Job review #1472

Chain: A
1 6 11 16 21 26 31 36 41 46 51 56 61 66 71 76 81 86 91 96 101 106 111 116 121 126 131 136 141 146 151 156 161 166 171 176 181 186 191 196 201 206 211 216
QVQLQQPGAELVKPGASVKLSCKASGYTFTSDWIHWVKQRPGHGLEWIGEIIPSYGRANYNEKIQKKATLTADKSSSTAFMQLSSLTSEDSAVYYCARERGDGYFAVWGAGTTVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD
Chain: B
1 6 11 16 21 26 31 36 41 46 51 56 61 66 71 76 81 86 91 96 101 106 111 116 121 126 131 136 141 146 151 156 161 166 171 176 181 186 191 196 201 206 211 216 221 226 231 236 241 246 251 256 261 266 271 276 281 286 291 296 301 306 311 316 321 326 331 336 341 346 351 356 361 366 371 376 381 386 391 396 401 406 411 416
DILLTQSPAILSVSPGERVSFSCRASQSIGTDIHWYQQRTNGSPRLLIKYASESISGIPSRFSGSGSGTDFTLSINSVESEDIANYYCQQSNRWPFTFGSGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOOO
Chain: C
22 27 32 37 42 47 52 57 62 67 72 77 82 87 92 97 102 107 112 117 122
SALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWSVETATTVGYGDLYPVTLWGRCVAVVVMVAGITSFGLVTAALATWFVGREQERRGH

Job #1472 review - http://mole.upol.cz/online/1472/

Generated on 2017-09-19 19:05:32 by service v2.13.8.2.

5 tunnels click to expand / contract

  1. show | | profile | lining residues
    Tunnel 1 profile

    Unique lining residues set - all

    73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C, 107 THR C, 200107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C, 106 VAL C, 110 LEU C, 300101 THR C

    Unique lining residues set - sidechains

    75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 107 THR C, 200107 THR C, 106 VAL C, 110 LEU C, 300101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.24
    Polarity: 1.55
    Mutability: 93

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.11 0.45 0.18 -0.36 2.43 79
    2 74 THR C, 75 THR C, 103 PHE C, 100 ILE C 2.3 0.65 1.55 0.4 1.38 87
    3 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.4 1.88 0.33 -0.26 2.19 79
    4 75 THR C, 103 PHE C, 100 ILE C 2.72 2.22 2.2 0.8 0.71 87
    5 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 2.83 2.71 2.78 1.05 0.57 91
    6 75 THR C, 103 PHE C, 100 ILE C 3.06 3 2.2 0.8 0.71 87
    7 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 3.1 3.87 2.78 1.05 0.57 91
    8 103 PHE C, 100 ILE C, 300100 ILE C 3.11 4.48 3.93 1.66 0.2 85
    9 103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C 3.23 5.72 2.85 1.04 1 85
    10 100 ILE C, 104 GLY C, 107 THR C 3.6 5.79 1.13 0.08 1.72 105
    11 100 ILE C, 104 GLY C, 200107 THR C 3.58 5.97 1.13 0.08 1.72 105
    12 100 ILE C, 104 GLY C, 107 THR C 3.49 6.47 1.13 0.08 1.72 105
    13 103 PHE C, 300100 ILE C, 104 GLY C, 107 THR C 3.28 7.38 1.55 0.4 1.38 87
    14 103 PHE C, 300100 ILE C, 107 THR C 1.41 12 2.2 0.8 0.71 87
    15 300100 ILE C, 107 THR C, 103 PHE C 1.82 12.45 1.13 0.08 1.72 105
    16 300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C 1.83 12.6 0.75 -0.14 2.14 105
    17 107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C 1.78 12.74 -0.48 -0.79 2.95 107
    18 300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C 1.9 13.07 0.75 -0.14 2.14 105
    19 107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C, 106 VAL C 2 13.26 0.46 -0.41 2.39 102
    20 107 THR C, 103 PHE C, 300101 THR C, 106 VAL C 1.85 14.12 0.68 -0.31 2.14 102
    21 107 THR C, 300101 THR C, 106 VAL C 1.83 14.42 1.03 -0.15 1.72 102
    22 107 THR C, 300101 THR C, 106 VAL C, 110 LEU C 1.75 15.16 1.73 0.18 1.33 86
    23 106 VAL C, 110 LEU C, 300101 THR C 1.22 19.41 2.43 0.5 0.64 86

    layer with bottle neck

    layer with local minimum

  2. show | | profile | lining residues
    Tunnel 2 profile

    Unique lining residues set - all

    73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C, 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C, 200110 LEU C, 101 THR C

    Unique lining residues set - sidechains

    75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200107 THR C, 200106 VAL C, 200110 LEU C, 101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.6
    Hydrophobicity: 0.3
    Polarity: 1.49
    Mutability: 91

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.11 0.55 0.18 -0.36 2.43 79
    2 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.34 1.79 0.33 -0.26 2.19 79
    3 75 THR C, 103 PHE C, 100 ILE C 2.7 2.21 2.2 0.8 0.71 87
    4 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 2.84 2.57 2.78 1.05 0.57 91
    5 75 THR C, 103 PHE C, 100 ILE C 3 3.02 2.2 0.8 0.71 87
    6 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 3.12 3.53 2.78 1.05 0.57 91
    7 103 PHE C, 100 ILE C, 300100 ILE C 3.13 4.98 3.93 1.66 0.2 85
    8 103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C 3.47 5.61 2.85 1.04 1 85
    9 103 PHE C, 100 ILE C, 104 GLY C 3.19 7.04 2.3 0.79 1.29 77
    10 100 ILE C, 104 GLY C, 200107 THR C 1.95 10.03 1.13 0.08 1.72 105
    11 100 ILE C, 104 GLY C, 200107 THR C, 200103 PHE C 1.5 11.2 0.75 -0.14 2.14 105
    12 100 ILE C, 200107 THR C, 200103 PHE C 1.47 12.52 1.13 0.08 1.72 105
    13 100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C 1.91 13.15 0.75 -0.14 2.14 105
    14 100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C 1.96 13.37 0.46 -0.41 2.39 102
    15 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C 1.87 14.09 0.68 -0.31 2.14 102
    16 200107 THR C, 101 THR C, 200106 VAL C 1.83 14.46 1.03 -0.15 1.72 102
    17 200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C 1.79 15.12 1.73 0.18 1.33 86
    18 200106 VAL C, 200110 LEU C, 101 THR C 1.21 19.42 2.43 0.5 0.64 86

    layer with bottle neck

    layer with local minimum

  3. show | | profile | lining residues
    Tunnel 3 profile

    Unique lining residues set - all

    73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C, 107 THR C, 200107 THR C, 200104 GLY C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C

    Unique lining residues set - sidechains

    75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C, 107 THR C, 200107 THR C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.8
    Hydrophobicity: 0.46
    Polarity: 1.18
    Mutability: 95

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.11 0.61 0.18 -0.36 2.43 79
    2 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.38 2.05 0.33 -0.26 2.19 79
    3 75 THR C, 103 PHE C, 100 ILE C 2.82 2.5 2.2 0.8 0.71 87
    4 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 2.99 2.81 2.78 1.05 0.57 91
    5 103 PHE C, 100 ILE C, 300100 ILE C 2.94 3.19 3.93 1.66 0.2 85
    6 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 3.12 5.15 2.78 1.05 0.57 91
    7 75 THR C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C 3.99 6.63 1.38 0.26 1.05 105
    8 100 ILE C, 300100 ILE C, 100075 THR C, 100100 ILE C, 200100 ILE C 4.39 7.01 3.46 1.29 0.44 103
    9 100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C 4.48 7.35 3.46 1.29 0.44 103
    10 100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C 4.65 7.53 2.42 0.78 0.74 104
    11 100 ILE C, 300100 ILE C, 300107 THR C, 107 THR C, 200107 THR C 4.66 7.66 1.38 0.26 1.05 105
    12 100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C 4.68 7.68 2.42 0.78 0.74 104
    13 100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C 4.66 7.74 2.42 0.78 0.74 104
    14 300100 ILE C, 100100 ILE C, 300107 THR C, 107 THR C, 200107 THR C 4.68 7.81 1.38 0.26 1.05 105
    15 100 ILE C, 300100 ILE C, 100100 ILE C, 300107 THR C, 107 THR C 4.63 7.82 2.42 0.78 0.74 104
    16 300100 ILE C, 100100 ILE C, 100107 THR C, 300107 THR C, 107 THR C 4.63 7.95 1.38 0.26 1.05 105
    17 100 ILE C, 200100 ILE C, 100107 THR C, 107 THR C, 200107 THR C 4.69 8.26 1.38 0.26 1.05 105
    18 100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C, 200104 GLY C 4.02 9.34 1.44 0.26 1.39 105
    19 100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C 3.82 9.56 1.98 0.51 1.33 104
    20 100 ILE C, 200100 ILE C, 200104 GLY C, 200103 PHE C 3.57 9.86 2.85 1.04 1 85
    21 200100 ILE C, 200104 GLY C, 200103 PHE C 3.17 11.13 2.3 0.79 1.29 77
    22 200100 ILE C, 100107 THR C, 200104 GLY C 1.68 14.74 1.13 0.08 1.72 105
    23 200100 ILE C, 100107 THR C, 100103 PHE C 1.43 16.45 1.13 0.08 1.72 105
    24 200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C 1.91 17 0.75 -0.14 2.14 105
    25 100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C 1.95 17.23 0.46 -0.41 2.39 102
    26 100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C 1.9 18 0.68 -0.31 2.14 102
    27 100107 THR C, 200101 THR C, 100106 VAL C 1.83 18.42 1.03 -0.15 1.72 102
    28 100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C 1.75 19.23 1.73 0.18 1.33 86
    29 100106 VAL C, 100110 LEU C, 200101 THR C 1.23 23.36 2.43 0.5 0.64 86

    layer with bottle neck

    layer with local minimum

  4. show | | profile | lining residues
    Tunnel 4 profile

    Unique lining residues set - all

    73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100100 ILE C, 100075 THR C, 200100 ILE C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C, 100103 PHE C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C, 300110 LEU C, 100101 THR C

    Unique lining residues set - sidechains

    75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100100 ILE C, 100075 THR C, 200100 ILE C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100103 PHE C, 300106 VAL C, 300110 LEU C, 100101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.7
    Hydrophobicity: 0.4
    Polarity: 1.29
    Mutability: 95

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.11 0.56 0.18 -0.36 2.43 79
    2 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.35 2.03 0.33 -0.26 2.19 79
    3 75 THR C, 103 PHE C, 100 ILE C 2.8 2.46 2.2 0.8 0.71 87
    4 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 2.96 2.72 2.78 1.05 0.57 91
    5 75 THR C, 103 PHE C, 100 ILE C 2.96 2.95 2.2 0.8 0.71 87
    6 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 3 5.38 2.78 1.05 0.57 91
    7 75 THR C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C 4.1 6.15 1.38 0.26 1.05 105
    8 75 THR C, 100 ILE C, 300100 ILE C, 300075 THR C, 100100 ILE C 4.52 6.47 2.42 0.78 0.74 104
    9 200075 THR C, 300075 THR C, 100100 ILE C, 100075 THR C, 200100 ILE C 4.38 6.95 1.38 0.26 1.05 105
    10 75 THR C, 100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C 4.5 7.63 3.46 1.29 0.44 103
    11 100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 107 THR C 4.55 7.98 3.46 1.29 0.44 103
    12 100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C 4.67 8.3 2.42 0.78 0.74 104
    13 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C, 300107 THR C 4.55 8.64 1.38 0.26 1.05 105
    14 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C, 100104 GLY C 4.13 9.29 1.44 0.26 1.39 105
    15 100100 ILE C, 200100 ILE C, 100107 THR C, 100104 GLY C 3.93 9.53 1.98 0.51 1.33 104
    16 100100 ILE C, 200100 ILE C, 100104 GLY C, 100103 PHE C 3.57 9.96 2.85 1.04 1 85
    17 100100 ILE C, 100104 GLY C, 100103 PHE C 3.14 11.22 2.3 0.79 1.29 77
    18 100100 ILE C, 300107 THR C, 100104 GLY C 1.79 14.47 1.13 0.08 1.72 105
    19 100100 ILE C, 300107 THR C, 100104 GLY C, 300103 PHE C 1.44 15.6 0.75 -0.14 2.14 105
    20 100100 ILE C, 300107 THR C, 300103 PHE C 1.55 16.34 1.13 0.08 1.72 105
    21 100100 ILE C, 300107 THR C, 300103 PHE C, 100101 THR C 1.85 17.11 0.75 -0.14 2.14 105
    22 300107 THR C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C 1.96 17.33 0.46 -0.41 2.39 102
    23 300107 THR C, 300103 PHE C, 100101 THR C, 300106 VAL C 1.91 18.01 0.68 -0.31 2.14 102
    24 300107 THR C, 100101 THR C, 300106 VAL C 1.83 18.41 1.03 -0.15 1.72 102
    25 300107 THR C, 100101 THR C, 300106 VAL C, 300110 LEU C 1.81 19.12 1.73 0.18 1.33 86
    26 300106 VAL C, 300110 LEU C, 100101 THR C 1.21 23.46 2.43 0.5 0.64 86

    layer with bottle neck

    layer with local minimum

  5. show | | profile | lining residues
    Tunnel 5 profile

    Unique lining residues set - all

    73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C

    Unique lining residues set - sidechains

    75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 0.8
    Hydrophobicity: 0.16
    Polarity: 4.81
    Mutability: 96

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.11 0.42 0.18 -0.36 2.43 79
    2 74 THR C, 75 THR C, 103 PHE C, 100 ILE C 2.28 0.61 1.55 0.4 1.38 87
    3 74 THR C, 75 THR C, 100 ILE C, 103 PHE C 2.38 1.86 0.33 -0.26 2.19 79
    4 75 THR C, 103 PHE C, 100 ILE C 2.75 2.48 2.2 0.8 0.71 87
    5 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 2.98 2.68 2.78 1.05 0.57 91
    6 75 THR C, 103 PHE C, 100 ILE C 3.05 2.82 2.2 0.8 0.71 87
    7 103 PHE C, 100 ILE C, 300100 ILE C 2.93 2.92 3.93 1.66 0.2 85
    8 75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C 2.97 5.03 2.78 1.05 0.57 91
    9 75 THR C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C 3.92 6.25 1.38 0.26 1.05 105
    10 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C 4.55 6.59 1.38 0.26 1.05 105
    11 100 ILE C, 300100 ILE C, 100075 THR C, 100100 ILE C, 200100 ILE C 4.42 6.84 3.46 1.29 0.44 103
    12 100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C 4.4 7.51 3.46 1.29 0.44 103
    13 300100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C 4.67 7.91 0.34 -0.25 1.35 106
    14 100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C 4.63 8.87 3.46 1.29 0.44 103
    15 300100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C 4.63 9.54 0.34 -0.25 1.35 106
    16 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 104 GLY C 4.15 10.29 -0.64 -0.78 2 107
    17 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C 1.45 19.92 -0.7 -0.77 1.66 107
    18 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 100111 ALA C 2.22 20.79 -0.2 -0.61 1.33 105
    19 107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C 2.21 22.19 1.3 -0.14 0.33 101
    20 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 300111 ALA C 2.15 24.11 -0.2 -0.61 1.33 105
    21 107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C 2.26 25.26 1.3 -0.14 0.33 101
    22 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C 1.75 27.64 1.8 0.02 0 100
    23 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C 2.2 28.49 2.28 0.24 0.03 99
    24 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C 2.17 29.45 3.72 0.91 0.1 98
    25 111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C 2.44 29.76 3.72 0.91 0.1 98
    26 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C 2.27 30.18 2.28 0.24 0.03 99
    27 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C 2.31 30.95 2.28 0.24 0.03 99
    28 100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C 2.33 31.71 3.72 0.91 0.1 98
    29 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C 1.71 39.38 4.2 1.13 0.13 98
    30 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C 2.14 40.99 2.66 0.68 0.81 95
    31 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C 2.91 41.83 -3.5 -1.1 3.53 84
    32 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C 2.9 42.13 2.66 0.68 0.81 95
    33 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C 3 42.23 -1.96 -0.65 2.85 86
    34 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C 2.64 48.67 -3.5 -1.1 3.53 84
    35 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C 3.86 49.83 -3.44 -0.83 13.14 85
    36 200119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C 4.43 49.93 -3.26 -0.01 41.99 89
    37 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C 4.41 50.15 -3.26 -0.01 41.99 89
    38 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C 4.4 50.24 -3.44 -0.83 13.14 85
    39 100119 GLN C, 200119 GLN C, 124 HIS C, 100124 HIS C, 300124 HIS C 4.41 50.24 -3.32 -0.28 32.37 88

    layer with bottle neck

    layer with local minimum

show all | hide all

You can download all tunnels as PyMol script, PDB file or print the report.

56 pores click to expand / contract

This is an experimental feature.

Merged pores Created by merging tunnels from the selected start point.

No merged pores were found.

Auto pores Computed from pairs of exit points.

  1. show | | profile | lining residues
    Pore 1 profile

    Unique lining residues set - all

    100156 THR A, 100041 ASN B, 100155 VAL A, 100154 PRO A, 100113 THR A, 100093 VAL A, 100095 TYR A, 100039 GLN A, 100042 GLY A, 100041 PRO A, 100041 ASN B, 100038 GLN B, 100085 ASN B, 100040 THR B, 100040 THR B, 100165 ASP B, 100103 LYS B, 100010 ILE B

    Unique lining residues set - sidechains

    100156 THR A, 100041 ASN B, 100154 PRO A, 100113 THR A, 100093 VAL A, 100095 TYR A, 100039 GLN A, 100038 GLN B, 100085 ASN B, 100040 THR B, 100165 ASP B, 100103 LYS B, 100010 ILE B

    Physicochemical properties of lining side-chains

    Charge: 0 (1-1)
    Hydropathy: -1.7
    Hydrophobicity: -0.65
    Polarity: 7.41
    Mutability: 89

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100041 ASN B 2.78 0.83 -2.1 -0.77 2.52 105
    2 100156 THR A, 100041 ASN B, 100155 VAL A 2.66 2.73 -1.53 -0.78 2.81 105
    3 100156 THR A, 100041 ASN B, 100155 VAL A, 100154 PRO A 2.88 3 -1.55 -0.61 2.5 89
    4 100041 ASN B, 100154 PRO A 2.73 5.06 -2.55 -0.43 2.48 81
    5 100041 ASN B, 100154 PRO A, 100113 THR A 2.88 5.82 -1.93 -0.54 2.21 89
    6 100041 ASN B, 100154 PRO A, 100113 THR A, 100093 VAL A 2.9 6.11 -0.4 -0.13 1.69 91
    7 100041 ASN B, 100113 THR A, 100093 VAL A 2.85 6.9 0 -0.14 1.72 103
    8 100041 ASN B, 100093 VAL A 2.57 8.37 0.35 0.18 1.76 101
    9 100041 ASN B, 100093 VAL A, 100095 TYR A 2.4 10.95 -0.2 0.49 1.71 84
    10 100041 ASN B, 100093 VAL A, 100039 GLN A 2.99 11.27 -0.93 -0.25 2.35 95
    11 100041 ASN B, 100039 GLN A 2.97 12.23 -3.5 -0.94 3.46 94
    12 100041 ASN B, 100039 GLN A, 100042 GLY A 3.24 12.56 -2.47 -0.89 3.43 94
    13 100041 ASN B, 100039 GLN A, 100042 GLY A, 100041 PRO A 3.27 13 -1.95 -0.87 3.42 94
    14 100041 ASN B, 100039 GLN A, 100042 GLY A 3.11 13.51 -2.47 -0.89 3.43 94
    15 100039 GLN A, 100042 GLY A, 100041 ASN B 3.08 14.72 -1.43 -0.9 3.43 84
    16 100039 GLN A, 100041 ASN B, 100038 GLN B 3.11 14.97 -2.47 -1 3.48 84
    17 100039 GLN A, 100042 GLY A, 100041 ASN B, 100038 GLN B 3.14 15.15 -1.95 -0.95 3.46 84
    18 100039 GLN A, 100042 GLY A, 100041 ASN B, 100038 GLN B, 100085 ASN B 3.29 15.83 -2.26 -0.91 3.44 90
    19 100042 GLY A, 100041 ASN B, 100085 ASN B, 100040 THR B 3.29 16.55 -1.18 -0.79 3.38 104
    20 100042 GLY A, 100041 ASN B, 100085 ASN B, 100040 THR B 3.3 16.86 -1.25 -0.79 2.95 105
    21 100042 GLY A, 100085 ASN B, 100040 THR B 3.32 17.42 -1.53 -0.78 2.81 105
    22 100042 GLY A, 100085 ASN B, 100040 THR B, 100165 ASP B 3.29 17.53 -2.03 -0.85 14.53 99
    23 100042 GLY A, 100085 ASN B, 100165 ASP B 3.28 17.58 -2.47 -0.87 18.82 95
    24 100042 GLY A, 100085 ASN B, 100040 THR B, 100165 ASP B 3.29 17.83 -2.03 -0.85 14.53 99
    25 100085 ASN B, 100040 THR B, 100165 ASP B 3.11 18.44 -2.57 -0.86 18.25 99
    26 100042 GLY A, 100085 ASN B, 100165 ASP B 2.7 23.92 -2.47 -0.87 18.82 95
    27 100042 GLY A, 100085 ASN B, 100165 ASP B, 100103 LYS B 3.66 24.72 -2.83 -0.76 26.49 87
    28 100042 GLY A, 100165 ASP B, 100103 LYS B, 100010 ILE B 3.81 24.86 -0.83 -0.11 25.68 87

    pore with bottle neck

    pore with local minimum

  2. show | | profile | lining residues
    Pore 2 profile

    Unique lining residues set - all

    100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

    Unique lining residues set - sidechains

    100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

    Physicochemical properties of lining side-chains

    Charge: -1 (1-2)
    Hydropathy: -1.4
    Hydrophobicity: -0.5
    Polarity: 17.57
    Mutability: 98

