A)
    N
    CE1
    CG
    CB CD2
    Leu 309(B)
    CZ
    Phe 319(A)
    CE2

    Ile 318(A) Cys 174(A)

    Thr 178(A)

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