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100165 SER A, 100168 VAL A, 100169 LYS B 1.57 0.75 -1.57 -0.67 18.75 72
    2 100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A 1.65 2.05 -1.28 -0.7 14.91 72
    3 100168 VAL A, 100169 LYS B, 100167 GLY A 1.69 2.94 -1.57 -0.67 18.75 72
    4 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.94 3.18 -1.98 -0.44 26.97 81
    5 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.9 3.36 -1.98 -0.44 26.97 81
    6 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.99 3.47 -1.98 -0.44 26.97 81
    7 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.81 3.8 -1.98 -0.44 26.97 81
    8 100168 VAL A, 100167 GLY A, 100169 HIS A, 100167 ASP B 1.73 3.97 -1.88 -0.6 27.02 88
    9 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B 1.75 4.82 -2.75 -0.5 38.55 83
    10 100169 LYS B, 100167 GLY A, 100167 ASP B 1.63 6.39 -2.6 -0.75 34.19 79
    11 100169 LYS B, 100167 GLY A, 100166 SER A 1.58 8.05 -1.57 -0.67 18.75 72
    12 100169 LYS B, 100167 GLY A, 100166 SER A 1.81 8.24 -1.7 -0.73 18.18 94
    13 100169 LYS B, 100166 SER A 1.85 8.49 -2.35 -0.69 25.59 94
    14 100169 LYS B, 100167 GLY A, 100166 SER A 1.96 11.59 -1.7 -0.73 18.18 94
    15 100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B 3.53 13.1 -2.15 -0.81 26.06 91
    16 100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B 4.28 13.62 -1.28 -0.9 14.53 101
    17 100167 GLY A, 100166 SER A, 100170 ASP B 4.57 14.49 -1.57 -0.94 18.25 101
    18 100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A 5.02 15.37 -0.7 -0.45 14.05 98
    19 100167 GLY A, 100170 ASP B, 100140 MET A 4.2 17.11 -0.67 -0.28 18.17 89
    20 100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B 3.91 18.47 -1.38 -0.4 14.47 94
    21 100170 ASP B, 100140 MET A, 100138 ASN B 4 19.67 -1.7 -0.27 18.17 94
    22 100140 MET A, 100138 ASN B, 100187 THR A 3.52 21.81 -0.77 -0.18 2.16 101
    23 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B 2.76 23.47 -0.75 -0.33 2.03 102
    24 100140 MET A, 100187 THR A, 100114 THR B 2.61 25.52 0.17 -0.18 1.58 102
    25 100140 MET A, 100114 THR B 2.71 26.28 0.6 0.12 1.55 100
    26 100140 MET A, 100114 THR B, 100138 ASN A 2.94 26.88 -0.77 -0.18 2.16 101
    27 100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A 2.9 27.78 -0.78 -0.38 2.04 105
    28 100140 MET A, 100114 THR B, 100138 ASN A 2.74 28.71 -0.77 -0.18 2.16 101

    pore with bottle neck

    pore with local minimum

  3. show | | profile | lining residues
    Pore 3 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100171 PHE A, 100182 LEU A, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100182 LEU A, 100170 THR A, 100156 THR A, 100168 VAL A, 100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

    Physicochemical properties of lining side-chains

    Charge: -3 (1-4)
    Hydropathy: -1.3
    Hydrophobicity: -0.55
    Polarity: 11.65
    Mutability: 92

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.29 0.14 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.15 1.77 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.14 4.11 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.66 4.73 -2.25 -0.68 14.51 82
    5 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.68 5.27 -1.78 -0.44 2.48 73
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.39 6.58 -1.78 -0.44 2.48 73
    7 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.47 6.97 -2.55 -0.52 14.11 74
    8 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.37 7.77 -2.55 -0.52 14.11 74
    9 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.32 11.33 -2.25 -0.7 14.56 79
    10 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.39 12.5 -1.95 -0.88 15.01 90
    11 100041 ASN B, 100153 GLU A, 100172 PRO A, 100171 PHE A, 100182 LEU A 2.65 12.81 -0.8 -0.47 12.03 78
    12 100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A 2.59 13.77 -0.13 -0.31 2.57 79
    13 100041 ASN B, 100171 PHE A, 100182 LEU A 2.75 14.01 -0.03 -0.14 2.3 79
    14 100041 ASN B, 100182 LEU A, 100170 THR A 2.77 14.18 -0.13 -0.13 1.72 88
    15 100041 ASN B, 100182 LEU A, 100170 THR A, 100155 VAL A 2.61 15.52 -0.2 -0.3 2.14 88
    16 100041 ASN B, 100170 THR A, 100155 VAL A 2.53 19.29 -1.53 -0.78 2.81 105
    17 100041 ASN B, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A 3.28 19.56 -1.14 -0.78 2.69 106
    18 100041 ASN B, 100156 THR A, 100157 VAL A 3.13 19.76 -1.53 -0.78 2.81 105
    19 100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A 3.23 19.96 -1.33 -0.78 2.52 106
    20 100041 ASN B, 100170 THR A, 100157 VAL A 3.26 20.08 -1.53 -0.78 2.81 105
    21 100041 ASN B, 100170 THR A, 100155 VAL A 3.17 20.22 -1.53 -0.78 2.81 105
    22 100041 ASN B, 100170 THR A, 100157 VAL A 3.24 20.4 -1.53 -0.78 2.81 105
    23 100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A 3.28 20.92 -1.33 -0.78 2.52 106
    24 100041 ASN B, 100170 THR A, 100157 VAL A 3.27 24.13 -1.53 -0.78 2.81 105
    25 100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B 4.22 24.75 -1.25 -0.79 2.95 105
    26 100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A 4.57 24.93 -1.08 -0.79 3.04 105
    27 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A 4.62 25.1 0.68 -0.31 2.14 102
    28 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B 4.58 25.23 -1.16 -0.72 12.26 89
    29 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B 4.55 25.28 -0.13 -0.22 14.1 85
    30 100170 THR A, 100157 VAL A, 100168 VAL A, 100169 LYS B 4.41 25.99 -0.2 -0.21 13.67 92
    31 100157 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A 4.3 26.42 -0.13 -0.22 14.1 85
    32 100168 VAL A, 100169 LYS B, 100165 SER A 1.93 30.95 -0.03 -0.03 17.67 85
    33 100168 VAL A, 100169 LYS B, 100165 SER A 1.43 32.75 -1.57 -0.67 18.75 72
    34 100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A 1.58 34.24 -1.28 -0.7 14.91 72
    35 100168 VAL A, 100169 LYS B, 100167 GLY A 1.75 35.12 -1.57 -0.67 18.75 72
    36 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.9 35.39 -1.98 -0.44 26.97 81
    37 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 2.01 35.51 -1.98 -0.44 26.97 81
    38 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.75 35.87 -1.98 -0.44 26.97 81
    39 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B 1.79 36.58 -2.75 -0.5 38.55 83
    40 100169 LYS B, 100167 GLY A, 100167 ASP B 1.68 38.22 -2.6 -0.75 34.19 79
    41 100169 LYS B, 100167 GLY A 1.62 39.07 -2.15 -0.61 26.44 72
    42 100169 LYS B, 100167 GLY A, 100166 SER A 1.68 40.06 -1.57 -0.67 18.75 72
    43 100169 LYS B, 100167 GLY A, 100166 SER A 1.82 43.41 -1.7 -0.73 18.18 94
    44 100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B 3.41 44.72 -2.15 -0.81 26.06 91
    45 100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B 4.11 45.82 -1.28 -0.9 14.53 101
    46 100167 GLY A, 100166 SER A, 100170 ASP B 4.71 46.31 -1.57 -0.94 18.25 101
    47 100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A 5 47.38 -0.7 -0.45 14.05 98
    48 100167 GLY A, 100170 ASP B, 100140 MET A 4.34 48.88 -0.67 -0.28 18.17 89
    49 100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B 3.91 50.38 -1.38 -0.4 14.47 94
    50 100170 ASP B, 100140 MET A, 100138 ASN B 4.02 51.72 -1.7 -0.27 18.17 94
    51 100140 MET A, 100138 ASN B, 100187 THR A 3.52 53.72 -0.77 -0.18 2.16 101
    52 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B 2.81 55.55 -0.75 -0.33 2.03 102
    53 100140 MET A, 100187 THR A, 100114 THR B 2.62 57.88 0.17 -0.18 1.58 102
    54 100140 MET A, 100114 THR B 2.84 58.63 0.6 0.12 1.55 100
    55 100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A 2.97 59.7 -0.78 -0.38 2.04 105
    56 100140 MET A, 100114 THR B, 100138 ASN A 2.75 60.69 -0.77 -0.18 2.16 101

    pore with bottle neck

    pore with local minimum

  4. show | | profile | lining residues
    Pore 4 profile

    Unique lining residues set - all

    100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100113 PRO B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A, 100135 ALA A, 100117 ILE B, 100116 SER B, 100117 ILE B, 100132 GLY A, 100208 SER B, 100209 PHE B, 100119 PRO B, 100210 ASN B, 100133 SER A, 100218 ARG A, 100211 ARG B, 100186 TYR B, 100211 ARG B, 100125 LEU B

    Unique lining residues set - sidechains

    100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100207 LYS B, 100116 SER B, 100135 ALA A, 100117 ILE B, 100209 PHE B, 100119 PRO B, 100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 2 (4-2)
    Hydropathy: -1.1
    Hydrophobicity: -0.41
    Polarity: 12.37
    Mutability: 88

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100165 SER A, 100168 VAL A, 100169 LYS B 1.57 0.7 -1.57 -0.67 18.75 72
    2 100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A 1.64 1.87 -1.28 -0.7 14.91 72
    3 100168 VAL A, 100169 LYS B, 100167 GLY A 1.67 3.08 -1.57 -0.67 18.75 72
    4 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.97 3.23 -1.98 -0.44 26.97 81
    5 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.92 3.37 -1.98 -0.44 26.97 81
    6 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.99 3.48 -1.98 -0.44 26.97 81
    7 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.78 3.81 -1.98 -0.44 26.97 81
    8 100168 VAL A, 100167 GLY A, 100169 HIS A, 100167 ASP B 1.7 3.97 -1.88 -0.6 27.02 88
    9 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B 1.84 4.78 -2.75 -0.5 38.55 83
    10 100169 LYS B, 100167 GLY A, 100167 ASP B 1.66 6.27 -2.6 -0.75 34.19 79
    11 100169 LYS B, 100167 GLY A 1.58 7.01 -2.15 -0.61 26.44 72
    12 100169 LYS B, 100167 GLY A, 100166 SER A 1.71 7.97 -1.57 -0.67 18.75 72
    13 100169 LYS B, 100167 GLY A, 100166 SER A 1.82 11.69 -1.7 -0.73 18.18 94
    14 100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B 3.61 13.04 -2.15 -0.81 26.06 91
    15 100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B 4.26 13.53 -1.28 -0.9 14.53 101
    16 100167 GLY A, 100166 SER A, 100170 ASP B 4.54 14.4 -1.57 -0.94 18.25 101
    17 100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A 4.98 15.43 -0.7 -0.45 14.05 98
    18 100167 GLY A, 100170 ASP B, 100140 MET A 4.37 16.76 -0.67 -0.28 18.17 89
    19 100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B 3.92 18.42 -1.38 -0.4 14.47 94
    20 100170 ASP B, 100140 MET A, 100138 ASN B 4.03 19.8 -1.7 -0.27 18.17 94
    21 100140 MET A, 100138 ASN B, 100187 THR A 3.54 21.57 -0.77 -0.18 2.16 101
    22 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B 2.88 23.13 -0.75 -0.33 2.03 102
    23 100140 MET A, 100187 THR A, 100114 THR B 2.65 25.62 0.17 -0.18 1.58 102
    24 100140 MET A, 100114 THR B 2.84 26.35 0.6 0.12 1.55 100
    25 100140 MET A, 100114 THR B, 100138 ASN A 3.06 26.87 -0.77 -0.18 2.16 101
    26 100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A 2.89 27.84 -0.78 -0.38 2.04 105
    27 100140 MET A, 100114 THR B, 100138 ASN A 2.42 30.45 -0.77 -0.18 2.16 101
    28 100114 THR B, 100138 ASN A 2.7 34 -2.1 -0.77 2.52 105
    29 100114 THR B, 100138 ASN A, 100113 PRO B 4.31 34.55 -1.53 -0.78 2.81 105
    30 100114 THR B, 100138 ASN A, 100113 PRO B, 100207 LYS B 4.3 35.21 -2.13 -0.69 14.48 94
    31 100114 THR B, 100138 ASN A, 100207 LYS B 3.18 37.26 -2.7 -0.65 18.18 94
    32 100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A 2.93 38.26 -2.13 -0.69 14.48 94
    33 100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B 2.79 39.58 -1.78 -0.71 12.26 94
    34 100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B 2.71 39.98 -1.35 -0.7 14.48 89
    35 100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B 2.54 40.61 -1.78 -0.71 12.26 94
    36 100114 THR B, 100138 ASN A, 100136 GLN A, 100115 VAL B, 100116 SER B 2.55 40.99 -1.16 -0.82 2.69 109
    37 100114 THR B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A 2.61 42.04 -0.54 -0.83 2.69 112
    38 100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B 2.66 42.71 -1.24 -0.75 11.92 98
    39 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B 2.56 43.38 -1.38 -0.75 14.48 94
    40 100136 GLN A, 100115 VAL B, 100116 SER B 2.51 43.98 -0.53 -0.86 2.81 117
    41 100136 GLN A, 100115 VAL B, 100116 SER B, 100135 ALA A 2.33 44.84 0.05 -0.64 2.11 108
    42 100115 VAL B, 100116 SER B, 100135 ALA A 2.25 45.99 0.2 -0.58 1.68 108
    43 100116 SER B, 100135 ALA A, 100117 ILE B 1.92 48.79 0.2 -0.58 1.68 108
    44 100135 ALA A, 100116 SER B, 100117 ILE B 1.88 49.78 1.97 0.34 1.17 101
    45 100135 ALA A, 100117 ILE B 1.56 51.49 3.15 0.92 0.07 101
    46 100135 ALA A, 100117 ILE B, 100132 GLY A, 100208 SER B 1.62 52.45 1.38 0.06 1.72 101
    47 100135 ALA A, 100117 ILE B, 100132 GLY A 1.83 52.97 1.97 0.34 1.17 101
    48 100117 ILE B, 100132 GLY A, 100209 PHE B 1.59 54.29 2.3 0.79 1.29 77
    49 100117 ILE B, 100132 GLY A, 100209 PHE B, 100119 PRO B 1.57 54.77 0.1 -0.09 2.17 54
    50 100117 ILE B, 100132 GLY A, 100119 PRO B 1.58 54.93 -0.8 -0.56 2.78 58
    51 100117 ILE B, 100132 GLY A, 100119 PRO B 1.44 55.13 0.83 0.31 1.7 80
    52 100117 ILE B, 100132 GLY A, 100119 PRO B 1.66 55.54 -0.8 -0.56 2.78 58
    53 100132 GLY A, 100209 PHE B, 100119 PRO B 1.15 59.77 0.27 0.15 1.77 54
    54 100132 GLY A, 100209 PHE B, 100119 PRO B, 100210 ASN B 2.06 60.19 0.1 -0.09 2.17 54
    55 100132 GLY A, 100209 PHE B, 100119 PRO B, 100210 ASN B, 100133 SER A 2.2 60.69 0 -0.23 2.41 54
    56 100132 GLY A, 100119 PRO B, 100210 ASN B, 100133 SER A, 100218 ARG A 2.21 61.68 -1.46 -0.58 12.74 70
    57 100119 PRO B, 100210 ASN B, 100218 ARG A 2.05 63.26 -2.17 -0.44 18.99 70
    58 100209 PHE B, 100119 PRO B, 100210 ASN B, 100218 ARG A 2.04 63.76 -0.93 0.01 14.33 64
    59 100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B 2.01 64.39 -1.73 -0.53 15.09 70
    60 100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B, 100186 TYR B 1.97 64.74 -1.64 -0.2 12.39 63
    61 100119 PRO B, 100218 ARG A, 100211 ARG B, 100186 TYR B 1.9 66.44 -1.95 -0.05 14.64 63
    62 100218 ARG A, 100186 TYR B, 100211 ARG B 1.91 68.04 -3.43 0.09 35.2 72
    63 100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B 2.41 68.04 -1.63 0.35 26.44 67

    pore with bottle neck

    pore with local minimum

  5. show | | profile | lining residues
    Pore 5 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100182 LEU A, 100171 PHE A, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100113 PRO B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A, 100135 ALA A, 100117 ILE B, 100116 SER B, 100117 ILE B, 100208 SER B, 100132 GLY A, 100209 PHE B, 100119 PRO B, 100133 SER A, 100210 ASN B, 100218 ARG A, 100211 ARG B, 100186 TYR B, 100211 ARG B, 100125 LEU B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100182 LEU A, 100170 THR A, 100156 THR A, 100168 VAL A, 100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100207 LYS B, 100116 SER B, 100135 ALA A, 100117 ILE B, 100209 PHE B, 100119 PRO B, 100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 0 (4-4)
    Hydropathy: -1.1
    Hydrophobicity: -0.45
    Polarity: 10.87
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.3 0.12 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.17 2.12 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.21 3.92 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.65 4.21 -1.94 -0.69 11.94 88
    5 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.68 4.76 -2.25 -0.68 14.51 82
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.67 5.29 -1.78 -0.44 2.48 73
    7 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.42 6.55 -1.78 -0.44 2.48 73
    8 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.48 7.26 -2.55 -0.52 14.11 74
    9 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.44 7.66 -2.55 -0.52 14.11 74
    10 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.3 11.67 -2.25 -0.7 14.56 79
    11 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.54 12.25 -1.95 -0.88 15.01 90
    12 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100182 LEU A 2.72 12.61 -0.8 -0.47 12.03 78
    13 100041 ASN B, 100153 GLU A, 100172 PRO A, 100182 LEU A, 100171 PHE A 2.73 12.83 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100172 PRO A, 100182 LEU A, 100171 PHE A 2.61 13.74 -0.13 -0.31 2.57 79
    15 100041 ASN B, 100182 LEU A, 100171 PHE A 2.77 13.97 -0.03 -0.14 2.3 79
    16 100041 ASN B, 100182 LEU A, 100170 THR A 2.77 14.15 -0.13 -0.13 1.72 88
    17 100041 ASN B, 100182 LEU A, 100170 THR A, 100155 VAL A 2.53 15.95 -0.2 -0.3 2.14 88
    18 100041 ASN B, 100170 THR A, 100155 VAL A 2.45 19.41 -1.53 -0.78 2.81 105
    19 100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A 3.25 19.6 -1.33 -0.78 2.52 106
    20 100041 ASN B, 100156 THR A, 100157 VAL A 3.27 19.83 -1.53 -0.78 2.81 105
    21 100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A 3.2 20.02 -1.33 -0.78 2.52 106
    22 100041 ASN B, 100170 THR A, 100157 VAL A 3.17 20.14 -1.53 -0.78 2.81 105
    23 100041 ASN B, 100170 THR A, 100155 VAL A 3.17 20.35 -1.53 -0.78 2.81 105
    24 100041 ASN B, 100170 THR A, 100157 VAL A 3.26 20.51 -1.53 -0.78 2.81 105
    25 100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A 3.27 21.04 -1.33 -0.78 2.52 106
    26 100041 ASN B, 100170 THR A, 100157 VAL A 3.26 24.14 -1.53 -0.78 2.81 105
    27 100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B 4.16 24.95 -1.25 -0.79 2.95 105
    28 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A 4.6 25.18 0.68 -0.31 2.14 102
    29 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B 4.56 25.31 -1.16 -0.72 12.26 89
    30 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B 4.53 25.36 -0.13 -0.22 14.1 85
    31 100170 THR A, 100157 VAL A, 100168 VAL A, 100169 LYS B 4.46 26.07 -0.2 -0.21 13.67 92
    32 100157 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A 4.27 26.48 -0.13 -0.22 14.1 85
    33 100168 VAL A, 100169 LYS B, 100165 SER A 2.21 30.78 -0.03 -0.03 17.67 85
    34 100168 VAL A, 100169 LYS B, 100165 SER A 1.43 32.78 -1.57 -0.67 18.75 72
    35 100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A 1.55 33.97 -1.28 -0.7 14.91 72
    36 100168 VAL A, 100169 LYS B, 100167 GLY A 1.76 34.96 -1.57 -0.67 18.75 72
    37 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.9 35.23 -1.98 -0.44 26.97 81
    38 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.91 35.44 -1.98 -0.44 26.97 81
    39 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.96 35.57 -1.98 -0.44 26.97 81
    40 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A 1.88 35.92 -1.98 -0.44 26.97 81
    41 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B 1.7 36.53 -2.75 -0.5 38.55 83
    42 100169 LYS B, 100167 GLY A, 100167 ASP B 1.64 38.03 -2.6 -0.75 34.19 79
    43 100169 LYS B, 100167 GLY A 1.7 38.86 -2.15 -0.61 26.44 72
    44 100169 LYS B, 100167 GLY A, 100166 SER A 1.81 40.02 -1.57 -0.67 18.75 72
    45 100169 LYS B, 100167 GLY A, 100166 SER A 1.84 43.56 -1.7 -0.73 18.18 94
    46 100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B 3.49 45.2 -2.15 -0.81 26.06 91
    47 100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B 4.35 45.74 -1.28 -0.9 14.53 101
    48 100167 GLY A, 100166 SER A, 100170 ASP B 4.66 46.59 -1.57 -0.94 18.25 101
    49 100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A 5 47.51 -0.7 -0.45 14.05 98
    50 100167 GLY A, 100170 ASP B, 100140 MET A 4.27 48.98 -0.67 -0.28 18.17 89
    51 100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B 3.99 50.4 -1.38 -0.4 14.47 94
    52 100170 ASP B, 100140 MET A, 100138 ASN B 4.06 51.93 -1.7 -0.27 18.17 94
    53 100140 MET A, 100138 ASN B, 100187 THR A 3.56 53.54 -0.77 -0.18 2.16 101
    54 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B 2.92 55.24 -0.75 -0.33 2.03 102
    55 100140 MET A, 100187 THR A, 100114 THR B 2.63 57.21 0.17 -0.18 1.58 102
    56 100140 MET A, 100114 THR B 2.73 58.76 0.6 0.12 1.55 100
    57 100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A 3.02 59.85 -0.78 -0.38 2.04 105
    58 100140 MET A, 100114 THR B, 100138 ASN A 2.25 62.78 -0.77 -0.18 2.16 101
    59 100114 THR B, 100138 ASN A 2.64 66.35 -2.1 -0.77 2.52 105
    60 100114 THR B, 100138 ASN A, 100113 PRO B, 100207 LYS B 4.42 66.93 -2.13 -0.69 14.48 94
    61 100114 THR B, 100138 ASN A, 100207 LYS B 3.51 69.02 -2.7 -0.65 18.18 94
    62 100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A 2.7 70.97 -2.13 -0.69 14.48 94
    63 100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B 2.71 71.65 -1.78 -0.71 12.26 94
    64 100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B 2.66 72.15 -1.35 -0.7 14.48 89
    65 100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B 2.56 72.49 -1.78 -0.71 12.26 94
    66 100114 THR B, 100138 ASN A, 100136 GLN A, 100115 VAL B, 100116 SER B 2.52 72.88 -1.16 -0.82 2.69 109
    67 100114 THR B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A 2.58 73.96 -0.54 -0.83 2.69 112
    68 100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B 2.73 74.68 -1.24 -0.75 11.92 98
    69 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B 2.72 75.41 -1.38 -0.75 14.48 94
    70 100136 GLN A, 100115 VAL B, 100116 SER B 2.66 76.06 -0.53 -0.86 2.81 117
    71 100136 GLN A, 100115 VAL B, 100116 SER B, 100135 ALA A 2.29 76.92 0.05 -0.64 2.11 108
    72 100115 VAL B, 100116 SER B, 100135 ALA A 2.25 78.02 0.2 -0.58 1.68 108
    73 100116 SER B, 100135 ALA A, 100117 ILE B 2.03 80.83 0.2 -0.58 1.68 108
    74 100135 ALA A, 100116 SER B, 100117 ILE B 1.9 81.91 1.97 0.34 1.17 101
    75 100135 ALA A, 100117 ILE B 1.64 83.15 3.15 0.92 0.07 101
    76 100135 ALA A, 100117 ILE B, 100208 SER B 1.57 83.77 1.97 0.34 1.17 101
    77 100135 ALA A, 100117 ILE B, 100208 SER B, 100132 GLY A 1.59 84.3 1.38 0.06 1.72 101
    78 100135 ALA A, 100117 ILE B, 100132 GLY A 1.69 84.95 1.97 0.34 1.17 101
    79 100117 ILE B, 100208 SER B, 100132 GLY A 1.85 85.17 1.23 0.07 2.3 103
    80 100117 ILE B, 100132 GLY A, 100209 PHE B 1.59 86.38 2.3 0.79 1.29 77
    81 100117 ILE B, 100132 GLY A, 100209 PHE B, 100119 PRO B 1.6 86.89 0.1 -0.09 2.17 54
    82 100117 ILE B, 100132 GLY A, 100119 PRO B 1.64 87.03 -0.8 -0.56 2.78 58
    83 100117 ILE B, 100132 GLY A, 100119 PRO B 1.41 87.43 0.83 0.31 1.7 80
    84 100117 ILE B, 100132 GLY A, 100209 PHE B, 100119 PRO B 1.22 88.15 0.1 -0.09 2.17 54
    85 100132 GLY A, 100209 PHE B, 100119 PRO B 1.1 91.89 0.27 0.15 1.77 54
    86 100132 GLY A, 100209 PHE B, 100119 PRO B, 100133 SER A, 100210 ASN B 2.22 92.63 0 -0.23 2.41 54
    87 100132 GLY A, 100119 PRO B, 100133 SER A, 100210 ASN B, 100218 ARG A 2.2 93.74 -1.46 -0.58 12.74 70
    88 100119 PRO B, 100210 ASN B, 100218 ARG A 2.05 95.25 -2.17 -0.44 18.99 70
    89 100209 PHE B, 100119 PRO B, 100210 ASN B, 100218 ARG A 2.04 95.79 -0.93 0.01 14.33 64
    90 100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B 2.03 96.45 -1.73 -0.53 15.09 70
    91 100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B, 100186 TYR B 1.98 96.63 -1.64 -0.2 12.39 63
    92 100119 PRO B, 100218 ARG A, 100211 ARG B, 100186 TYR B 1.86 98.33 -1.95 -0.05 14.64 63
    93 100218 ARG A, 100186 TYR B, 100211 ARG B 2 100.05 -3.43 0.09 35.2 72
    94 100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B 2.41 100.05 -1.63 0.35 26.44 67

    pore with bottle neck

    pore with local minimum

  6. show | | profile | lining residues
    Pore 6 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C,

    Physicochemical properties of lining side-chains

    Charge: 4 (8-4)
    Hydropathy: -1.5
    Hydrophobicity: -0.4
    Polarity: 15.01
    Mutability: 85

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.28 0.27 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.24 0.44 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.16 0.68 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.17 0.83 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.19 0.97 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3.24 1.57 -1.53 -0.78 2.81 105
    7 100170 THR A, 100041 ASN B, 100155 VAL A 2.43 5.59 -1.53 -0.78 2.81 105
    8 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.48 6.65 -0.2 -0.3 2.14 88
    9 100170 THR A, 100041 ASN B, 100182 LEU A 2.76 6.98 -0.13 -0.13 1.72 88
    10 100041 ASN B, 100182 LEU A, 100171 PHE A 2.75 7.15 -0.03 -0.14 2.3 79
    11 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.6 7.91 -0.13 -0.31 2.57 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.6 8.65 -0.8 -0.47 12.03 78
    13 100041 ASN B, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.57 9.12 -1.64 -0.86 12.68 90
    14 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.51 9.66 -1.95 -0.88 15.01 90
    15 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.38 12.73 -2.25 -0.7 14.56 79
    16 100041 ASN B, 100153 GLU A, 100172 PRO A 3.08 13.37 -2.87 -0.67 18.29 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.34 13.86 -2.55 -0.52 14.11 74
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.44 14.41 -2.55 -0.52 14.11 74
    19 100153 GLU A, 100172 PRO A, 100041 PRO A 3.45 14.72 -2.23 -0.44 17.69 64
    20 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.32 16.8 -1.78 -0.53 14.11 64
    21 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.28 19.02 -1.7 -0.23 14.12 61
    22 100173 ALA A, 100041 PRO A, 100180 TYR A 3.62 20.92 -1.1 0.07 2.19 54
    23 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.34 21.41 0.13 0.34 1.68 54
    24 100041 PRO A, 100180 TYR A, 100175 LEU A 4.38 22.04 0.3 0.72 1.11 54
    25 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.44 22.59 0.13 0.34 1.68 54
    26 100041 PRO A, 100180 TYR A, 100175 LEU A 4.22 27.17 0.3 0.72 1.11 54
    27 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.15 27.74 -0.06 0.08 1.67 69
    28 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.09 28.07 0.02 0.3 1.25 69
    29 100180 TYR A, 100091 SER A, 100088 SER A 4.05 28.21 -0.97 -0.28 1.65 94
    30 100091 SER A, 100088 SER A 4.06 28.28 -0.8 -0.97 1.67 117
    31 100180 TYR A, 100091 SER A, 100088 SER A 4.13 28.58 -0.97 -0.28 1.65 94
    32 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.4 28.8 0.23 0.08 1.27 84
    33 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.52 29.43 0.02 0.3 1.25 69
    34 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.63 29.84 0.15 -0.22 1.26 86
    35 100041 PRO A, 100091 SER A, 100088 SER A 4.64 30.74 -1.07 -0.68 1.64 97
    36 100041 PRO A, 100088 SER A 4.76 31.82 -1.2 -0.53 1.63 87
    37 100041 PRO A, 100088 SER A, 100040 ARG A 4.59 34.04 -2.3 -0.49 18.42 86
    38 100041 PRO A, 100088 SER A, 100040 ARG A 2.76 36.57 -2.17 -0.44 18.99 70
    39 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.6 36.88 -1.73 -0.53 15.09 70
    40 100088 SER A, 100040 ARG A, 100091 SER A 2.32 38.39 -1.77 -0.67 19.59 83
    41 100088 SER A, 100040 ARG A 1.98 39.38 -2.45 -0.61 27.69 83
    42 100040 ARG A 0.38 45.98 -4.5 -0.42 52 83
    43 100040 ARG A, 100043 HIS A 1.49 46.92 -3.85 -0.08 51.8 87
    44 100040 ARG A, 100046 GLU A 2.37 50.01 -4 -0.78 50.95 80
    45 100040 ARG A, 100046 GLU A, 100064 ILE A 4.71 50.63 -1.17 0.08 34.01 87
    46 100040 ARG A, 100046 GLU A, 300018 ARG B 4.01 52.55 -4.17 -0.66 51.3 81
    47 100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B 3.47 56.45 -2 -0.04 38.51 86
    48 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A 3.56 59.51 -0.98 -0.14 26.35 87
    49 100046 GLU A, 100064 ILE A, 100063 LYS A 3.4 60.25 0.2 -0.04 17.8 90
    50 100046 GLU A, 100064 ILE A, 100063 LYS A 2.98 65.05 -0.97 0.09 33.18 84
    51 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 5.41 65.4 -0.93 -0.18 25.3 92
    52 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 5.59 65.72 -1.1 -0.35 25.3 80
    53 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.8 69.38 0.23 0.35 24.92 76
    54 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.44 70.32 -1 -0.3 25.73 67
    55 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.15 71 -1.5 -0.4 21.26 76
    56 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.98 71.37 -2.4 -0.78 21.56 90
    57 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.91 71.7 -2.03 -0.87 14.58 96
    58 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.03 71.89 -2.4 -0.78 21.56 90
    59 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 4.06 72.69 -0.94 -0.32 11.61 84
    60 100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B 3.94 73.06 -0.3 -0.21 13.67 77
    61 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.79 73.47 -1.08 -0.2 13.67 84
    62 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.43 75.29 -1.08 -0.27 25.25 79
    63 100063 LYS A, 100003 LEU B, 100001 ASP B 3.48 76.95 -1.2 -0.1 33.11 70
    64 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 3.87 78.14 -1.08 -0.27 25.25 79
    65 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.18 78.32 -1.56 -0.42 30.14 81
    66 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.01 79.09 -0.98 -0.43 25.3 83
    67 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.96 79.23 -0.2 -0.37 13.72 82
    68 100003 LEU B, 300070 ASP B, 100001 ASP B 3 81.47 -0.03 -0.23 17.74 70
    69 100003 LEU B, 300070 ASP B 2.14 84.37 0.15 0.05 24.92 70
    70 100003 LEU B, 300070 ASP B, 100026 SER B 2.11 87.09 -0.17 -0.29 17.17 85
    71 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.57 88.69 -1.25 -0.32 25.88 85
    72 300070 ASP B, 100026 SER B, 300024 ARG B 3.2 90.47 -2.93 -0.81 34.46 95
    73 300070 ASP B, 300024 ARG B, 100026 SER B 3.64 91.64 -2.8 -0.75 35.03 84
    74 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.76 93.1 -2.28 -0.76 26.69 92
    75 300024 ARG B, 100026 SER B, 300069 THR B 4.32 94.53 -1.87 -0.66 19.01 95
    76 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.87 95.55 -1.5 -0.7 15.11 95
    77 100026 SER B, 300069 THR B, 300026 SER B 4.42 98.34 -0.5 -0.79 2.81 107
    78 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.43 99.22 -0.48 -0.79 2.95 107
    79 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.51 101.31 -0.46 -0.79 3.04 107
    80 100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B 5.17 101.59 -1.28 -0.92 2.99 100
    81 100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B 4.16 104.44 -1.35 -0.91 2.56 102
    82 100026 SER B, 100027 GLN B, 300028 SER B 5.16 105.07 -1.57 -0.96 2.86 100
    83 300027 GLN B, 100027 GLN B, 300028 SER B 5.61 105.68 -1.57 -0.96 2.86 100
    84 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B 6.04 106.63 -2.05 -0.99 3.03 95
    85 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.18 107.77 -2.05 -0.99 3.03 95
    86 100027 GLN B, 300028 SER B, 100028 SER B 4.99 111.19 -1.7 -1.01 2.29 106
    87 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.78 111.67 -2.4 -0.87 14.72 100
    88 100027 GLN B, 100028 SER B, 100093 ARG B 4.84 112.05 -2.93 -0.83 19.07 94
    89 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.64 112.93 -2.4 -0.87 14.72 100
    90 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.33 113.56 -2.3 -0.82 15.15 94
    91 100027 GLN B, 300028 SER B, 100093 ARG B 2.42 117.86 -2.93 -0.83 19.07 94
    92 300028 SER B, 100093 ARG B 2.76 118.55 -2.65 -0.7 26.84 100
    93 300028 SER B, 100093 ARG B, 100082 TYR C 3.08 120.21 -2.2 -0.09 18.43 83
    94 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 4.18 123.43 -2.78 -0.18 26.82 83
    95 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.1 123.81 -2.3 -0.3 22.13 83
    96 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.35 124.74 -2.22 -0.27 22.47 72
    97 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C 6.87 124.97 -1.58 0.04 12.4 61
    98 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B 6.77 125.3 -2.4 0.12 22.12 66
    99 300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C 6.36 126.13 -2.4 0.12 22.12 66
    100 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.69 127.77 -1.58 0.04 12.4 61
    101 100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C 5.25 128.7 -1.88 0.25 14.65 61
    102 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 3.26 131.64 -2.43 -0.3 15.13 72
    103 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 3.43 132.31 -2.2 -0.78 15.57 83
    104 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.73 133.36 -2.43 -0.3 15.13 72
    105 100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C 3.67 133.54 -2.43 -0.3 15.13 72
    106 100093 ARG B, 200082 TYR C, 100058 GLN C 3.63 134.47 -3.1 -0.14 19.05 72
    107 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.75 134.7 -2.43 -0.3 15.13 72
    108 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.68 135.12 -2.53 -0.35 14.7 83
    109 100028 SER B, 100093 ARG B, 100058 GLN C 3.61 135.35 -2.93 -0.83 19.07 94
    110 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.72 136.29 -2.53 -0.35 14.7 83
    111 100028 SER B, 100093 ARG B, 200082 TYR C 3.85 136.63 -2.2 -0.09 18.43 83
    112 100028 SER B, 200093 ARG B, 200082 TYR C 3.27 138.99 -2.2 -0.09 18.43 83
    113 200027 GLN B, 100028 SER B, 200093 ARG B 2.51 140.97 -2.93 -0.83 19.07 94

    pore with bottle neck

    pore with local minimum

  7. show | | profile | lining residues
    Pore 7 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C, 200057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 3 (10-7)
    Hydropathy: -1.5
    Hydrophobicity: -0.41
    Polarity: 15.94
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.31 0.14 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.13 1.97 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.19 4.02 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.69 4.8 -2.25 -0.68 14.51 82
    5 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.71 4.96 -1.78 -0.44 2.48 73
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.67 5.18 -1.78 -0.44 2.48 73
    7 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.55 6.48 -1.78 -0.44 2.48 73
    8 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.52 7.03 -2.55 -0.52 14.11 74
    9 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.48 7.88 -2.55 -0.52 14.11 74
    10 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A 3.36 9.97 -1.78 -0.53 14.11 64
    11 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A 3.31 12.26 -1.7 -0.23 14.12 61
    12 100041 PRO A, 100173 ALA A, 100180 TYR A 3.49 14.21 -1.1 0.07 2.19 54
    13 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.4 14.6 0.13 0.34 1.68 54
    14 100041 PRO A, 100180 TYR A, 100175 LEU A 4.37 15.38 0.3 0.72 1.11 54
    15 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.44 15.78 0.13 0.34 1.68 54
    16 100041 PRO A, 100180 TYR A, 100175 LEU A 4.32 20.45 0.3 0.72 1.11 54
    17 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.28 21.03 -0.06 0.08 1.67 69
    18 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.22 21.36 0.23 0.08 1.27 84
    19 100180 TYR A, 100091 SER A, 100088 SER A 4.17 21.49 -0.97 -0.28 1.65 94
    20 100091 SER A, 100088 SER A 4.13 21.56 -0.8 -0.97 1.67 117
    21 100180 TYR A, 100091 SER A, 100088 SER A 4.13 21.9 -0.97 -0.28 1.65 94
    22 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.25 22.13 0.23 0.08 1.27 84
    23 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.35 22.45 0.02 0.3 1.25 69
    24 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.47 23.28 0.15 -0.22 1.26 86
    25 100041 PRO A, 100091 SER A, 100088 SER A 4.68 23.75 -1.07 -0.68 1.64 97
    26 100041 PRO A, 100088 SER A 4.79 24.96 -1.2 -0.53 1.63 87
    27 100041 PRO A, 100088 SER A, 100040 ARG A 4.53 27.19 -2.3 -0.49 18.42 86
    28 100041 PRO A, 100088 SER A, 100040 ARG A 2.92 29.84 -2.17 -0.44 18.99 70
    29 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.75 30.16 -1.73 -0.53 15.09 70
    30 100088 SER A, 100040 ARG A, 100091 SER A 2.42 31.09 -1.77 -0.67 19.59 83
    31 100088 SER A, 100040 ARG A 1.88 32.92 -2.45 -0.61 27.69 83
    32 100040 ARG A 0.81 38.56 -4.5 -0.42 52 83
    33 100040 ARG A, 100043 HIS A 1.23 39.67 -3.85 -0.08 51.8 87
    34 100040 ARG A, 100046 GLU A 1.87 43.67 -4 -0.78 50.95 80
    35 100040 ARG A, 100046 GLU A, 300018 ARG B 3.99 46.23 -4.17 -0.66 51.3 81
    36 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.53 49.84 -2 -0.04 38.51 86
    37 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.61 53.09 -0.98 -0.14 26.35 87
    38 100046 GLU A, 100064 ILE A, 100063 LYS A 3.34 53.83 0.2 -0.04 17.8 90
    39 100046 GLU A, 100064 ILE A, 100063 LYS A 2.94 58.17 -0.97 0.09 33.18 84
    40 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 5.33 58.6 -0.93 -0.18 25.3 92
    41 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 5.39 59.5 -1.1 -0.35 25.3 80
    42 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.8 62.59 0.23 0.35 24.92 76
    43 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.58 63.57 -1 -0.3 25.73 67
    44 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.39 64.27 -1.5 -0.4 21.26 76
    45 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.26 64.64 -2.4 -0.78 21.56 90
    46 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.17 64.99 -2.03 -0.87 14.58 96
    47 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.16 65.2 -2.4 -0.78 21.56 90
    48 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.9 66.07 -0.94 -0.32 11.61 84
    49 100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B 3.77 66.47 -0.3 -0.21 13.67 77
    50 100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B 3.65 66.89 -0.3 -0.21 13.67 77
    51 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.47 68.87 -1.08 -0.27 25.25 79
    52 100063 LYS A, 100003 LEU B, 100001 ASP B 3.61 70.52 -1.2 -0.1 33.11 70
    53 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 4.07 71.35 -1.08 -0.27 25.25 79
    54 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.19 71.55 -1.56 -0.42 30.14 81
    55 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.99 72.37 -0.98 -0.43 25.3 83
    56 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.94 72.53 -0.2 -0.37 13.72 82
    57 100003 LEU B, 300070 ASP B, 100001 ASP B 3.05 74.63 -0.03 -0.23 17.74 70
    58 100003 LEU B, 300070 ASP B 2.19 77.63 0.15 0.05 24.92 70
    59 100003 LEU B, 300070 ASP B, 100026 SER B 2.13 80.45 -0.17 -0.29 17.17 85
    60 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.58 82.11 -1.25 -0.32 25.88 85
    61 300070 ASP B, 100026 SER B, 300024 ARG B 3.25 83.72 -2.93 -0.81 34.46 95
    62 300070 ASP B, 300024 ARG B, 100026 SER B 3.64 84.88 -2.8 -0.75 35.03 84
    63 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.76 86.4 -2.28 -0.76 26.69 92
    64 300024 ARG B, 100026 SER B, 300069 THR B 4.29 87.85 -1.87 -0.66 19.01 95
    65 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.89 88.98 -1.5 -0.7 15.11 95
    66 100026 SER B, 300069 THR B, 300026 SER B 4.38 92.12 -0.5 -0.79 2.81 107
    67 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.43 92.98 -0.48 -0.79 2.95 107
    68 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.58 94.52 -0.46 -0.79 3.04 107
    69 100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B 5.14 94.67 -0.58 -0.84 2.52 112
    70 100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B 5.18 94.81 -1.28 -0.92 2.99 100
    71 100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B 4.17 97.85 -1.35 -0.91 2.56 102
    72 100026 SER B, 300028 SER B, 100027 GLN B 5.22 98.49 -1.57 -0.96 2.86 100
    73 300028 SER B, 100027 GLN B, 300027 GLN B 5.51 99.11 -2.6 -1.06 2.91 95
    74 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B 5.76 100 -2.05 -0.99 3.03 95
    75 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.16 100.85 -2.05 -0.99 3.03 95
    76 300028 SER B, 100027 GLN B, 100028 SER B 4.96 104.38 -1.7 -1.01 2.29 106
    77 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.78 104.92 -2.4 -0.87 14.72 100
    78 100027 GLN B, 100028 SER B, 100093 ARG B 4.85 105.31 -2.93 -0.83 19.07 94
    79 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.61 106.25 -2.4 -0.87 14.72 100
    80 300028 SER B, 100027 GLN B, 100093 ARG B 2.46 111.41 -2.93 -0.83 19.07 94
    81 300028 SER B, 100093 ARG B 2.96 112.11 -2.65 -0.7 26.84 100
    82 300028 SER B, 100093 ARG B, 100082 TYR C 3.27 113.69 -2.2 -0.09 18.43 83
    83 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 4.22 116.62 -2.78 -0.18 26.82 83
    84 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.19 117.02 -2.3 -0.3 22.13 83
    85 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.45 117.99 -2.22 -0.27 22.47 72
    86 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C 6.75 118.23 -1.58 0.04 12.4 61
    87 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B 6.45 118.58 -2.4 0.12 22.12 66
    88 300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C 6.34 118.93 -2.4 0.12 22.12 66
    89 300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C 6.2 119.54 -2.22 -0.27 22.47 72
    90 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.68 121.3 -1.58 0.04 12.4 61
    91 100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C 5.22 122.26 -1.88 0.25 14.65 61
    92 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 3.23 124.75 -2.43 -0.3 15.13 72
    93 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 3.33 125.44 -2.2 -0.78 15.57 83
    94 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.69 126.77 -2.43 -0.3 15.13 72
    95 100093 ARG B, 200082 TYR C, 100058 GLN C 3.55 127.79 -3.1 -0.14 19.05 72
    96 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.62 128.02 -2.43 -0.3 15.13 72
    97 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.68 128.51 -2.53 -0.35 14.7 83
    98 100028 SER B, 100093 ARG B, 200082 TYR C 3.85 128.54 -2.2 -0.09 18.43 83
    99 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.69 129.19 -2.53 -0.35 14.7 83
    100 100028 SER B, 200082 TYR C, 100058 GLN C 3.25 131.45 -1.87 -0.32 2.27 83
    101 100028 SER B, 200082 TYR C, 100058 GLN C, 100030 GLY B 3.11 132.58 -1.5 -0.44 2.55 83
    102 200082 TYR C, 100058 GLN C, 100030 GLY B, 100092 ASN B 3.11 134.6 -2.18 -0.39 2.98 79
    103 200082 TYR C, 100030 GLY B, 100092 ASN B 3.18 134.93 -1.73 -0.15 2.79 77
    104 200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C 3.21 135.58 -0.25 0.17 2.13 84
    105 200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C 3.28 135.84 -1.1 0.05 12.1 83
    106 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B 3.11 137.06 -1.54 -0.38 21.72 92
    107 100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B 2.93 138.27 -1.05 -0.28 26.3 89
    108 100030 GLY B, 200084 VAL C, 100064 ARG C 2.93 138.35 -0.23 -0.03 18.5 90
    109 100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B 2.94 138.47 -0.35 -0.22 14.29 96
    110 100030 GLY B, 100064 ARG C, 100031 THR B 2.98 138.51 -1.87 -0.66 19.01 95
    111 100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B 2.99 138.56 -2.2 -0.77 27.12 84
    112 100030 GLY B, 100064 ARG C, 100032 ASP B 3 138.64 -2.8 -0.75 35.03 84
    113 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B 2.67 139.41 -1.13 -0.28 25.87 93
    114 200084 VAL C, 100064 ARG C, 100031 THR B 2.42 140.17 -0.33 -0.02 17.93 96
    115 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B 2.23 141.28 -1.13 -0.28 25.87 93
    116 100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C 2.2 142.5 -2.28 -0.76 26.69 92
    117 100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 201001 DGA C 2.32 143.54 -2.28 -0.76 26.69 92
    118 100064 ARG C, 100031 THR B, 200084 VAL C, 201001 DGA C 2.58 144.02 -1.87 -0.66 19.01 95
    119 100031 THR B, 200084 VAL C, 201001 DGA C 2.7 145.69 -0.55 -0.79 2.52 107
    120 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C 2.88 146.22 -1.25 -0.88 14.58 92
    121 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C 2.88 146.65 -1.33 -0.87 14.15 97
    122 100031 THR B, 200084 VAL C, 201001 DGA C, 200085 THR C, 200054 ALA C 2.79 147.33 0 -0.58 1.68 104
    123 100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C 2.89 148.47 -0.78 -0.67 13.31 97
    124 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C 2.91 150.52 -0.8 -0.63 17.19 94
    125 100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C 3.07 151.84 -0.7 -0.67 13.74 94
    126 100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A 3.51 152.5 -1.46 -0.62 21.39 91
    127 100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A 3.78 152.96 -2.28 -0.78 26.74 89
    128 100053 GLU B, 200053 GLY C, 200057 ARG A 3.82 153.86 -2.8 -0.79 35.09 80

    pore with bottle neck

    pore with local minimum

  8. show | | profile | lining residues
    Pore 8 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 58 GLN C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 58 GLN C, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C, 300057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 3 (10-7)
    Hydropathy: -1.6
    Hydrophobicity: -0.41
    Polarity: 16.07
    Mutability: 88

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.31 0.14 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.13 2 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.19 4.06 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.66 4.71 -2.25 -0.68 14.51 82
    5 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.72 5 -1.78 -0.44 2.48 73
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.7 5.23 -1.78 -0.44 2.48 73
    7 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.58 6.23 -1.78 -0.44 2.48 73
    8 100041 ASN B, 100172 PRO A, 100041 PRO A 3.54 6.56 -2.23 -0.32 2.18 73
    9 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.47 7.09 -2.55 -0.52 14.11 74
    10 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.44 7.65 -2.55 -0.52 14.11 74
    11 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A 3.42 10.11 -1.78 -0.53 14.11 64
    12 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A 3.38 11.92 -1.7 -0.23 14.12 61
    13 100041 PRO A, 100173 ALA A, 100180 TYR A 3.53 14.32 -1.1 0.07 2.19 54
    14 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.33 14.65 0.13 0.34 1.68 54
    15 100041 PRO A, 100180 TYR A, 100175 LEU A 4.38 15.33 0.3 0.72 1.11 54
    16 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.46 15.64 0.13 0.34 1.68 54
    17 100041 PRO A, 100180 TYR A, 100175 LEU A 4.06 20.16 0.3 0.72 1.11 54
    18 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.14 20.84 -0.06 0.08 1.67 69
    19 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.22 21.26 0.02 0.3 1.25 69
    20 100180 TYR A, 100091 SER A, 100088 SER A 4.29 21.45 -0.97 -0.28 1.65 94
    21 100091 SER A, 100088 SER A 4.35 21.52 -0.8 -0.97 1.67 117
    22 100180 TYR A, 100091 SER A, 100088 SER A 4.39 21.82 -0.97 -0.28 1.65 94
    23 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.45 22.04 0.23 0.08 1.27 84
    24 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.47 22.7 0.02 0.3 1.25 69
    25 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.52 23.14 0.15 -0.22 1.26 86
    26 100041 PRO A, 100091 SER A, 100088 SER A 4.57 24.08 -1.07 -0.68 1.64 97
    27 100041 PRO A, 100088 SER A 4.81 25.15 -1.2 -0.53 1.63 87
    28 100041 PRO A, 100088 SER A, 100040 ARG A 4.36 27.71 -2.3 -0.49 18.42 86
    29 100041 PRO A, 100088 SER A, 100040 ARG A 2.93 29.78 -2.17 -0.44 18.99 70
    30 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.77 30.11 -1.73 -0.53 15.09 70
    31 100088 SER A, 100040 ARG A, 100091 SER A 1.41 31.72 -1.77 -0.67 19.59 83
    32 100088 SER A, 100040 ARG A 0.78 32.8 -2.45 -0.61 27.69 83
    33 100040 ARG A 0.01 38.48 -4.5 -0.42 52 83
    34 100040 ARG A, 100043 HIS A 1.47 39.61 -3.85 -0.08 51.8 87
    35 100040 ARG A, 100046 GLU A 2.36 43.66 -4 -0.78 50.95 80
    36 100040 ARG A, 100046 GLU A, 300018 ARG B 4.17 45.7 -4.17 -0.66 51.3 81
    37 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.46 49.34 -2 -0.04 38.51 86
    38 100046 GLU A, 300018 ARG B, 100064 ILE A 3.77 49.91 -1.17 0.08 34.01 87
    39 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.5 53.22 -0.98 -0.14 26.35 87
    40 100046 GLU A, 100064 ILE A, 100063 LYS A 2.89 58.29 -0.97 0.09 33.18 84
    41 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 5.25 58.66 -0.93 -0.18 25.3 92
    42 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 5.42 59.01 -1.1 -0.35 25.3 80
    43 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.87 62.91 0.23 0.35 24.92 76
    44 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.58 63.82 -1 -0.3 25.73 67
    45 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.33 64.42 -1.5 -0.4 21.26 76
    46 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.17 64.69 -2.4 -0.78 21.56 90
    47 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.11 65.04 -2.03 -0.87 14.58 96
    48 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.11 65.25 -2.4 -0.78 21.56 90
    49 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.85 66.2 -0.94 -0.32 11.61 84
    50 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.73 66.62 -1.08 -0.2 13.67 84
    51 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.49 68.52 -1.08 -0.27 25.25 79
    52 100063 LYS A, 100003 LEU B, 100001 ASP B 3.55 70.25 -1.2 -0.1 33.11 70
    53 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 4 71.23 -1.08 -0.27 25.25 79
    54 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.21 71.43 -1.56 -0.42 30.14 81
    55 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.95 72.44 -0.98 -0.43 25.3 83
    56 100003 LEU B, 300070 ASP B, 100001 ASP B 3.07 74.5 -0.03 -0.23 17.74 70
    57 100003 LEU B, 300070 ASP B 2.15 77.51 0.15 0.05 24.92 70
    58 100003 LEU B, 300070 ASP B, 100026 SER B 2.07 80.36 -0.17 -0.29 17.17 85
    59 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.66 82.04 -1.25 -0.32 25.88 85
    60 300070 ASP B, 100026 SER B, 300024 ARG B 3.25 83.7 -2.93 -0.81 34.46 95
    61 300070 ASP B, 300024 ARG B, 100026 SER B 3.63 84.87 -2.8 -0.75 35.03 84
    62 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.76 86.4 -2.28 -0.76 26.69 92
    63 300024 ARG B, 100026 SER B, 300069 THR B 4.35 87.85 -1.87 -0.66 19.01 95
    64 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.89 88.61 -1.5 -0.7 15.11 95
    65 100026 SER B, 300069 THR B, 300026 SER B 4.42 91.31 -0.5 -0.79 2.81 107
    66 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.52 92.23 -0.48 -0.79 2.95 107
    67 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.68 94.53 -0.46 -0.79 3.04 107
    68 100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B 5.12 94.83 -1.28 -0.92 2.99 100
    69 100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B 4.17 98.02 -1.35 -0.91 2.56 102
    70 300027 GLN B, 100027 GLN B, 300028 SER B 5.41 98.67 -1.57 -0.96 2.86 100
    71 100027 GLN B, 300028 SER B, 300027 GLN B 5.87 99.27 -2.6 -1.06 2.91 95
    72 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B 6.26 99.75 -2.05 -0.99 3.03 95
    73 100027 GLN B, 300028 SER B, 100028 SER B 6.54 100.07 -1.7 -1.01 2.29 106
    74 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.2 100.99 -2.05 -0.99 3.03 95
    75 100027 GLN B, 300028 SER B, 100028 SER B 4.98 104.5 -1.7 -1.01 2.29 106
    76 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.82 104.84 -2.4 -0.87 14.72 100
    77 100027 GLN B, 100028 SER B, 100093 ARG B 4.87 105.47 -2.93 -0.83 19.07 94
    78 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.81 105.98 -2.4 -0.87 14.72 100
    79 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.43 106.64 -2.3 -0.82 15.15 94
    80 100027 GLN B, 300028 SER B, 100093 ARG B 2.44 111.68 -2.93 -0.83 19.07 94
    81 300028 SER B, 100093 ARG B, 100082 TYR C 3.01 113.36 -2.2 -0.09 18.43 83
    82 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 3.84 114.08 -2.78 -0.18 26.82 83
    83 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.73 114.96 -2.53 -0.35 14.7 83
    84 300028 SER B, 300093 ARG B, 300058 GLN C 3.63 115.24 -2.93 -0.83 19.07 94
    85 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.64 115.86 -2.53 -0.35 14.7 83
    86 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.66 116.12 -2.43 -0.3 15.13 72
    87 100082 TYR C, 300093 ARG B, 300058 GLN C 3.66 116.98 -3.1 -0.14 19.05 72
    88 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C 3.74 118.19 -2.43 -0.3 15.13 72
    89 300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C 3.36 118.87 -2.2 -0.78 15.57 83
    90 300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C 3.18 122.56 -2.43 -0.3 15.13 72
    91 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C 5.24 123.48 -1.88 0.25 14.65 61
    92 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C 5.64 124.76 -1.58 0.04 12.4 61
    93 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.25 125.17 -2.4 0.12 22.12 66
    94 100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.78 125.37 -2.4 0.12 22.12 66
    95 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.85 125.61 -2.4 0.12 22.12 66
    96 300079 GLY C, 79 GLY C, 93 ARG B, 82 TYR C, 200079 GLY C 6.85 125.87 -1.4 -0.34 12.75 66
    97 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B 6.39 126.9 -2.22 -0.27 22.47 72
    98 300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B 6.11 127.36 -2.3 -0.3 22.13 83
    99 300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B 4.61 129.85 -2.78 -0.18 26.82 83
    100 300082 TYR C, 93 ARG B, 28 SER B 4.02 130.99 -2.2 -0.09 18.43 83
    101 300082 TYR C, 93 ARG B, 28 SER B, 58 GLN C 3.7 132.27 -2.53 -0.35 14.7 83
    102 300082 TYR C, 28 SER B, 58 GLN C 3.38 134.58 -1.87 -0.32 2.27 83
    103 300082 TYR C, 28 SER B, 58 GLN C, 30 GLY B 3.15 135.69 -1.5 -0.44 2.55 83
    104 300082 TYR C, 58 GLN C, 30 GLY B, 92 ASN B 3.12 137.43 -2.18 -0.39 2.98 79
    105 300082 TYR C, 30 GLY B, 92 ASN B 3.23 138.1 -1.73 -0.15 2.79 77
    106 300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C 3.32 138.7 -0.25 0.17 2.13 84
    107 300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C 3.26 138.96 -1.1 0.05 12.1 83
    108 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B 3.05 140.27 -1.54 -0.38 21.72 92
    109 30 GLY B, 300084 VAL C, 64 ARG C, 32 ASP B 2.96 141.28 -1.05 -0.28 26.3 89
    110 30 GLY B, 300084 VAL C, 64 ARG C 2.96 141.38 -0.23 -0.03 18.5 90
    111 30 GLY B, 300084 VAL C, 64 ARG C, 31 THR B 2.96 141.52 -0.35 -0.22 14.29 96
    112 30 GLY B, 64 ARG C, 31 THR B 2.98 141.56 -1.87 -0.66 19.01 95
    113 30 GLY B, 64 ARG C, 32 ASP B, 31 THR B 2.93 141.67 -2.2 -0.77 27.12 84
    114 30 GLY B, 64 ARG C, 32 ASP B, 31 THR B 2.89 141.77 -2.28 -0.76 26.69 92
    115 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B 2.62 142.68 -1.13 -0.28 25.87 93
    116 300084 VAL C, 64 ARG C, 31 THR B 2.53 143.07 -0.33 -0.02 17.93 96
    117 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B 2.41 144.75 -1.13 -0.28 25.87 93
    118 64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C 2.44 145.94 -2.28 -0.76 26.69 92
    119 64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C, 301001 DGA C 2.56 146.45 -2.28 -0.76 26.69 92
    120 64 ARG C, 31 THR B, 300084 VAL C, 301001 DGA C 2.62 147.45 -1.87 -0.66 19.01 95
    121 31 THR B, 300084 VAL C, 301001 DGA C 2.67 148.59 -0.55 -0.79 2.52 107
    122 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B 2.67 149.15 -1.53 -0.9 18.31 92
    123 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C 2.67 149.61 -1.33 -0.87 14.15 97
    124 31 THR B, 300084 VAL C, 301001 DGA C, 300085 THR C, 300054 ALA C 2.68 150.38 0 -0.58 1.68 104
    125 31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C 2.92 151.47 -0.78 -0.67 13.31 97
    126 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C 2.92 153.53 -0.8 -0.63 17.19 94
    127 53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C 3.04 154.88 -0.7 -0.67 13.74 94
    128 53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A 3.51 155.56 -1.46 -0.62 21.39 91
    129 53 GLU B, 300085 THR C, 300053 GLY C, 300057 ARG A 3.78 156.02 -2.28 -0.78 26.74 89
    130 53 GLU B, 300053 GLY C, 300057 ARG A 3.83 156.93 -2.8 -0.79 35.09 80

    pore with bottle neck

    pore with local minimum

  9. show | | profile | lining residues
    Pore 9 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C, 200057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 4 (10-6)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 15.45
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.28 0.27 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.22 0.45 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.19 0.63 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.21 0.78 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.24 0.94 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3.28 1.23 -1.53 -0.78 2.81 105
    7 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.31 1.63 -1.33 -0.78 2.52 106
    8 100170 THR A, 100041 ASN B, 100155 VAL A 2.59 5.4 -1.53 -0.78 2.81 105
    9 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.51 6.54 -0.2 -0.3 2.14 88
    10 100170 THR A, 100041 ASN B, 100182 LEU A 2.77 6.89 -0.13 -0.13 1.72 88
    11 100041 ASN B, 100182 LEU A, 100171 PHE A 2.76 7.24 -0.03 -0.14 2.3 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.68 7.97 -0.13 -0.31 2.57 79
    13 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.51 8.57 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.4 9.08 -0.8 -0.47 12.03 78
    15 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.31 9.67 -1.95 -0.88 15.01 90
    16 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.28 12.93 -2.25 -0.7 14.56 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A 3.12 13.27 -2.87 -0.67 18.29 79
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.24 13.81 -2.55 -0.52 14.11 74
    19 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.41 14.42 -2.55 -0.52 14.11 74
    20 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.38 16.64 -1.78 -0.53 14.11 64
    21 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.32 19.06 -1.7 -0.23 14.12 61
    22 100173 ALA A, 100041 PRO A, 100180 TYR A 3.62 21.02 -1.1 0.07 2.19 54
    23 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.31 21.38 0.13 0.34 1.68 54
    24 100041 PRO A, 100180 TYR A, 100175 LEU A 4.39 22.1 0.3 0.72 1.11 54
    25 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.47 22.56 0.13 0.34 1.68 54
    26 100041 PRO A, 100180 TYR A, 100175 LEU A 4.04 26.75 0.3 0.72 1.11 54
    27 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A 4 27.49 0.02 0.3 1.25 69
    28 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 3.99 27.96 -0.06 0.08 1.67 69
    29 100180 TYR A, 100091 SER A, 100088 SER A 4 28.17 -0.97 -0.28 1.65 94
    30 100091 SER A, 100088 SER A 4.05 28.24 -0.8 -0.97 1.67 117
    31 100180 TYR A, 100091 SER A, 100088 SER A 4.13 28.56 -0.97 -0.28 1.65 94
    32 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.33 28.8 0.23 0.08 1.27 84
    33 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.44 29.52 0.02 0.3 1.25 69
    34 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.62 29.99 0.15 -0.22 1.26 86
    35 100041 PRO A, 100091 SER A, 100088 SER A 4.7 30.48 -1.07 -0.68 1.64 97
    36 100041 PRO A, 100088 SER A 4.79 31.73 -1.2 -0.53 1.63 87
    37 100041 PRO A, 100088 SER A, 100040 ARG A 4.29 34.27 -2.3 -0.49 18.42 86
    38 100041 PRO A, 100088 SER A, 100040 ARG A 3.04 36.48 -2.17 -0.44 18.99 70
    39 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.79 36.82 -1.73 -0.53 15.09 70
    40 100088 SER A, 100040 ARG A, 100091 SER A 1.76 37.8 -1.77 -0.67 19.59 83
    41 100088 SER A, 100040 ARG A 1.22 39.77 -2.45 -0.61 27.69 83
    42 100040 ARG A 1.2 45.65 -4.5 -0.42 52 83
    43 100040 ARG A, 100043 HIS A 2.63 46.73 -3.85 -0.08 51.8 87
    44 100040 ARG A, 100043 HIS A, 100046 GLU A 3.14 47.64 -3.73 -0.43 51.17 83
    45 100040 ARG A, 100046 GLU A 3.61 50.11 -4 -0.78 50.95 80
    46 100040 ARG A, 100046 GLU A, 300018 ARG B 3.74 52.86 -4.17 -0.66 51.3 81
    47 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.52 56.19 -2 -0.04 38.51 86
    48 100046 GLU A, 300018 ARG B, 100064 ILE A 3.88 56.79 -1.17 0.08 34.01 87
    49 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.57 59.52 -0.98 -0.14 26.35 87
    50 100046 GLU A, 100064 ILE A, 100063 LYS A 3.23 60.32 0.2 -0.04 17.8 90
    51 100046 GLU A, 100064 ILE A, 100063 LYS A 2.87 64.91 -0.97 0.09 33.18 84
    52 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 5.2 65.33 -0.93 -0.18 25.3 92
    53 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 5.32 65.67 -1.1 -0.35 25.3 80
    54 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.74 69.7 0.23 0.35 24.92 76
    55 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.48 70.62 -1 -0.3 25.73 67
    56 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.27 71.19 -1.5 -0.4 21.26 76
    57 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.13 71.42 -2.4 -0.78 21.56 90
    58 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.1 71.59 -2.03 -0.87 14.58 96
    59 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.18 71.8 -2.4 -0.78 21.56 90
    60 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 4 72.68 -0.94 -0.32 11.61 84
    61 100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B 3.83 73.1 -0.3 -0.21 13.67 77
    62 100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B 3.65 73.55 -0.3 -0.21 13.67 77
    63 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.44 75.03 -1.08 -0.27 25.25 79
    64 100063 LYS A, 100003 LEU B, 100001 ASP B 3.49 76.85 -1.2 -0.1 33.11 70
    65 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 3.78 77.91 -1.08 -0.27 25.25 79
    66 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.05 78.11 -1.56 -0.42 30.14 81
    67 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4 79.04 -0.98 -0.43 25.3 83
    68 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.92 79.2 -0.2 -0.37 13.72 82
    69 100003 LEU B, 300070 ASP B, 100001 ASP B 3.13 81.2 -0.03 -0.23 17.74 70
    70 100003 LEU B, 300070 ASP B 2.18 84.35 0.15 0.05 24.92 70
    71 100003 LEU B, 300070 ASP B, 100026 SER B 2.12 86.83 -0.17 -0.29 17.17 85
    72 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.51 88.6 -1.25 -0.32 25.88 85
    73 300070 ASP B, 100026 SER B, 300024 ARG B 3.17 90.37 -2.93 -0.81 34.46 95
    74 300070 ASP B, 300024 ARG B, 100026 SER B 3.63 91.32 -2.8 -0.75 35.03 84
    75 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.69 93.37 -2.28 -0.76 26.69 92
    76 300024 ARG B, 100026 SER B, 300069 THR B 4.49 94.39 -1.87 -0.66 19.01 95
    77 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.76 95.63 -1.5 -0.7 15.11 95
    78 100026 SER B, 300069 THR B, 300026 SER B 4.31 97.99 -0.5 -0.79 2.81 107
    79 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.4 98.95 -0.48 -0.79 2.95 107
    80 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.6 101.24 -0.46 -0.79 3.04 107
    81 100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B 5.19 101.57 -1.28 -0.92 2.99 100
    82 100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B 4.16 104.53 -1.35 -0.91 2.56 102
    83 100026 SER B, 100027 GLN B, 300028 SER B 5.22 105.21 -1.57 -0.96 2.86 100
    84 100027 GLN B, 300028 SER B, 300027 GLN B 5.51 105.85 -2.6 -1.06 2.91 95
    85 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B 5.76 106.72 -2.05 -0.99 3.03 95
    86 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.17 107.73 -2.05 -0.99 3.03 95
    87 100027 GLN B, 300028 SER B, 100028 SER B 4.89 111.28 -1.7 -1.01 2.29 106
    88 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.82 111.56 -2.4 -0.87 14.72 100
    89 100027 GLN B, 100028 SER B, 100093 ARG B 4.82 111.99 -2.93 -0.83 19.07 94
    90 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.63 112.42 -2.4 -0.87 14.72 100
    91 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.35 113.04 -2.3 -0.82 15.15 94
    92 100027 GLN B, 300028 SER B, 100093 ARG B 2.42 117.76 -2.93 -0.83 19.07 94
    93 300028 SER B, 100093 ARG B 2.79 118.51 -2.65 -0.7 26.84 100
    94 300028 SER B, 100093 ARG B, 100082 TYR C 3.2 120.25 -2.2 -0.09 18.43 83
    95 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 4.38 123.34 -2.78 -0.18 26.82 83
    96 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.17 123.75 -2.3 -0.3 22.13 83
    97 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.37 124.73 -2.22 -0.27 22.47 72
    98 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C 6.51 124.95 -1.58 0.04 12.4 61
    99 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B 6.49 125.39 -2.4 0.12 22.12 66
    100 300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C 6.46 125.93 -2.4 0.12 22.12 66
    101 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.99 127.71 -1.58 0.04 12.4 61
    102 100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C 5.47 128.73 -1.88 0.25 14.65 61
    103 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 3.23 131.41 -2.43 -0.3 15.13 72
    104 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 3.34 132.14 -2.2 -0.78 15.57 83
    105 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.74 133.3 -2.43 -0.3 15.13 72
    106 100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C 3.69 133.52 -2.43 -0.3 15.13 72
    107 100093 ARG B, 200082 TYR C, 100058 GLN C 3.57 134.35 -3.1 -0.14 19.05 72
    108 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.57 134.61 -2.43 -0.3 15.13 72
    109 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.6 135.14 -2.53 -0.35 14.7 83
    110 100028 SER B, 100093 ARG B, 200082 TYR C 3.77 135.18 -2.2 -0.09 18.43 83
    111 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.75 135.91 -2.53 -0.35 14.7 83
    112 100028 SER B, 200082 TYR C, 100058 GLN C 3.33 138.3 -1.87 -0.32 2.27 83
    113 100028 SER B, 200082 TYR C, 100058 GLN C, 100030 GLY B 3.17 139.1 -1.5 -0.44 2.55 83
    114 200082 TYR C, 100058 GLN C, 100030 GLY B, 100092 ASN B 3.12 141.32 -2.18 -0.39 2.98 79
    115 200082 TYR C, 100030 GLY B, 100092 ASN B 3.25 141.66 -1.73 -0.15 2.79 77
    116 200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C 3.31 142.28 -0.25 0.17 2.13 84
    117 200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C 3.31 142.56 -1.1 0.05 12.1 83
    118 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B 3.04 143.97 -1.54 -0.38 21.72 92
    119 100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B 2.94 144.91 -1.05 -0.28 26.3 89
    120 100030 GLY B, 200084 VAL C, 100064 ARG C 2.93 144.98 -0.23 -0.03 18.5 90
    121 100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B 2.93 145.11 -0.35 -0.22 14.29 96
    122 100030 GLY B, 100064 ARG C, 100031 THR B 2.96 145.15 -1.87 -0.66 19.01 95
    123 100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B 2.99 145.23 -2.2 -0.77 27.12 84
    124 100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B 3 145.34 -2.28 -0.76 26.69 92
    125 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B 2.78 145.97 -1.13 -0.28 25.87 93
    126 200084 VAL C, 100064 ARG C, 100031 THR B 2.54 146.74 -0.33 -0.02 17.93 96
    127 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B 2.31 147.9 -1.13 -0.28 25.87 93
    128 100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C 2.18 149.18 -2.28 -0.76 26.69 92
    129 100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 201001 DGA C 2.16 150.26 -2.28 -0.76 26.69 92
    130 100064 ARG C, 100031 THR B, 200084 VAL C, 201001 DGA C 2.24 150.77 -1.87 -0.66 19.01 95
    131 100031 THR B, 200084 VAL C, 201001 DGA C 2.31 151.95 -0.55 -0.79 2.52 107
    132 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B 2.49 152.54 -1.53 -0.9 18.31 92
    133 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C 2.58 153.06 -1.25 -0.88 14.58 92
    134 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C 2.66 153.44 -1.33 -0.87 14.15 97
    135 100031 THR B, 200084 VAL C, 201001 DGA C, 200085 THR C, 200054 ALA C 2.74 153.94 0 -0.58 1.68 104
    136 100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C 2.96 155.17 -0.78 -0.67 13.31 97
    137 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C 2.89 156.81 -0.8 -0.63 17.19 94
    138 100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C 2.95 158.58 -0.7 -0.67 13.74 94
    139 100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A 3.61 159.08 -1.46 -0.62 21.39 91
    140 100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A 3.78 159.54 -2.28 -0.78 26.74 89
    141 100053 GLU B, 200053 GLY C, 200057 ARG A 3.83 160.49 -2.8 -0.79 35.09 80

    pore with bottle neck

    pore with local minimum

  10. show | | profile | lining residues
    Pore 10 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 58 GLN C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 58 GLN C, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C, 300057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 4 (10-6)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 15.24
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.28 0.28 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.21 0.46 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.18 0.65 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.81 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.21 0.97 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3.2 1.34 -1.53 -0.78 2.81 105
    7 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A 3.16 1.83 -1.14 -0.78 2.69 106
    8 100170 THR A, 100041 ASN B, 100155 VAL A 2.72 5.62 -1.53 -0.78 2.81 105
    9 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.64 6.65 -0.2 -0.3 2.14 88
    10 100170 THR A, 100041 ASN B, 100182 LEU A 2.76 7.02 -0.13 -0.13 1.72 88
    11 100041 ASN B, 100182 LEU A, 100171 PHE A 2.75 7.2 -0.03 -0.14 2.3 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.66 7.96 -0.13 -0.31 2.57 79
    13 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.78 8.48 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.7 8.96 -0.8 -0.47 12.03 78
    15 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.57 9.54 -1.95 -0.88 15.01 90
    16 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.36 12.89 -2.25 -0.7 14.56 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A 3.18 13.25 -2.87 -0.67 18.29 79
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.34 13.81 -2.55 -0.52 14.11 74
    19 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.41 14.41 -2.55 -0.52 14.11 74
    20 100153 GLU A, 100172 PRO A, 100041 PRO A 3.39 14.76 -2.23 -0.44 17.69 64
    21 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.39 16.66 -1.78 -0.53 14.11 64
    22 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.32 19.12 -1.7 -0.23 14.12 61
    23 100173 ALA A, 100041 PRO A, 100180 TYR A 3.7 21.08 -1.1 0.07 2.19 54
    24 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.47 21.42 0.13 0.34 1.68 54
    25 100041 PRO A, 100180 TYR A, 100175 LEU A 4.37 22.03 0.3 0.72 1.11 54
    26 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.32 22.73 0.13 0.34 1.68 54
    27 100041 PRO A, 100180 TYR A, 100175 LEU A 4.23 27.1 0.3 0.72 1.11 54
    28 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.52 27.74 -0.06 0.08 1.67 69
    29 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.57 28.09 0.02 0.3 1.25 69
    30 100180 TYR A, 100091 SER A, 100088 SER A 4.57 28.22 -0.97 -0.28 1.65 94
    31 100091 SER A, 100088 SER A 4.53 28.31 -0.8 -0.97 1.67 117
    32 100180 TYR A, 100091 SER A, 100088 SER A 4.47 28.48 -0.97 -0.28 1.65 94
    33 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.39 28.97 0.23 0.08 1.27 84
    34 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.39 29.34 0.02 0.3 1.25 69
    35 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.44 29.78 0.15 -0.22 1.26 86
    36 100041 PRO A, 100091 SER A, 100088 SER A 4.52 30.78 -1.07 -0.68 1.64 97
    37 100041 PRO A, 100088 SER A 4.82 31.91 -1.2 -0.53 1.63 87
    38 100041 PRO A, 100088 SER A, 100040 ARG A 4.53 34.08 -2.3 -0.49 18.42 86
    39 100041 PRO A, 100088 SER A, 100040 ARG A 3.15 36.4 -2.17 -0.44 18.99 70
    40 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.69 37.07 -1.73 -0.53 15.09 70
    41 100088 SER A, 100040 ARG A, 100091 SER A 2.11 38.42 -1.77 -0.67 19.59 83
    42 100088 SER A, 100040 ARG A 1.79 39.56 -2.45 -0.61 27.69 83
    43 100040 ARG A 0.97 45.52 -4.5 -0.42 52 83
    44 100040 ARG A, 100043 HIS A 1.5 46.65 -3.85 -0.08 51.8 87
    45 100040 ARG A, 100046 GLU A 2.15 50.09 -4 -0.78 50.95 80
    46 100040 ARG A, 100046 GLU A, 100064 ILE A 4.18 50.75 -1.17 0.08 34.01 87
    47 100040 ARG A, 100046 GLU A, 300018 ARG B 3.81 52.89 -4.17 -0.66 51.3 81
    48 100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B 3.57 56.3 -2 -0.04 38.51 86
    49 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A 3.26 59.72 -0.98 -0.14 26.35 87
    50 100046 GLU A, 100064 ILE A, 100063 LYS A 3.01 60.52 0.2 -0.04 17.8 90
    51 100046 GLU A, 100064 ILE A, 100063 LYS A 2.88 65.1 -0.97 0.09 33.18 84
    52 100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B 5.17 65.91 -1.1 -0.35 25.3 80
    53 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.74 70.15 0.23 0.35 24.92 76
    54 100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B 4.24 71.35 -1.5 -0.4 21.26 76
    55 100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B 4.13 71.74 -2.03 -0.87 14.58 96
    56 100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B 4.2 71.96 -2.4 -0.78 21.56 90
    57 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B 3.9 72.96 -0.94 -0.32 11.61 84
    58 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.72 73.4 -1.08 -0.2 13.67 84
    59 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.44 75.46 -1.08 -0.27 25.25 79
    60 100063 LYS A, 100003 LEU B, 100001 ASP B 3.54 77.23 -1.2 -0.1 33.11 70
    61 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 3.84 78.1 -1.08 -0.27 25.25 79
    62 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.05 78.31 -1.56 -0.42 30.14 81
    63 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.02 79.07 -0.98 -0.43 25.3 83
    64 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.95 79.23 -0.2 -0.37 13.72 82
    65 100003 LEU B, 300070 ASP B, 100001 ASP B 3.08 81.28 -0.03 -0.23 17.74 70
    66 100003 LEU B, 300070 ASP B 2.12 84.46 0.15 0.05 24.92 70
    67 100003 LEU B, 300070 ASP B, 100026 SER B 2.08 86.98 -0.17 -0.29 17.17 85
    68 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.65 88.76 -1.25 -0.32 25.88 85
    69 300070 ASP B, 100026 SER B, 300024 ARG B 3.3 90.43 -2.93 -0.81 34.46 95
    70 300070 ASP B, 300024 ARG B, 100026 SER B 3.64 91.52 -2.8 -0.75 35.03 84
    71 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.73 93.12 -2.28 -0.76 26.69 92
    72 300024 ARG B, 100026 SER B, 300069 THR B 4.33 94.62 -1.87 -0.66 19.01 95
    73 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.95 95.5 -1.5 -0.7 15.11 95
    74 100026 SER B, 300069 THR B, 300026 SER B 4.48 98.67 -0.5 -0.79 2.81 107
    75 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.48 99.61 -0.48 -0.79 2.95 107
    76 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.58 101.24 -0.46 -0.79 3.04 107
    77 100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B 5.05 101.39 -0.58 -0.84 2.52 112
    78 100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B 5.11 101.56 -1.28 -0.92 2.99 100
    79 100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B 4.2 104.5 -1.35 -0.91 2.56 102
    80 100026 SER B, 300028 SER B, 100027 GLN B 5.28 105.19 -1.57 -0.96 2.86 100
    81 300028 SER B, 100027 GLN B, 300027 GLN B 5.74 105.84 -2.6 -1.06 2.91 95
    82 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B 6.16 106.75 -2.05 -0.99 3.03 95
    83 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.23 107.79 -2.05 -0.99 3.03 95
    84 300028 SER B, 100027 GLN B, 100028 SER B 4.95 111.35 -1.7 -1.01 2.29 106
    85 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.87 111.5 -2.4 -0.87 14.72 100
    86 100027 GLN B, 100028 SER B, 100093 ARG B 4.84 112.11 -2.93 -0.83 19.07 94
    87 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.74 112.61 -2.4 -0.87 14.72 100
    88 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.49 113.29 -2.3 -0.82 15.15 94
    89 300028 SER B, 100027 GLN B, 100093 ARG B 2.47 118.66 -2.93 -0.83 19.07 94
    90 300028 SER B, 100093 ARG B, 100082 TYR C 3.4 120.29 -2.2 -0.09 18.43 83
    91 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 3.83 120.66 -2.78 -0.18 26.82 83
    92 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.67 121.66 -2.53 -0.35 14.7 83
    93 300028 SER B, 300093 ARG B, 300058 GLN C 3.58 121.96 -2.93 -0.83 19.07 94
    94 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.69 122.64 -2.53 -0.35 14.7 83
    95 100082 TYR C, 300093 ARG B, 300058 GLN C 3.66 123.6 -3.1 -0.14 19.05 72
    96 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C 3.71 123.79 -2.43 -0.3 15.13 72
    97 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C 3.54 125.22 -2.43 -0.3 15.13 72
    98 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C 3.31 125.57 -2.2 -0.78 15.57 83
    99 300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C 3.16 129.57 -2.43 -0.3 15.13 72
    100 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C 5.36 131.21 -1.58 0.04 12.4 61
    101 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B 6.05 131.62 -2.22 -0.27 22.47 72
    102 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.29 131.82 -2.4 0.12 22.12 66
    103 100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.62 132 -2.4 0.12 22.12 66
    104 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.71 132.25 -2.4 0.12 22.12 66
    105 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C 6.73 132.52 -2.22 -0.27 22.47 72
    106 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B 6.38 133.59 -2.22 -0.27 22.47 72
    107 300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B 6.13 134.08 -2.3 -0.3 22.13 83
    108 300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B 4.68 136.72 -2.78 -0.18 26.82 83
    109 300082 TYR C, 93 ARG B, 28 SER B 4.01 137.86 -2.2 -0.09 18.43 83
    110 300082 TYR C, 93 ARG B, 28 SER B, 58 GLN C 3.7 138.89 -2.53 -0.35 14.7 83
    111 300082 TYR C, 28 SER B, 58 GLN C 3.3 141.31 -1.87 -0.32 2.27 83
    112 300082 TYR C, 28 SER B, 58 GLN C, 30 GLY B 3.15 142.21 -1.5 -0.44 2.55 83
    113 300082 TYR C, 58 GLN C, 30 GLY B, 92 ASN B 3.1 144.48 -2.18 -0.39 2.98 79
    114 300082 TYR C, 30 GLY B, 92 ASN B 3.25 144.82 -1.73 -0.15 2.79 77
    115 300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C 3.27 145.43 -0.25 0.17 2.13 84
    116 300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C 3.23 145.72 -1.1 0.05 12.1 83
    117 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B 3.07 146.83 -1.54 -0.38 21.72 92
    118 30 GLY B, 300084 VAL C, 64 ARG C, 32 ASP B 2.95 148.08 -1.05 -0.28 26.3 89
    119 30 GLY B, 300084 VAL C, 64 ARG C 2.96 148.14 -0.23 -0.03 18.5 90
    120 30 GLY B, 300084 VAL C, 64 ARG C, 31 THR B 2.96 148.23 -0.35 -0.22 14.29 96
    121 30 GLY B, 64 ARG C, 31 THR B 3 148.27 -1.87 -0.66 19.01 95
    122 30 GLY B, 64 ARG C, 32 ASP B, 31 THR B 3 148.34 -2.2 -0.77 27.12 84
    123 30 GLY B, 64 ARG C, 32 ASP B 2.97 148.41 -2.8 -0.75 35.03 84
    124 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B 2.65 149.25 -1.13 -0.28 25.87 93
    125 300084 VAL C, 64 ARG C, 31 THR B 2.41 150.12 -0.33 -0.02 17.93 96
    126 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B 2.21 151.36 -1.13 -0.28 25.87 93
    127 64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C 2.15 152.62 -2.28 -0.76 26.69 92
    128 64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C, 301001 DGA C 2.19 153.17 -2.28 -0.76 26.69 92
    129 64 ARG C, 31 THR B, 300084 VAL C, 301001 DGA C 2.26 153.67 -1.87 -0.66 19.01 95
    130 31 THR B, 300084 VAL C, 301001 DGA C 2.36 155.44 -0.55 -0.79 2.52 107
    131 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C 2.68 156.01 -1.25 -0.88 14.58 92
    132 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C 2.76 156.46 -1.33 -0.87 14.15 97
    133 31 THR B, 300084 VAL C, 301001 DGA C, 300085 THR C, 300054 ALA C 2.84 157.05 0 -0.58 1.68 104
    134 31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C 2.94 158.2 -0.78 -0.67 13.31 97
    135 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C 2.87 159.85 -0.8 -0.63 17.19 94
    136 53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C 2.93 161.7 -0.7 -0.67 13.74 94
    137 53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A 3.61 162.21 -1.46 -0.62 21.39 91
    138 53 GLU B, 300085 THR C, 300053 GLY C, 300057 ARG A 3.79 162.68 -2.28 -0.78 26.74 89
    139 53 GLU B, 300053 GLY C, 300057 ARG A 3.83 163.63 -2.8 -0.79 35.09 80

    pore with bottle neck

    pore with local minimum

  11. show | | profile | lining residues
    Pore 11 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 300082 TYR C, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C, 57 ARG A

    Physicochemical properties of lining side-chains

    Charge: 3 (10-7)
    Hydropathy: -1.6
    Hydrophobicity: -0.38
    Polarity: 16.43
    Mutability: 88

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.31 0.13 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.13 1.87 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.16 3.94 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.62 4.15 -1.94 -0.69 11.94 88
    5 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.65 4.74 -2.25 -0.68 14.51 82
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.72 5.04 -1.78 -0.44 2.48 73
    7 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.71 5.29 -1.78 -0.44 2.48 73
    8 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.61 6.27 -1.78 -0.44 2.48 73
    9 100041 ASN B, 100172 PRO A, 100041 PRO A 3.57 6.58 -2.23 -0.32 2.18 73
    10 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.48 7.1 -2.55 -0.52 14.11 74
    11 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.4 7.63 -2.55 -0.52 14.11 74
    12 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A 3.38 9.99 -1.78 -0.53 14.11 64
    13 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A 3.38 12.23 -1.7 -0.23 14.12 61
    14 100041 PRO A, 100173 ALA A, 100180 TYR A 3.7 14.17 -1.1 0.07 2.19 54
    15 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.3 14.68 0.13 0.34 1.68 54
    16 100041 PRO A, 100180 TYR A, 100175 LEU A 4.38 15.32 0.3 0.72 1.11 54
    17 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.48 15.94 0.13 0.34 1.68 54
    18 100041 PRO A, 100180 TYR A, 100175 LEU A 4.11 20.63 0.3 0.72 1.11 54
    19 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.07 21.13 -0.06 0.08 1.67 69
    20 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.04 21.4 0.23 0.08 1.27 84
    21 100180 TYR A, 100091 SER A, 100088 SER A 4.04 21.49 -0.97 -0.28 1.65 94
    22 100091 SER A, 100088 SER A 4.07 21.58 -0.8 -0.97 1.67 117
    23 100180 TYR A, 100091 SER A, 100088 SER A 4.12 21.93 -0.97 -0.28 1.65 94
    24 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.3 22.16 0.23 0.08 1.27 84
    25 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.41 22.48 0.02 0.3 1.25 69
    26 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.51 23.3 0.15 -0.22 1.26 86
    27 100041 PRO A, 100091 SER A, 100088 SER A 4.7 23.76 -1.07 -0.68 1.64 97
    28 100041 PRO A, 100088 SER A 4.8 24.94 -1.2 -0.53 1.63 87
    29 100041 PRO A, 100088 SER A, 100040 ARG A 4.19 27.69 -2.3 -0.49 18.42 86
    30 100041 PRO A, 100088 SER A, 100040 ARG A 3.01 29.73 -2.17 -0.44 18.99 70
    31 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.79 30.05 -1.73 -0.53 15.09 70
    32 100088 SER A, 100040 ARG A, 100091 SER A 1.7 31.45 -1.77 -0.67 19.59 83
    33 100088 SER A, 100040 ARG A 1.48 32.37 -2.45 -0.61 27.69 83
    34 100040 ARG A 1.36 39.05 -4.5 -0.42 52 83
    35 100040 ARG A, 100043 HIS A 2.45 40.04 -3.85 -0.08 51.8 87
    36 100040 ARG A, 100043 HIS A, 100046 GLU A 2.91 40.89 -3.73 -0.43 51.17 83
    37 100040 ARG A, 100046 GLU A 3.37 43.84 -4 -0.78 50.95 80
    38 100040 ARG A, 100046 GLU A, 300018 ARG B 3.84 45.79 -4.17 -0.66 51.3 81
    39 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.56 49.78 -2 -0.04 38.51 86
    40 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.26 52.92 -0.98 -0.14 26.35 87
    41 100046 GLU A, 100064 ILE A, 100063 LYS A 3.07 53.66 0.2 -0.04 17.8 90
    42 100046 GLU A, 100064 ILE A, 100063 LYS A 2.95 57.93 -0.97 0.09 33.18 84
    43 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 5.05 58.45 -0.93 -0.18 25.3 92
    44 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 5.46 59.17 -1.1 -0.35 25.3 80
    45 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.78 63.05 0.23 0.35 24.92 76
    46 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.38 63.9 -1 -0.3 25.73 67
    47 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.1 64.45 -1.5 -0.4 21.26 76
    48 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.97 64.71 -2.4 -0.78 21.56 90
    49 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.95 65.04 -2.03 -0.87 14.58 96
    50 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.06 65.25 -2.4 -0.78 21.56 90
    51 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.89 66.14 -0.94 -0.32 11.61 84
    52 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.79 66.54 -1.08 -0.2 13.67 84
    53 100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B 3.69 66.95 -0.3 -0.21 13.67 77
    54 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.51 68.33 -1.08 -0.27 25.25 79
    55 100063 LYS A, 100003 LEU B, 100001 ASP B 3.54 70.5 -1.2 -0.1 33.11 70
    56 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 4.07 71.33 -1.08 -0.27 25.25 79
    57 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.19 71.52 -1.56 -0.42 30.14 81
    58 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.94 72.46 -0.98 -0.43 25.3 83
    59 100003 LEU B, 300070 ASP B, 100001 ASP B 2.96 74.76 -0.03 -0.23 17.74 70
    60 100003 LEU B, 300070 ASP B 2.08 77.7 0.15 0.05 24.92 70
    61 100003 LEU B, 300070 ASP B, 100026 SER B 2.01 80.45 -0.17 -0.29 17.17 85
    62 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.76 82.07 -1.25 -0.32 25.88 85
    63 300070 ASP B, 100026 SER B, 300024 ARG B 3.39 83.71 -2.93 -0.81 34.46 95
    64 300070 ASP B, 300024 ARG B, 100026 SER B 3.64 84.73 -2.8 -0.75 35.03 84
    65 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.71 86.66 -2.28 -0.76 26.69 92
    66 300024 ARG B, 100026 SER B, 300069 THR B 4.46 87.95 -1.87 -0.66 19.01 95
    67 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 5 88.68 -1.5 -0.7 15.11 95
    68 100026 SER B, 300069 THR B, 300026 SER B 4.33 91.37 -0.5 -0.79 2.81 107
    69 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.32 92.26 -0.48 -0.79 2.95 107
    70 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.44 94.52 -0.46 -0.79 3.04 107
    71 100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B 5.19 94.67 -0.58 -0.84 2.52 112
    72 100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B 5.21 94.81 -1.28 -0.92 2.99 100
    73 100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B 4.17 97.69 -1.35 -0.91 2.56 102
    74 100026 SER B, 300028 SER B, 100027 GLN B 5.19 98.32 -1.57 -0.96 2.86 100
    75 300027 GLN B, 300028 SER B, 100027 GLN B 5.49 98.94 -1.57 -0.96 2.86 100
    76 300028 SER B, 100027 GLN B, 100028 SER B, 300027 GLN B 5.73 99.89 -2.05 -0.99 3.03 95
    77 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.06 101.07 -2.05 -0.99 3.03 95
    78 300028 SER B, 100027 GLN B, 100028 SER B 4.96 104.5 -1.7 -1.01 2.29 106
    79 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.82 104.83 -2.4 -0.87 14.72 100
    80 100027 GLN B, 100028 SER B, 100093 ARG B 4.79 105.38 -2.93 -0.83 19.07 94
    81 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.61 105.79 -2.4 -0.87 14.72 100
    82 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.36 106.37 -2.3 -0.82 15.15 94
    83 300028 SER B, 100027 GLN B, 100093 ARG B 2.43 111.41 -2.93 -0.83 19.07 94
    84 300028 SER B, 100093 ARG B 2.98 112.1 -2.65 -0.7 26.84 100
    85 300028 SER B, 100093 ARG B, 100082 TYR C 3.38 113.65 -2.2 -0.09 18.43 83
    86 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 4.38 116.51 -2.78 -0.18 26.82 83
    87 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.06 117.28 -2.3 -0.3 22.13 83
    88 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.37 117.88 -2.22 -0.27 22.47 72
    89 300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C 6.5 118.12 -2.22 -0.27 22.47 72
    90 93 ARG B, 79 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C 6.56 118.3 -2.22 -0.27 22.47 72
    91 93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C 6.65 118.68 -2.4 0.12 22.12 66
    92 300093 ARG B, 93 ARG B, 79 GLY C, 300082 TYR C, 82 TYR C 6.85 119.13 -2.4 0.12 22.12 66
    93 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.75 121.54 -1.58 0.04 12.4 61
    94 100093 ARG B, 100082 TYR C, 100079 GLY C 5.08 122.44 -2.07 -0.04 19 66
    95 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 3 124.8 -2.43 -0.3 15.13 72
    96 100093 ARG B, 100079 GLY C, 100058 GLN C 2.87 125.1 -2.8 -0.77 19.64 83
    97 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 2.88 126.41 -2.2 -0.78 15.57 83
    98 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.7 127.9 -2.43 -0.3 15.13 72
    99 100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C 4.6 129.61 -2.2 -0.02 12.43 66
    100 100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C 5.45 130.39 -2.4 0.12 22.12 66
    101 100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C 5.82 131.52 -2.22 -0.27 22.47 72
    102 300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C 6.48 131.97 -2.22 -0.27 22.47 72
    103 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B 7.03 132.28 -2.3 -0.3 22.13 83
    104 100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C 7.19 132.69 -2.4 0.12 22.12 66
    105 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C 7 133.33 -2.4 0.12 22.12 66
    106 100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 5.91 135.08 -1.58 0.04 12.4 61
    107 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 5.18 136 -1.88 0.25 14.65 61
    108 200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C 3.24 138.49 -2.43 -0.3 15.13 72
    109 200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C 3.28 139.46 -2.2 -0.78 15.57 83
    110 200093 ARG B, 82 TYR C, 200079 GLY C, 200058 GLN C 3.65 140.46 -2.43 -0.3 15.13 72
    111 200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C 3.66 140.66 -2.43 -0.3 15.13 72
    112 200093 ARG B, 82 TYR C, 200058 GLN C 3.58 141.68 -3.1 -0.14 19.05 72
    113 200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C 3.72 142.24 -2.53 -0.35 14.7 83
    114 200028 SER B, 200093 ARG B, 82 TYR C 3.84 142.29 -2.2 -0.09 18.43 83
    115 200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C 3.61 143.08 -2.53 -0.35 14.7 83
    116 200028 SER B, 82 TYR C, 200058 GLN C 3.25 145.32 -1.87 -0.32 2.27 83
    117 200028 SER B, 82 TYR C, 200058 GLN C, 200030 GLY B 3.12 146.37 -1.5 -0.44 2.55 83
    118 82 TYR C, 200058 GLN C, 200030 GLY B, 200092 ASN B 3.12 148.29 -2.18 -0.39 2.98 79
    119 82 TYR C, 200030 GLY B, 200092 ASN B 3.19 148.62 -1.73 -0.15 2.79 77
    120 82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C 3.2 149.44 -0.25 0.17 2.13 84
    121 82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C 3.24 149.7 -1.1 0.05 12.1 83
    122 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B 3.1 151 -1.54 -0.38 21.72 92
    123 200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B 2.97 151.97 -1.05 -0.28 26.3 89
    124 200030 GLY B, 84 VAL C, 200064 ARG C 2.95 152.13 -0.23 -0.03 18.5 90
    125 200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B 2.95 152.25 -0.35 -0.22 14.29 96
    126 200030 GLY B, 200064 ARG C, 200031 THR B 2.95 152.28 -1.87 -0.66 19.01 95
    127 200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B 2.91 152.42 -2.2 -0.77 27.12 84
    128 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B 2.89 152.55 -1.13 -0.28 25.87 93
    129 84 VAL C, 200064 ARG C, 200031 THR B 2.86 152.71 -0.33 -0.02 17.93 96
    130 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B 2.77 153.2 -1.13 -0.28 25.87 93
    131 84 VAL C, 200064 ARG C, 200031 THR B 2.66 153.94 -0.33 -0.02 17.93 96
    132 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B 2.52 155.03 -1.13 -0.28 25.87 93
    133 200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C 2.39 156.22 -2.28 -0.76 26.69 92
    134 200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 1001 DGA C 2.32 157.24 -2.28 -0.76 26.69 92
    135 200064 ARG C, 200031 THR B, 84 VAL C, 1001 DGA C 2.33 157.71 -1.87 -0.66 19.01 95
    136 200031 THR B, 84 VAL C, 1001 DGA C 2.36 159.33 -0.55 -0.79 2.52 107
    137 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B 2.53 159.86 -1.53 -0.9 18.31 92
    138 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C 2.58 160.31 -1.33 -0.87 14.15 97
    139 200031 THR B, 84 VAL C, 1001 DGA C, 85 THR C, 54 ALA C 2.64 161.07 0 -0.58 1.68 104
    140 200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C 2.94 162.42 -0.78 -0.67 13.31 97
    141 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C 2.9 163.96 -0.8 -0.63 17.19 94
    142 200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C 2.97 165.65 -0.7 -0.67 13.74 94
    143 200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A 3.56 166.29 -1.46 -0.62 21.39 91
    144 200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A 3.79 166.75 -2.28 -0.78 26.74 89
    145 200053 GLU B, 53 GLY C, 57 ARG A 3.83 167.63 -2.8 -0.79 35.09 80

    pore with bottle neck

    pore with local minimum

  12. show | | profile | lining residues
    Pore 12 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C, 57 ARG A

    Physicochemical properties of lining side-chains

    Charge: 4 (10-6)
    Hydropathy: -1.6
    Hydrophobicity: -0.4
    Polarity: 15.56
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.29 0.25 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.23 0.44 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.18 0.7 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.86 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.19 1 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3.08 1.38 -1.53 -0.78 2.81 105
    7 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A 3.02 1.86 -1.14 -0.78 2.69 106
    8 100170 THR A, 100041 ASN B, 100155 VAL A 2.77 5.54 -1.53 -0.78 2.81 105
    9 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.73 6.57 -0.2 -0.3 2.14 88
    10 100170 THR A, 100041 ASN B, 100182 LEU A 2.76 6.91 -0.13 -0.13 1.72 88
    11 100041 ASN B, 100182 LEU A, 100171 PHE A 2.74 7.25 -0.03 -0.14 2.3 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.62 7.95 -0.13 -0.31 2.57 79
    13 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.59 8.42 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.56 8.86 -0.8 -0.47 12.03 78
    15 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.5 10 -1.95 -0.88 15.01 90
    16 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.48 12.7 -2.25 -0.7 14.56 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A 3.04 13.38 -2.87 -0.67 18.29 79
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.43 13.91 -2.55 -0.52 14.11 74
    19 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.57 14.51 -2.55 -0.52 14.11 74
    20 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.29 16.68 -1.78 -0.53 14.11 64
    21 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.28 19.02 -1.7 -0.23 14.12 61
    22 100173 ALA A, 100041 PRO A, 100180 TYR A 3.52 21 -1.1 0.07 2.19 54
    23 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.31 21.38 0.13 0.34 1.68 54
    24 100041 PRO A, 100180 TYR A, 100175 LEU A 4.39 22.07 0.3 0.72 1.11 54
    25 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.46 22.73 0.13 0.34 1.68 54
    26 100041 PRO A, 100180 TYR A, 100175 LEU A 4.08 26.92 0.3 0.72 1.11 54
    27 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.04 27.6 -0.06 0.08 1.67 69
    28 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.02 28.03 0.02 0.3 1.25 69
    29 100180 TYR A, 100091 SER A, 100088 SER A 4.02 28.21 -0.97 -0.28 1.65 94
    30 100091 SER A, 100088 SER A 4.05 28.28 -0.8 -0.97 1.67 117
    31 100180 TYR A, 100091 SER A, 100088 SER A 4.09 28.6 -0.97 -0.28 1.65 94
    32 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.24 28.83 0.23 0.08 1.27 84
    33 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.34 29.52 0.02 0.3 1.25 69
    34 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.55 29.97 0.15 -0.22 1.26 86
    35 100041 PRO A, 100091 SER A, 100088 SER A 4.66 30.45 -1.07 -0.68 1.64 97
    36 100041 PRO A, 100088 SER A 4.78 31.7 -1.2 -0.53 1.63 87
    37 100041 PRO A, 100088 SER A, 100040 ARG A 4.63 34.03 -2.3 -0.49 18.42 86
    38 100041 PRO A, 100088 SER A, 100040 ARG A 3.03 36.31 -2.17 -0.44 18.99 70
    39 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.69 36.99 -1.73 -0.53 15.09 70
    40 100088 SER A, 100040 ARG A, 100091 SER A 1.7 38.06 -1.77 -0.67 19.59 83
    41 100088 SER A, 100040 ARG A 1.11 38.95 -2.45 -0.61 27.69 83
    42 100040 ARG A -0.01 45.89 -4.5 -0.42 52 83
    43 100040 ARG A, 100043 HIS A 1.63 46.91 -3.85 -0.08 51.8 87
    44 100040 ARG A, 100046 GLU A 2.46 50.17 -4 -0.78 50.95 80
    45 100040 ARG A, 100046 GLU A, 300018 ARG B 4.11 52.84 -4.17 -0.66 51.3 81
    46 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.57 56.59 -2 -0.04 38.51 86
    47 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.12 59.94 -0.98 -0.14 26.35 87
    48 100046 GLU A, 100064 ILE A, 100063 LYS A 3.01 60.69 0.2 -0.04 17.8 90
    49 100046 GLU A, 100064 ILE A, 100063 LYS A 3.01 65.09 -0.97 0.09 33.18 84
    50 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 5.16 65.44 -0.93 -0.18 25.3 92
    51 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 5.44 65.83 -1.1 -0.35 25.3 80
    52 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.95 69.84 0.23 0.35 24.92 76
    53 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.61 70.72 -1 -0.3 25.73 67
    54 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.32 71.25 -1.5 -0.4 21.26 76
    55 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.16 71.48 -2.4 -0.78 21.56 90
    56 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.11 71.63 -2.03 -0.87 14.58 96
    57 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.17 72.06 -2.4 -0.78 21.56 90
    58 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.98 72.67 -0.94 -0.32 11.61 84
    59 100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B 3.82 73.08 -0.3 -0.21 13.67 77
    60 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.66 73.51 -1.08 -0.2 13.67 84
    61 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.45 75.5 -1.08 -0.27 25.25 79
    62 100063 LYS A, 100003 LEU B, 100001 ASP B 3.55 77.2 -1.2 -0.1 33.11 70
    63 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 3.83 78.07 -1.08 -0.27 25.25 79
    64 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.04 78.27 -1.56 -0.42 30.14 81
    65 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4 79.13 -0.98 -0.43 25.3 83
    66 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.93 79.29 -0.2 -0.37 13.72 82
    67 100003 LEU B, 300070 ASP B, 100001 ASP B 3.09 81.18 -0.03 -0.23 17.74 70
    68 100003 LEU B, 300070 ASP B 2.13 84.23 0.15 0.05 24.92 70
    69 100003 LEU B, 300070 ASP B, 100026 SER B 2.02 87.13 -0.17 -0.29 17.17 85
    70 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.68 88.83 -1.25 -0.32 25.88 85
    71 300070 ASP B, 100026 SER B, 300024 ARG B 3.41 90.44 -2.93 -0.81 34.46 95
    72 300070 ASP B, 300024 ARG B, 100026 SER B 3.64 91.38 -2.8 -0.75 35.03 84
    73 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.72 93.37 -2.28 -0.76 26.69 92
    74 300024 ARG B, 100026 SER B, 300069 THR B 4.39 94.7 -1.87 -0.66 19.01 95
    75 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.77 95.54 -1.5 -0.7 15.11 95
    76 100026 SER B, 300069 THR B, 300026 SER B 4.45 98.59 -0.5 -0.79 2.81 107
    77 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.66 99.5 -0.48 -0.79 2.95 107
    78 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.82 101.2 -0.46 -0.79 3.04 107
    79 100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B 5.16 101.36 -0.58 -0.84 2.52 112
    80 100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B 5.16 101.51 -1.28 -0.92 2.99 100
    81 100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B 4.16 104.66 -1.35 -0.91 2.56 102
    82 100026 SER B, 300028 SER B, 100027 GLN B 5.24 105.32 -1.57 -0.96 2.86 100
    83 300028 SER B, 100027 GLN B, 300027 GLN B 5.51 105.94 -2.6 -1.06 2.91 95
    84 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B 5.76 106.78 -2.05 -0.99 3.03 95
    85 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.14 107.72 -2.05 -0.99 3.03 95
    86 300028 SER B, 100027 GLN B, 100028 SER B 5 111.26 -1.7 -1.01 2.29 106
    87 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.87 111.58 -2.4 -0.87 14.72 100
    88 100027 GLN B, 100028 SER B, 100093 ARG B 4.93 111.94 -2.93 -0.83 19.07 94
    89 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.53 112.77 -2.4 -0.87 14.72 100
    90 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.14 113.44 -2.3 -0.82 15.15 94
    91 300028 SER B, 100027 GLN B, 100093 ARG B 2.53 118.04 -2.93 -0.83 19.07 94
    92 300028 SER B, 100093 ARG B 2.81 118.76 -2.65 -0.7 26.84 100
    93 300028 SER B, 100093 ARG B, 100082 TYR C 3.1 120.39 -2.2 -0.09 18.43 83
    94 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 4.21 123.39 -2.78 -0.18 26.82 83
    95 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.18 123.8 -2.3 -0.3 22.13 83
    96 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.44 124.75 -2.22 -0.27 22.47 72
    97 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C 7.03 124.97 -1.58 0.04 12.4 61
    98 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B 6.96 125.33 -2.4 0.12 22.12 66
    99 300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C 6.71 125.75 -2.4 0.12 22.12 66
    100 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.33 126.43 -2.22 -0.27 22.47 72
    101 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.31 128.24 -1.58 0.04 12.4 61
    102 100093 ARG B, 100082 TYR C, 100079 GLY C 4.74 129.18 -2.07 -0.04 19 66
    103 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 2.99 131.58 -2.43 -0.3 15.13 72
    104 100093 ARG B, 100079 GLY C, 100058 GLN C 2.84 131.89 -2.8 -0.77 19.64 83
    105 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 2.86 132.76 -2.2 -0.78 15.57 83
    106 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.39 135.06 -2.43 -0.3 15.13 72
    107 100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C 4.8 135.96 -2.2 -0.02 12.43 66
    108 100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C 5.26 136.82 -2.4 0.12 22.12 66
    109 100093 ARG B, 100079 GLY C, 200079 GLY C, 200093 ARG B, 200082 TYR C 5.7 138.11 -2.22 -0.27 22.47 72
    110 300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C 6.46 138.66 -2.22 -0.27 22.47 72
    111 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B 7.03 138.96 -2.3 -0.3 22.13 83
    112 100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C 7.17 139.38 -2.4 0.12 22.12 66
    113 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C 6.97 140.05 -2.4 0.12 22.12 66
    114 100079 GLY C, 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C 5.9 141.89 -1.58 0.04 12.4 61
    115 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C 5.17 142.85 -1.88 0.25 14.65 61
    116 200079 GLY C, 200093 ARG B, 200082 TYR C, 200058 GLN C 3.29 145.31 -2.43 -0.3 15.13 72
    117 200079 GLY C, 200093 ARG B, 200058 GLN C, 200080 ASP C 3.41 146.01 -2.2 -0.78 15.57 83
    118 82 TYR C, 200079 GLY C, 200093 ARG B, 200058 GLN C 3.69 147.12 -2.43 -0.3 15.13 72
    119 82 TYR C, 200093 ARG B, 200058 GLN C, 200080 ASP C 3.7 147.33 -2.43 -0.3 15.13 72
    120 82 TYR C, 200093 ARG B, 200058 GLN C 3.56 148.39 -3.1 -0.14 19.05 72
    121 200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C 3.58 148.95 -2.53 -0.35 14.7 83
    122 200028 SER B, 82 TYR C, 200093 ARG B 3.76 149 -2.2 -0.09 18.43 83
    123 200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C 3.76 149.55 -2.53 -0.35 14.7 83
    124 200028 SER B, 82 TYR C, 200058 GLN C 3.43 151.82 -1.87 -0.32 2.27 83
    125 200028 SER B, 82 TYR C, 200058 GLN C, 200030 GLY B 3.2 153.03 -1.5 -0.44 2.55 83
    126 82 TYR C, 200058 GLN C, 200030 GLY B, 200092 ASN B 3.16 155.15 -2.18 -0.39 2.98 79
    127 82 TYR C, 200030 GLY B, 200092 ASN B 3.18 155.48 -1.73 -0.15 2.79 77
    128 82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C 3.2 156.1 -0.25 0.17 2.13 84
    129 82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C 3.25 156.36 -1.1 0.05 12.1 83
    130 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B 3.1 157.7 -1.54 -0.38 21.72 92
    131 200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B 2.98 158.7 -1.05 -0.28 26.3 89
    132 200030 GLY B, 84 VAL C, 200064 ARG C 2.97 158.8 -0.23 -0.03 18.5 90
    133 200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B 2.96 158.93 -0.35 -0.22 14.29 96
    134 200030 GLY B, 200064 ARG C, 200031 THR B 2.97 158.97 -1.87 -0.66 19.01 95
    135 200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B 2.94 159.03 -2.2 -0.77 27.12 84
    136 200030 GLY B, 200064 ARG C, 200032 ASP B 2.92 159.09 -2.8 -0.75 35.03 84
    137 200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B 2.88 159.21 -2.28 -0.76 26.69 92
    138 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B 2.67 159.87 -1.13 -0.28 25.87 93
    139 84 VAL C, 200064 ARG C, 200031 THR B 2.46 160.64 -0.33 -0.02 17.93 96
    140 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B 2.3 161.78 -1.13 -0.28 25.87 93
    141 200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C 2.27 163.03 -2.28 -0.76 26.69 92
    142 200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 1001 DGA C 2.35 164.08 -2.28 -0.76 26.69 92
    143 200064 ARG C, 200031 THR B, 84 VAL C, 1001 DGA C 2.54 164.57 -1.87 -0.66 19.01 95
    144 200031 THR B, 84 VAL C, 1001 DGA C 2.65 165.71 -0.55 -0.79 2.52 107
    145 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B 2.85 166.29 -1.53 -0.9 18.31 92
    146 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C 2.92 166.81 -1.25 -0.88 14.58 92
    147 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C 2.97 167.22 -1.33 -0.87 14.15 97
    148 200031 THR B, 84 VAL C, 1001 DGA C, 85 THR C, 54 ALA C 2.92 167.75 0 -0.58 1.68 104
    149 200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C 2.9 168.76 -0.78 -0.67 13.31 97
    150 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C 2.85 170.84 -0.8 -0.63 17.19 94
    151 200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C 2.99 172.46 -0.7 -0.67 13.74 94
    152 200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A 3.64 172.95 -1.46 -0.62 21.39 91
    153 200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A 3.8 173.41 -2.28 -0.78 26.74 89
    154 200053 GLU B, 53 GLY C, 57 ARG A 3.84 174.33 -2.8 -0.79 35.09 80

    pore with bottle neck

    pore with local minimum

  13. show | | profile | lining residues
    Pore 13 profile

    Unique lining residues set - all

    100031 THR B, 100064 ARG C, 200084 VAL C, 201001 DGA C, 100032 ASP B, 200084 VAL C, 100030 GLY B, 100031 THR B, 100092 ASN B, 200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B, 100028 SER B, 100080 ASP C, 100079 GLY C, 100082 TYR C, 300079 GLY C, 93 ARG B, 200093 ARG B, 300093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 200028 SER B, 300082 TYR C, 300058 GLN C, 300080 ASP C, 28 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 200027 GLN B, 200028 SER B, 27 GLN B, 27 GLN B, 300026 SER B, 69 THR B, 26 SER B, 28 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A, 300169 HIS A, 300167 ASP B, 300166 SER A, 300166 SER A, 300170 ASP B, 300169 LYS B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300207 LYS B, 300115 VAL B, 300136 GLN A, 300140 MET A, 300116 SER B, 300135 ALA A, 300117 ILE B, 300116 SER B, 300117 ILE B, 300132 GLY A, 300208 SER B, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A, 300211 ARG B, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Unique lining residues set - sidechains

    100031 THR B, 100064 ARG C, 201001 DGA C, 100032 ASP B, 200084 VAL C, 100092 ASN B, 200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B, 100082 TYR C, 93 ARG B, 200093 ARG B, 300093 ARG B, 82 TYR C, 200028 SER B, 300082 TYR C, 300058 GLN C, 28 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 200027 GLN B, 27 GLN B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A, 300168 VAL A, 300169 LYS B, 300169 HIS A, 300167 ASP B, 300166 SER A, 300170 ASP B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300207 LYS B, 300116 SER B, 300135 ALA A, 300117 ILE B, 300209 PHE B, 300119 PRO B, 300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 6 (13-7)
    Hydropathy: -1.4
    Hydrophobicity: -0.39
    Polarity: 14.31
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100031 THR B, 100064 ARG C, 200084 VAL C, 201001 DGA C 2.77 0.73 -1.87 -0.66 19.01 95
    2 100031 THR B, 100064 ARG C, 200084 VAL C, 201001 DGA C, 100032 ASP B 2.71 1.45 -2.28 -0.76 26.69 92
    3 100031 THR B, 100064 ARG C, 200084 VAL C, 100032 ASP B 2.66 2.12 -2.28 -0.76 26.69 92
    4 100031 THR B, 100064 ARG C, 100032 ASP B, 200084 VAL C 2.58 4.9 -1.13 -0.28 25.87 93
    5 100064 ARG C, 100032 ASP B, 100030 GLY B, 100031 THR B 2.86 4.98 -2.2 -0.77 27.12 84
    6 100031 THR B, 100064 ARG C, 100030 GLY B 2.96 5.02 -1.87 -0.66 19.01 95
    7 100031 THR B, 100064 ARG C, 200084 VAL C, 100030 GLY B 2.94 5.25 -0.35 -0.22 14.29 96
    8 100064 ARG C, 200084 VAL C, 100030 GLY B 2.95 5.45 -0.23 -0.03 18.5 90
    9 100064 ARG C, 100032 ASP B, 200084 VAL C, 100030 GLY B 2.98 6.5 -1.05 -0.28 26.3 89
    10 100064 ARG C, 100032 ASP B, 200084 VAL C, 100030 GLY B, 100092 ASN B 3.12 7.78 -1.54 -0.38 21.72 92
    11 100064 ARG C, 200084 VAL C, 100030 GLY B, 100092 ASN B, 200082 TYR C 3.26 7.95 -1.1 0.05 12.1 83
    12 200084 VAL C, 100030 GLY B, 100092 ASN B, 200082 TYR C 3.26 8.86 -0.25 0.17 2.13 84
    13 100030 GLY B, 100092 ASN B, 200082 TYR C 3.26 9.28 -1.73 -0.15 2.79 77
    14 100030 GLY B, 100092 ASN B, 200082 TYR C, 100058 GLN C 3.08 11.29 -2.18 -0.39 2.98 79
    15 100030 GLY B, 200082 TYR C, 100058 GLN C, 100028 SER B 3.18 12.49 -1.5 -0.44 2.55 83
    16 200082 TYR C, 100058 GLN C, 100028 SER B 3.41 14.77 -1.87 -0.32 2.27 83
    17 200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B 3.78 14.95 -2.53 -0.35 14.7 83
    18 200082 TYR C, 100028 SER B, 100093 ARG B 3.76 15.04 -2.2 -0.09 18.43 83
    19 200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B 3.68 15.6 -2.53 -0.35 14.7 83
    20 200082 TYR C, 100058 GLN C, 100093 ARG B, 100028 SER B 3.7 15.91 -2.43 -0.3 15.13 72
    21 200082 TYR C, 100058 GLN C, 100093 ARG B 3.76 16.79 -3.1 -0.14 19.05 72
    22 200082 TYR C, 100058 GLN C, 100093 ARG B, 100080 ASP C 3.93 17.01 -2.43 -0.3 15.13 72
    23 200082 TYR C, 100058 GLN C, 100093 ARG B, 100079 GLY C 3.18 18.21 -2.43 -0.3 15.13 72
    24 100058 GLN C, 100093 ARG B, 100080 ASP C, 100079 GLY C 2.98 18.95 -2.2 -0.78 15.57 83
    25 100058 GLN C, 100093 ARG B, 100079 GLY C, 100082 TYR C 3.1 21.86 -2.43 -0.3 15.13 72
    26 100093 ARG B, 100079 GLY C, 100082 TYR C 5.36 22.99 -2.07 -0.04 19 66
    27 200082 TYR C, 100093 ARG B, 100079 GLY C, 100082 TYR C, 300079 GLY C 6.05 24.69 -1.58 0.04 12.4 61
    28 93 ARG B, 200093 ARG B, 300093 ARG B, 79 GLY C, 82 TYR C 7.07 25.09 -3.04 -0.19 32.2 74
    29 93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C 7.3 25.23 -2.22 -0.27 22.47 72
    30 93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200028 SER B 7.34 25.39 -2.3 -0.3 22.13 83
    31 93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C 6.92 26.44 -2.22 -0.27 22.47 72
    32 100093 ARG B, 100079 GLY C, 100082 TYR C, 300079 GLY C, 300093 ARG B 6.49 27.33 -2.22 -0.27 22.47 72
    33 100093 ARG B, 100082 TYR C, 300079 GLY C, 300093 ARG B, 300082 TYR C 5.28 29.39 -2.4 0.12 22.12 66
    34 100082 TYR C, 300079 GLY C, 300093 ARG B, 300082 TYR C, 300058 GLN C 4.59 30.34 -2.2 -0.02 12.43 66
    35 100082 TYR C, 300079 GLY C, 300093 ARG B, 300058 GLN C 3.36 31.68 -2.43 -0.3 15.13 72
    36 300079 GLY C, 300093 ARG B, 300058 GLN C, 300080 ASP C 2.8 32.47 -2.2 -0.78 15.57 83
    37 300079 GLY C, 300093 ARG B, 300058 GLN C 2.93 32.95 -2.8 -0.77 19.64 83
    38 300079 GLY C, 300093 ARG B, 300082 TYR C, 300058 GLN C 3.31 35.72 -2.43 -0.3 15.13 72
    39 300079 GLY C, 300093 ARG B, 300082 TYR C 5.24 36.81 -2.07 -0.04 19 66
    40 100082 TYR C, 300079 GLY C, 300093 ARG B, 79 GLY C, 300082 TYR C 5.88 38.42 -1.58 0.04 12.4 61
    41 200082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C 6.75 38.73 -2.4 0.12 22.12 66
    42 200082 TYR C, 100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C 6.96 38.95 -2.4 0.12 22.12 66
    43 200082 TYR C, 100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C 7.04 39.2 -2.22 -0.27 22.47 72
    44 200082 TYR C, 100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C 6.96 39.53 -1.58 0.04 12.4 61
    45 300079 GLY C, 93 ARG B, 300093 ARG B, 79 GLY C, 300082 TYR C 6.63 40.37 -2.22 -0.27 22.47 72
    46 93 ARG B, 300093 ARG B, 79 GLY C, 300082 TYR C, 28 SER B 6.14 41.37 -2.3 -0.3 22.13 83
    47 93 ARG B, 300093 ARG B, 300082 TYR C, 28 SER B 4.05 43.86 -2.78 -0.18 26.82 83
    48 300093 ARG B, 300082 TYR C, 28 SER B 2.82 46.07 -2.2 -0.09 18.43 83
    49 300093 ARG B, 28 SER B 2.64 46.9 -2.65 -0.7 26.84 100
    50 300093 ARG B, 28 SER B, 300027 GLN B 2.64 51.36 -2.93 -0.83 19.07 94
    51 300093 ARG B, 28 SER B, 300027 GLN B, 300028 SER B 4.49 51.85 -2.3 -0.82 15.15 94
    52 300093 ARG B, 28 SER B, 300027 GLN B, 300028 SER B 4.64 52.07 -2.4 -0.87 14.72 100
    53 300093 ARG B, 300027 GLN B, 300028 SER B 4.71 52.46 -2.93 -0.83 19.07 94
    54 300093 ARG B, 28 SER B, 300027 GLN B, 300028 SER B 4.79 53.3 -2.4 -0.87 14.72 100
    55 28 SER B, 300027 GLN B, 300028 SER B 5.09 56.63 -1.7 -1.01 2.29 106
    56 100028 SER B, 100027 GLN B, 200027 GLN B, 200028 SER B 6.12 57.42 -2.05 -0.99 3.03 95
    57 28 SER B, 300027 GLN B, 300028 SER B, 27 GLN B 5.64 58.75 -2.05 -0.99 3.03 95
    58 28 SER B, 300027 GLN B, 27 GLN B 5.37 59.52 -1.57 -0.96 2.86 100
    59 28 SER B, 300027 GLN B, 300026 SER B 5.12 60.22 -1.57 -0.96 2.86 100
    60 28 SER B, 300027 GLN B, 300026 SER B, 69 THR B 4.49 62.51 -1.35 -0.91 2.56 102
    61 28 SER B, 300027 GLN B, 27 GLN B, 300026 SER B 4.8 62.73 -1.28 -0.92 2.99 100
    62 27 GLN B, 300026 SER B, 69 THR B, 26 SER B, 28 SER B 4.91 66.1 -0.46 -0.79 3.04 107
    63 300026 SER B, 69 THR B, 26 SER B 5 68.77 -0.5 -0.79 2.81 107
    64 300026 SER B, 69 THR B, 26 SER B, 24 ARG B 4.65 69.55 -1.5 -0.7 15.11 95
    65 300026 SER B, 69 THR B, 24 ARG B 4.3 71.45 -1.87 -0.66 19.01 95
    66 300026 SER B, 69 THR B, 24 ARG B, 70 ASP B 3.93 72.79 -2.28 -0.76 26.69 92
    67 300026 SER B, 24 ARG B, 70 ASP B 3.7 73.45 -2.8 -0.75 35.03 84
    68 24 ARG B, 70 ASP B, 300026 SER B 3.3 75.49 -2.93 -0.81 34.46 95
    69 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B 2.49 77.56 -1.25 -0.32 25.88 85
    70 70 ASP B, 300026 SER B, 300003 LEU B 2.08 80.41 -0.17 -0.29 17.17 85
    71 70 ASP B, 300003 LEU B 2.18 82.74 0.15 0.05 24.92 70
    72 70 ASP B, 300003 LEU B, 300001 ASP B 3 84.74 -0.03 -0.23 17.74 70
    73 70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B 3.83 84.89 -0.2 -0.37 13.72 82
    74 70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B 3.91 85.93 -0.98 -0.43 25.3 83
    75 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A 3.76 87.27 -1.08 -0.27 25.25 79
    76 300003 LEU B, 300001 ASP B, 300063 LYS A 3.54 89.3 -1.2 -0.1 33.11 70
    77 300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B 3.55 90.84 -1.08 -0.27 25.25 79
    78 300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A 3.84 91.3 -1.08 -0.2 13.67 84
    79 300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B 3.97 92.17 -0.94 -0.32 11.61 84
    80 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.25 92.35 -2.4 -0.78 21.56 90
    81 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.28 92.7 -2.03 -0.87 14.58 96
    82 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.29 93.48 -2.4 -0.78 21.56 90
    83 300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.29 94.65 -1.5 -0.4 21.26 76
    84 300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A 4.3 98.45 0.23 0.35 24.92 76
    85 300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B 4.42 98.96 -1.1 -0.35 25.3 80
    86 300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B 4.42 99.78 -0.93 -0.18 25.3 92
    87 300063 LYS A, 300046 GLU A, 300064 ILE A 3.85 104.3 -0.97 0.09 33.18 84
    88 300046 GLU A, 300064 ILE A, 300063 LYS A 3.74 105.19 0.2 -0.04 17.8 90
    89 300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B 3.59 107.98 -0.98 -0.14 26.35 87
    90 300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A 3.61 111.37 -2 -0.04 38.51 86
    91 300046 GLU A, 18 ARG B, 300040 ARG A 3.97 113.97 -4.17 -0.66 51.3 81
    92 300046 GLU A, 300064 ILE A, 300040 ARG A 4.03 114.67 -1.17 0.08 34.01 87
    93 300046 GLU A, 300040 ARG A 3 117.42 -4 -0.78 50.95 80
    94 300040 ARG A 1.06 124.22 -4.5 -0.42 52 83
    95 300040 ARG A, 300088 SER A 1 124.93 -2.45 -0.61 27.69 83
    96 300040 ARG A, 300088 SER A, 300091 SER A 1.15 125.27 -1.77 -0.67 19.59 83
    97 300040 ARG A, 300088 SER A, 300041 PRO A, 300091 SER A 1.47 125.54 -1.83 -0.57 14.66 86
    98 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A 1.9 126.37 -1.73 -0.53 15.09 70
    99 300040 ARG A, 300088 SER A, 300041 PRO A 2.95 129.18 -2.17 -0.44 18.99 70
    100 300040 ARG A, 300041 PRO A, 300088 SER A 4.78 131.14 -2.3 -0.49 18.42 86
    101 300041 PRO A, 300088 SER A 4.89 132.22 -1.2 -0.53 1.63 87
    102 300041 PRO A, 300091 SER A, 300088 SER A 4.7 132.76 -1.07 -0.68 1.64 97
    103 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A 4.53 133.22 0.15 -0.22 1.26 86
    104 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.31 133.82 0.02 0.3 1.25 69
    105 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.26 134.01 0.23 0.08 1.27 84
    106 300091 SER A, 300088 SER A, 300180 TYR A 4.24 134.12 -0.97 -0.28 1.65 94
    107 300091 SER A, 300088 SER A 4.24 134.27 -0.8 -0.97 1.67 117
    108 300091 SER A, 300088 SER A, 300180 TYR A 4.26 134.71 -0.97 -0.28 1.65 94
    109 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.29 135.51 0.02 0.3 1.25 69
    110 300041 PRO A, 300091 SER A, 300175 LEU A, 300180 TYR A 4.33 136.55 0.02 0.3 1.25 69
    111 300041 PRO A, 300175 LEU A, 300180 TYR A 4.37 140.14 0.3 0.72 1.11 54
    112 300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A 4.41 140.34 0.13 0.34 1.68 54
    113 300041 PRO A, 300175 LEU A, 300180 TYR A 4.36 141.04 0.3 0.72 1.11 54
    114 300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A 4.23 141.85 0.13 0.34 1.68 54
    115 300041 PRO A, 300180 TYR A, 300173 ALA A 3.62 143.78 -1.1 0.07 2.19 54
    116 300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A 3.28 145.86 -1.7 -0.23 14.12 61
    117 300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A 3.3 147.92 -1.78 -0.53 14.11 64
    118 300041 PRO A, 300153 GLU A, 300172 PRO A 3.48 148.27 -2.23 -0.44 17.69 64
    119 300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B 3.44 148.89 -2.55 -0.52 14.11 74
    120 300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B 3.37 149.24 -2.55 -0.52 14.11 74
    121 300153 GLU A, 300172 PRO A, 300041 ASN B 3.14 150.18 -2.87 -0.67 18.29 79
    122 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B 2.52 152.87 -2.25 -0.7 14.56 79
    123 300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A 2.38 153.99 -1.95 -0.88 15.01 90
    124 300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A 2.39 154.3 -0.8 -0.47 12.03 78
    125 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A 2.44 154.5 -0.8 -0.47 12.03 78
    126 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A 2.59 155.24 -0.13 -0.31 2.57 79
    127 300041 ASN B, 300182 LEU A, 300171 PHE A 2.73 155.66 -0.03 -0.14 2.3 79
    128 300041 ASN B, 300182 LEU A, 300170 THR A 2.71 155.82 -0.13 -0.13 1.72 88
    129 300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A 2.59 157.11 -0.2 -0.3 2.14 88
    130 300041 ASN B, 300170 THR A, 300155 VAL A 2.59 161.07 -1.53 -0.78 2.81 105
    131 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 2.9 161.25 -1.33 -0.78 2.52 106
    132 300041 ASN B, 300156 THR A, 300157 VAL A 3.01 161.44 -1.53 -0.78 2.81 105
    133 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 3.21 161.62 -1.33 -0.78 2.52 106
    134 300041 ASN B, 300170 THR A, 300157 VAL A 3.28 161.75 -1.53 -0.78 2.81 105
    135 300041 ASN B, 300170 THR A, 300155 VAL A 3.3 161.93 -1.53 -0.78 2.81 105
    136 300041 ASN B, 300170 THR A, 300157 VAL A 3.26 162.15 -1.53 -0.78 2.81 105
    137 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 3.21 162.53 -1.33 -0.78 2.52 106
    138 300041 ASN B, 300170 THR A, 300157 VAL A 3.2 165.63 -1.53 -0.78 2.81 105
    139 300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B 4.1 166.49 -1.25 -0.79 2.95 105
    140 300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A 4.44 166.64 -1.08 -0.79 3.04 105
    141 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A 4.52 166.79 0.68 -0.31 2.14 102
    142 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B 4.51 166.93 -1.16 -0.72 12.26 89
    143 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B 4.51 166.98 -0.13 -0.22 14.1 85
    144 300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B 4.49 167.74 -0.2 -0.21 13.67 92
    145 300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A 4.26 168.12 -0.13 -0.22 14.1 85
    146 300168 VAL A, 300169 LYS B, 300165 SER A 1.99 173.04 -0.03 -0.03 17.67 85
    147 300168 VAL A, 300169 LYS B, 300165 SER A 1.27 174.45 -1.57 -0.67 18.75 72
    148 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A 1.34 175.57 -1.28 -0.7 14.91 72
    149 300168 VAL A, 300169 LYS B, 300167 GLY A 1.79 176.51 -1.57 -0.67 18.75 72
    150 300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A 1.9 176.81 -1.98 -0.44 26.97 81
    151 300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A 1.89 177.09 -1.98 -0.44 26.97 81
    152 300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A 1.85 177.12 -1.98 -0.44 26.97 81
    153 300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A 1.74 177.56 -1.98 -0.44 26.97 81
    154 300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B 1.72 178.09 -2.75 -0.5 38.55 83
    155 300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B 1.73 178.68 -2.75 -0.5 38.55 83
    156 300169 LYS B, 300167 GLY A, 300167 ASP B 1.75 179.41 -2.6 -0.75 34.19 79
    157 300169 LYS B, 300167 GLY A 1.78 180.19 -2.15 -0.61 26.44 72
    158 300169 LYS B, 300167 GLY A, 300166 SER A 1.81 181.75 -1.57 -0.67 18.75 72
    159 300169 LYS B, 300167 GLY A, 300166 SER A 1.86 181.92 -1.7 -0.73 18.18 94
    160 300169 LYS B, 300166 SER A 1.91 182.13 -2.35 -0.69 25.59 94
    161 300169 LYS B, 300167 GLY A, 300166 SER A 1.98 185.52 -1.7 -0.73 18.18 94
    162 300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B 3.28 186.43 -2.15 -0.81 26.06 91
    163 300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B 4.47 187.38 -1.28 -0.9 14.53 101
    164 300167 GLY A, 300166 SER A, 300170 ASP B 4.68 188.2 -1.57 -0.94 18.25 101
    165 300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A 4.89 189.22 -0.7 -0.45 14.05 98
    166 300167 GLY A, 300170 ASP B, 300140 MET A 4.32 190.58 -0.67 -0.28 18.17 89
    167 300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B 4.08 191.89 -1.38 -0.4 14.47 94
    168 300170 ASP B, 300140 MET A, 300138 ASN B 3.9 193.58 -1.7 -0.27 18.17 94
    169 300140 MET A, 300138 ASN B, 300187 THR A 3.62 195.37 -0.77 -0.18 2.16 101
    170 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B 3.07 196.92 -0.75 -0.33 2.03 102
    171 300140 MET A, 300187 THR A, 300114 THR B 2.7 198.68 0.17 -0.18 1.58 102
    172 300140 MET A, 300114 THR B 2.53 200.2 0.6 0.12 1.55 100
    173 300140 MET A, 300114 THR B, 300138 ASN A 2.48 200.67 -0.77 -0.18 2.16 101
    174 300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A 2.48 201.65 -0.78 -0.38 2.04 105
    175 300140 MET A, 300114 THR B, 300138 ASN A 2.73 204.39 -0.77 -0.18 2.16 101
    176 300114 THR B, 300138 ASN A 3.5 207.84 -2.1 -0.77 2.52 105
    177 300114 THR B, 300138 ASN A, 300207 LYS B 3.41 210.06 -2.7 -0.65 18.18 94
    178 300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B 3.24 211.15 -2.13 -0.69 14.48 94
    179 300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A 3.07 212.12 -2.13 -0.69 14.48 94
    180 300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A 2.68 213.33 -1.78 -0.71 12.26 94
    181 300114 THR B, 300207 LYS B, 300115 VAL B, 300136 GLN A 2.65 213.75 -1.35 -0.7 14.48 89
    182 300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A 2.63 214.39 -1.78 -0.71 12.26 94
    183 300114 THR B, 300115 VAL B, 300136 GLN A, 300140 MET A, 300116 SER B 2.57 215.86 -0.54 -0.83 2.69 112
    184 300114 THR B, 300115 VAL B, 300136 GLN A, 300116 SER B 2.54 216.53 -0.58 -0.84 2.52 112
    185 300207 LYS B, 300115 VAL B, 300136 GLN A, 300116 SER B 2.51 217.2 -1.38 -0.75 14.48 94
    186 300115 VAL B, 300136 GLN A, 300116 SER B 2.47 217.78 -0.53 -0.86 2.81 117
    187 300115 VAL B, 300136 GLN A, 300116 SER B, 300135 ALA A 2.37 218.59 0.05 -0.64 2.11 108
    188 300115 VAL B, 300116 SER B, 300135 ALA A 2.28 219.75 0.2 -0.58 1.68 108
    189 300116 SER B, 300135 ALA A, 300117 ILE B 1.96 222.07 0.2 -0.58 1.68 108
    190 300135 ALA A, 300117 ILE B, 300116 SER B 1.91 222.57 0.33 -0.53 2.25 100
    191 300135 ALA A, 300116 SER B, 300117 ILE B 1.81 223.56 1.97 0.34 1.17 101
    192 300135 ALA A, 300117 ILE B 1.68 225.27 3.15 0.92 0.07 101
    193 300135 ALA A, 300117 ILE B, 300132 GLY A, 300208 SER B 1.66 226.21 1.38 0.06 1.72 101
    194 300135 ALA A, 300117 ILE B, 300132 GLY A 1.67 226.72 1.97 0.34 1.17 101
    195 300117 ILE B, 300132 GLY A, 300209 PHE B 1.71 228.04 2.3 0.79 1.29 77
    196 300117 ILE B, 300132 GLY A, 300209 PHE B, 300119 PRO B 1.72 228.52 0.1 -0.09 2.17 54
    197 300117 ILE B, 300132 GLY A, 300119 PRO B 1.63 228.67 -0.8 -0.56 2.78 58
    198 300117 ILE B, 300132 GLY A, 300119 PRO B 1.38 228.88 0.83 0.31 1.7 80
    199 300117 ILE B, 300132 GLY A, 300119 PRO B 1.25 229.3 -0.8 -0.56 2.78 58
    200 300132 GLY A, 300209 PHE B, 300119 PRO B 1.1 233.53 0.27 0.15 1.77 54
    201 300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B 1.58 233.94 0.1 -0.09 2.17 54
    202 300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A 1.81 234.43 0 -0.23 2.41 54
    203 300132 GLY A, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A 2.32 235.42 -1.46 -0.58 12.74 70
    204 300119 PRO B, 300210 ASN B, 300218 ARG A 2.09 237 -2.17 -0.44 18.99 70
    205 300209 PHE B, 300119 PRO B, 300210 ASN B, 300218 ARG A 2.05 237.5 -0.93 0.01 14.33 64
    206 300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B 1.95 238.12 -1.73 -0.53 15.09 70
    207 300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B, 300186 TYR B 1.95 238.48 -1.64 -0.2 12.39 63
    208 300119 PRO B, 300218 ARG A, 300211 ARG B, 300186 TYR B 2.02 240.18 -1.95 -0.05 14.64 63
    209 300218 ARG A, 300186 TYR B, 300211 ARG B 2.23 241.77 -3.43 0.09 35.2 72
    210 300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B 2.41 241.77 -1.63 0.35 26.44 67

    pore with bottle neck

    pore with local minimum

  14. show | | profile | lining residues
    Pore 14 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 100027 GLN B, 200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200002 ILE B, 200098 PHE B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200042 GLY A, 200165 ASP B, 200040 THR B, 200085 ASN B, 200103 LYS B, 200010 ILE B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200165 ASP B, 200040 THR B, 200085 ASN B, 200103 LYS B, 200010 ILE B

    Physicochemical properties of lining side-chains

    Charge: 4 (13-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 15.06
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.26 0.26 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.45 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.2 0.61 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.22 0.74 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 1.03 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3 1.51 -1.53 -0.78 2.81 105
    7 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A 2.89 2.08 -1.25 -0.79 2.95 105
    8 100170 THR A, 100041 ASN B, 100155 VAL A 2.51 5.72 -1.53 -0.78 2.81 105
    9 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.52 6.66 -0.2 -0.3 2.14 88
    10 100170 THR A, 100041 ASN B, 100182 LEU A 2.78 7.02 -0.13 -0.13 1.72 88
    11 100041 ASN B, 100182 LEU A, 100171 PHE A 2.76 7.2 -0.03 -0.14 2.3 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.57 7.93 -0.13 -0.31 2.57 79
    13 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.41 8.34 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.34 8.75 -0.8 -0.47 12.03 78
    15 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.31 9.88 -1.95 -0.88 15.01 90
    16 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.37 12.65 -2.25 -0.7 14.56 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A 3.11 13.36 -2.87 -0.67 18.29 79
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.36 13.89 -2.55 -0.52 14.11 74
    19 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.47 14.5 -2.55 -0.52 14.11 74
    20 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.31 16.7 -1.78 -0.53 14.11 64
    21 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.3 19.09 -1.7 -0.23 14.12 61
    22 100173 ALA A, 100041 PRO A, 100180 TYR A 3.75 21.04 -1.1 0.07 2.19 54
    23 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.42 21.41 0.13 0.34 1.68 54
    24 100041 PRO A, 100180 TYR A, 100175 LEU A 4.37 22.12 0.3 0.72 1.11 54
    25 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.46 22.49 0.13 0.34 1.68 54
    26 100041 PRO A, 100180 TYR A, 100175 LEU A 4.21 27.28 0.3 0.72 1.11 54
    27 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.2 27.85 -0.06 0.08 1.67 69
    28 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.2 28.15 0.23 0.08 1.27 84
    29 100180 TYR A, 100091 SER A, 100088 SER A 4.23 28.26 -0.97 -0.28 1.65 94
    30 100091 SER A, 100088 SER A 4.27 28.35 -0.8 -0.97 1.67 117
    31 100180 TYR A, 100091 SER A, 100088 SER A 4.33 28.52 -0.97 -0.28 1.65 94
    32 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.41 29 0.23 0.08 1.27 84
    33 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.6 29.36 0.02 0.3 1.25 69
    34 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.71 29.8 0.15 -0.22 1.26 86
    35 100041 PRO A, 100091 SER A, 100088 SER A 4.82 30.76 -1.07 -0.68 1.64 97
    36 100041 PRO A, 100088 SER A 5 31.9 -1.2 -0.53 1.63 87
    37 100041 PRO A, 100088 SER A, 100040 ARG A 4.55 33.89 -2.3 -0.49 18.42 86
    38 100041 PRO A, 100088 SER A, 100040 ARG A 3.28 36.63 -2.17 -0.44 18.99 70
    39 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.9 36.96 -1.73 -0.53 15.09 70
    40 100088 SER A, 100040 ARG A, 100091 SER A 1.5 38 -1.77 -0.67 19.59 83
    41 100088 SER A, 100040 ARG A 0.61 40.1 -2.45 -0.61 27.69 83
    42 100040 ARG A 0.21 45.88 -4.5 -0.42 52 83
    43 100040 ARG A, 100043 HIS A 1.27 46.91 -3.85 -0.08 51.8 87
    44 100040 ARG A, 100046 GLU A 1.98 50.22 -4 -0.78 50.95 80
    45 100040 ARG A, 100046 GLU A, 300018 ARG B 4.43 52.92 -4.17 -0.66 51.3 81
    46 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.53 56.18 -2 -0.04 38.51 86
    47 100046 GLU A, 300018 ARG B, 100064 ILE A 3.51 56.77 -1.17 0.08 34.01 87
    48 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.15 59.42 -0.98 -0.14 26.35 87
    49 100046 GLU A, 100064 ILE A, 100063 LYS A 3.18 60.22 0.2 -0.04 17.8 90
    50 100046 GLU A, 100064 ILE A, 100063 LYS A 3.32 64.79 -0.97 0.09 33.18 84
    51 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 4.97 65.29 -0.93 -0.18 25.3 92
    52 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 4.84 66.16 -1.1 -0.35 25.3 80
    53 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 4.35 69.35 0.23 0.35 24.92 76
    54 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.23 70.36 -1 -0.3 25.73 67
    55 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.16 71.06 -1.5 -0.4 21.26 76
    56 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.14 71.41 -2.4 -0.78 21.56 90
    57 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.15 71.78 -2.03 -0.87 14.58 96
    58 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.2 72 -2.4 -0.78 21.56 90
    59 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 4 72.97 -0.94 -0.32 11.61 84
    60 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.88 73.4 -1.08 -0.2 13.67 84
    61 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.56 75.37 -1.08 -0.27 25.25 79
    62 100063 LYS A, 100003 LEU B, 100001 ASP B 3.58 77.13 -1.2 -0.1 33.11 70
    63 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 3.83 78.06 -1.08 -0.27 25.25 79
    64 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.1 78.27 -1.56 -0.42 30.14 81
    65 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.84 79.15 -0.98 -0.43 25.3 83
    66 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.8 79.32 -0.2 -0.37 13.72 82
    67 100003 LEU B, 300070 ASP B, 100001 ASP B 3.09 81.29 -0.03 -0.23 17.74 70
    68 100003 LEU B, 300070 ASP B 2.21 84.4 0.15 0.05 24.92 70
    69 100003 LEU B, 300070 ASP B, 100026 SER B 2.09 86.85 -0.17 -0.29 17.17 85
    70 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.4 89.03 -1.25 -0.32 25.88 85
    71 300070 ASP B, 100026 SER B, 300024 ARG B 3.34 90.45 -2.93 -0.81 34.46 95
    72 300070 ASP B, 300024 ARG B, 100026 SER B 3.57 91.62 -2.8 -0.75 35.03 84
    73 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.84 93.2 -2.28 -0.76 26.69 92
    74 300024 ARG B, 100026 SER B, 300069 THR B 4.57 94.65 -1.87 -0.66 19.01 95
    75 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.67 95.48 -1.5 -0.7 15.11 95
    76 100026 SER B, 300069 THR B, 300026 SER B 4.48 98.47 -0.5 -0.79 2.81 107
    77 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.7 99.4 -0.48 -0.79 2.95 107
    78 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.86 101.19 -0.46 -0.79 3.04 107
    79 100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B 5.16 101.38 -0.58 -0.84 2.52 112
    80 100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B 5.12 101.52 -1.28 -0.92 2.99 100
    81 100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B 4.23 104.74 -1.35 -0.91 2.56 102
    82 100026 SER B, 300028 SER B, 100027 GLN B 5.43 105.41 -1.57 -0.96 2.86 100
    83 300028 SER B, 100027 GLN B, 300027 GLN B 5.72 106.03 -2.6 -1.06 2.91 95
    84 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B 5.98 106.52 -2.05 -0.99 3.03 95
    85 300028 SER B, 100027 GLN B, 100028 SER B 6.21 106.84 -1.7 -1.01 2.29 106
    86 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.39 107.84 -2.05 -0.99 3.03 95
    87 300028 SER B, 100027 GLN B, 100028 SER B 4.99 111.36 -1.7 -1.01 2.29 106
    88 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.79 111.63 -2.4 -0.87 14.72 100
    89 100027 GLN B, 100028 SER B, 100093 ARG B 4.76 112.05 -2.93 -0.83 19.07 94
    90 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.57 113.05 -2.4 -0.87 14.72 100
    91 300028 SER B, 100027 GLN B, 100093 ARG B 2.5 118.44 -2.93 -0.83 19.07 94
    92 300028 SER B, 100093 ARG B 2.73 119.14 -2.65 -0.7 26.84 100
    93 300028 SER B, 100093 ARG B, 100082 TYR C 3.04 120.22 -2.2 -0.09 18.43 83
    94 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 3.85 123.27 -2.78 -0.18 26.82 83
    95 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.1 124.07 -2.3 -0.3 22.13 83
    96 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.53 124.71 -2.22 -0.27 22.47 72
    97 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C 6.94 124.95 -1.58 0.04 12.4 61
    98 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B 7.09 125.33 -2.4 0.12 22.12 66
    99 300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C 6.97 125.73 -2.4 0.12 22.12 66
    100 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.66 126.41 -2.22 -0.27 22.47 72
    101 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.63 128.3 -1.58 0.04 12.4 61
    102 100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C 5.02 129.27 -1.88 0.25 14.65 61
    103 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 3.12 131.63 -2.43 -0.3 15.13 72
    104 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 3.16 132.35 -2.2 -0.78 15.57 83
    105 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.47 133.45 -2.43 -0.3 15.13 72
    106 100093 ARG B, 200082 TYR C, 100058 GLN C 3.65 134.43 -3.1 -0.14 19.05 72
    107 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.57 134.68 -2.43 -0.3 15.13 72
    108 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.47 135.14 -2.53 -0.35 14.7 83
    109 100028 SER B, 100093 ARG B, 100058 GLN C 3.48 135.45 -2.93 -0.83 19.07 94
    110 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.83 136.7 -2.53 -0.35 14.7 83
    111 100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C 3.98 137.11 -2.78 -0.18 26.82 83
    112 100028 SER B, 200093 ARG B, 200082 TYR C 3.3 139.03 -2.2 -0.09 18.43 83
    113 100028 SER B, 200027 GLN B, 200093 ARG B 2.48 144.2 -2.93 -0.83 19.07 94
    114 100028 SER B, 200027 GLN B, 200093 ARG B, 200028 SER B 4.08 144.73 -2.3 -0.82 15.15 94
    115 100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B 4.49 145.04 -2.4 -0.87 14.72 100
    116 200027 GLN B, 200028 SER B, 200093 ARG B 4.83 145.53 -2.93 -0.83 19.07 94
    117 100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B 5.08 146.2 -2.4 -0.87 14.72 100
    118 100028 SER B, 200027 GLN B, 200028 SER B 5.07 149.7 -1.7 -1.01 2.29 106
    119 300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B 5.99 150.68 -2.05 -0.99 3.03 95
    120 100027 GLN B, 100028 SER B, 200027 GLN B, 200028 SER B 5.49 151.9 -2.05 -0.99 3.03 95
    121 100028 SER B, 200027 GLN B, 100027 GLN B 5.22 152.57 -1.57 -0.96 2.86 100
    122 100028 SER B, 200027 GLN B, 200026 SER B 4.97 153.19 -1.57 -0.96 2.86 100
    123 100028 SER B, 200027 GLN B, 200026 SER B, 100069 THR B 4.51 155.54 -1.35 -0.91 2.56 102
    124 100028 SER B, 200027 GLN B, 100027 GLN B, 200026 SER B 4.82 155.94 -1.28 -0.92 2.99 100
    125 100026 SER B, 100028 SER B, 100027 GLN B, 200026 SER B, 100069 THR B 4.92 158.97 -0.46 -0.79 3.04 107
    126 100026 SER B, 100027 GLN B, 200026 SER B, 100069 THR B 5.01 159.9 -0.48 -0.79 2.95 107
    127 100026 SER B, 200026 SER B, 100069 THR B 4.97 161.67 -0.5 -0.79 2.81 107
    128 100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B 4.68 162.93 -1.5 -0.7 15.11 95
    129 200026 SER B, 100069 THR B, 100024 ARG B 4.34 164.65 -1.87 -0.66 19.01 95
    130 200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B 3.91 165.83 -2.28 -0.76 26.69 92
    131 200026 SER B, 100024 ARG B, 100070 ASP B 3.63 166.55 -2.8 -0.75 35.03 84
    132 100024 ARG B, 100070 ASP B, 200026 SER B 3.45 168.59 -2.93 -0.81 34.46 95
    133 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B 2.76 170.37 -1.25 -0.32 25.88 85
    134 100070 ASP B, 200026 SER B, 200003 LEU B 2.09 173.36 -0.17 -0.29 17.17 85
    135 100070 ASP B, 200003 LEU B 2.18 175.9 0.15 0.05 24.92 70
    136 100070 ASP B, 200003 LEU B, 200001 ASP B 2.96 177.9 -0.03 -0.23 17.74 70
    137 100070 ASP B, 200003 LEU B, 200001 ASP B, 100072 THR B 3.93 178.02 -0.2 -0.37 13.72 82
    138 100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B 3.95 179.03 -0.98 -0.43 25.3 83
    139 100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A 4.09 179.27 -1.56 -0.42 30.14 81
    140 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A 4.04 180.1 -1.08 -0.27 25.25 79
    141 200003 LEU B, 200001 ASP B, 200063 LYS A 3.72 182.44 -1.2 -0.1 33.11 70
    142 200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B 3.51 183.8 -1.08 -0.27 25.25 79
    143 200003 LEU B, 200063 LYS A, 200097 THR B, 200002 ILE B 3.49 184.21 -0.3 -0.21 13.67 77
    144 200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B 3.49 184.58 -0.3 -0.21 13.67 77
    145 200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A 3.53 185.3 -0.94 -0.32 11.61 84
    146 200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A 3.83 185.46 -2.4 -0.78 21.56 90
    147 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A 4.01 185.69 -2.03 -0.87 14.58 96
    148 200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A 4.44 186.2 -2.4 -0.78 21.56 90
    149 200003 LEU B, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200046 GLU A 4.66 187.06 -1.5 -0.4 21.26 76
    150 200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A 4.84 188.16 -1 -0.3 25.73 67
    151 200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A 4.83 191.54 0.23 0.35 24.92 76
    152 200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B 4.61 191.89 -1.1 -0.35 25.3 80
    153 200063 LYS A, 200046 GLU A, 200064 ILE A, 100020 SER B 4.36 192.52 -0.93 -0.18 25.3 92
    154 200063 LYS A, 200046 GLU A, 200064 ILE A 3.54 197.14 -0.97 0.09 33.18 84
    155 200046 GLU A, 200064 ILE A, 200063 LYS A 3.75 197.93 0.2 -0.04 17.8 90
    156 200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B 3.85 201.07 -0.98 -0.14 26.35 87
    157 200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A 3.53 204.28 -2 -0.04 38.51 86
    158 200046 GLU A, 100018 ARG B, 200040 ARG A 3.93 207 -4.17 -0.66 51.3 81
    159 200046 GLU A, 200064 ILE A, 200040 ARG A 4.08 207.52 -1.17 0.08 34.01 87
    160 200046 GLU A, 200040 ARG A 1.96 211 -4 -0.78 50.95 80
    161 200040 ARG A -0.05 217.1 -4.5 -0.42 52 83
    162 200040 ARG A, 200088 SER A 0.06 217.87 -2.45 -0.61 27.69 83
    163 200040 ARG A, 200088 SER A, 200091 SER A 0.38 218.29 -1.77 -0.67 19.59 83
    164 200040 ARG A, 200088 SER A, 200091 SER A 0.88 218.52 -1.9 -0.73 19.02 100
    165 200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A 1.48 218.78 -1.83 -0.57 14.66 86
    166 200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A 2.13 219.52 -1.73 -0.53 15.09 70
    167 200040 ARG A, 200088 SER A, 200041 PRO A 3.36 221.99 -2.17 -0.44 18.99 70
    168 200040 ARG A, 200041 PRO A, 200088 SER A 4.91 224.13 -2.3 -0.49 18.42 86
    169 200041 PRO A, 200088 SER A 4.72 225.5 -1.2 -0.53 1.63 87
    170 200091 SER A, 200041 PRO A, 200088 SER A 4.6 225.97 -1.07 -0.68 1.64 97
    171 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A 4.4 226.68 0.15 -0.22 1.26 86
    172 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A 4.31 226.92 0.02 0.3 1.25 69
    173 200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A 4.24 227.11 0.23 0.08 1.27 84
    174 200091 SER A, 200088 SER A, 200180 TYR A 4.12 227.32 -0.97 -0.28 1.65 94
    175 200091 SER A, 200088 SER A 4.08 227.5 -0.8 -0.97 1.67 117
    176 200091 SER A, 200088 SER A, 200180 TYR A 4.04 227.93 -0.97 -0.28 1.65 94
    177 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A 4.03 228.62 0.02 0.3 1.25 69
    178 200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A 4.02 229.51 -0.06 0.08 1.67 69
    179 200041 PRO A, 200175 LEU A, 200180 TYR A 4.03 233.18 0.3 0.72 1.11 54
    180 200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A 4.28 233.62 0.13 0.34 1.68 54
    181 200041 PRO A, 200175 LEU A, 200180 TYR A 4.44 234.19 0.3 0.72 1.11 54
    182 200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A 4.29 235.04 0.13 0.34 1.68 54
    183 200041 PRO A, 200180 TYR A, 200173 ALA A 3.79 237.29 -1.1 0.07 2.19 54
    184 200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A 3.31 239.06 -1.7 -0.23 14.12 61
    185 200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A 3.24 241.46 -1.78 -0.53 14.11 64
    186 200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B 3.43 241.98 -2.55 -0.52 14.11 74
    187 200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B 3.49 242.64 -2.55 -0.52 14.11 74
    188 200041 PRO A, 200172 PRO A, 200041 ASN B, 200042 GLY A 3.55 243.64 -1.78 -0.44 2.48 73
    189 200041 PRO A, 200172 PRO A, 200041 ASN B, 200042 GLY A 3.65 243.85 -1.78 -0.44 2.48 73
    190 200041 PRO A, 200172 PRO A, 200041 ASN B, 200042 GLY A 3.68 244.11 -1.78 -0.44 2.48 73
    191 200172 PRO A, 200041 ASN B, 200042 GLY A, 200165 ASP B 3.61 244.86 -2.25 -0.68 14.51 82
    192 200172 PRO A, 200041 ASN B, 200042 GLY A, 200165 ASP B, 200040 THR B 3.54 245.14 -1.94 -0.69 11.94 88
    193 200041 ASN B, 200042 GLY A, 200165 ASP B, 200040 THR B 3.22 247.53 -2.03 -0.85 14.53 99
    194 200042 GLY A, 200165 ASP B, 200040 THR B 3.21 248.74 -1.53 -0.87 18.25 96
    195 200042 GLY A, 200165 ASP B, 200085 ASN B 3.27 248.81 -2.47 -0.87 18.82 95
    196 200042 GLY A, 200165 ASP B, 200040 THR B, 200085 ASN B 3.23 249.13 -2.03 -0.85 14.53 99
    197 200165 ASP B, 200040 THR B, 200085 ASN B 2.89 249.65 -2.57 -0.86 18.25 99
    198 200042 GLY A, 200165 ASP B, 200085 ASN B 2.67 254.9 -2.47 -0.87 18.82 95
    199 200042 GLY A, 200165 ASP B, 200085 ASN B, 200103 LYS B 3.54 255.95 -2.83 -0.76 26.49 87
    200 200042 GLY A, 200165 ASP B, 200103 LYS B, 200010 ILE B 3.93 256.16 -0.83 -0.11 25.68 87

    pore with bottle neck

    pore with local minimum

  15. show | | profile | lining residues
    Pore 15 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 200026 SER B, 100069 THR B, 100027 GLN B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A, 200170 THR A, 200155 VAL A, 200156 THR A, 200157 VAL A, 200040 THR B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 4 (12-8)
    Hydropathy: -1.5
    Hydrophobicity: -0.44
    Polarity: 14.39
    Mutability: 86

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.26 0.27 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.45 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.19 0.62 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.77 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.19 1.05 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3.04 1.59 -1.53 -0.78 2.81 105
    7 100170 THR A, 100041 ASN B, 100155 VAL A 2.62 5.8 -1.53 -0.78 2.81 105
    8 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.61 6.54 -0.2 -0.3 2.14 88
    9 100170 THR A, 100041 ASN B, 100182 LEU A 2.8 6.87 -0.13 -0.13 1.72 88
    10 100041 ASN B, 100182 LEU A, 100171 PHE A 2.76 7.23 -0.03 -0.14 2.3 79
    11 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.57 7.96 -0.13 -0.31 2.57 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.4 8.49 -0.8 -0.47 12.03 78
    13 100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.32 8.97 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.26 9.54 -1.95 -0.88 15.01 90
    15 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.24 12.84 -2.25 -0.7 14.56 79
    16 100041 ASN B, 100153 GLU A, 100172 PRO A 3.13 13.2 -2.87 -0.67 18.29 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.33 13.76 -2.55 -0.52 14.11 74
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.6 14.67 -2.55 -0.52 14.11 74
    19 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.4 16.96 -1.78 -0.53 14.11 64
    20 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.35 18.88 -1.7 -0.23 14.12 61
    21 100173 ALA A, 100041 PRO A, 100180 TYR A 3.49 20.95 -1.1 0.07 2.19 54
    22 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.09 21.36 0.13 0.34 1.68 54
    23 100041 PRO A, 100180 TYR A, 100175 LEU A 4.38 22.07 0.3 0.72 1.11 54
    24 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.4 22.43 0.13 0.34 1.68 54
    25 100041 PRO A, 100180 TYR A, 100175 LEU A 4.3 27.21 0.3 0.72 1.11 54
    26 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.26 27.8 -0.06 0.08 1.67 69
    27 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.22 28.12 0.23 0.08 1.27 84
    28 100180 TYR A, 100091 SER A, 100088 SER A 4.18 28.23 -0.97 -0.28 1.65 94
    29 100091 SER A, 100088 SER A 4.17 28.32 -0.8 -0.97 1.67 117
    30 100180 TYR A, 100091 SER A, 100088 SER A 4.17 28.49 -0.97 -0.28 1.65 94
    31 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.2 28.97 0.23 0.08 1.27 84
    32 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.32 29.34 0.02 0.3 1.25 69
    33 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.44 29.78 0.15 -0.22 1.26 86
    34 100041 PRO A, 100091 SER A, 100088 SER A 4.58 30.75 -1.07 -0.68 1.64 97
    35 100041 PRO A, 100088 SER A 4.94 31.89 -1.2 -0.53 1.63 87
    36 100041 PRO A, 100088 SER A, 100040 ARG A 4.51 33.93 -2.3 -0.49 18.42 86
    37 100041 PRO A, 100088 SER A, 100040 ARG A 3 36.29 -2.17 -0.44 18.99 70
    38 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.38 36.98 -1.73 -0.53 15.09 70
    39 100088 SER A, 100040 ARG A, 100091 SER A 1.85 38.11 -1.77 -0.67 19.59 83
    40 100088 SER A, 100040 ARG A 1.81 39.07 -2.45 -0.61 27.69 83
    41 100040 ARG A 1.85 44.91 -4.5 -0.42 52 83
    42 100040 ARG A, 100043 HIS A 2.59 46.14 -3.85 -0.08 51.8 87
    43 100040 ARG A, 100046 GLU A 2.83 50.39 -4 -0.78 50.95 80
    44 100040 ARG A, 100046 GLU A, 300018 ARG B 3.68 52.52 -4.17 -0.66 51.3 81
    45 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.55 56.4 -2 -0.04 38.51 86
    46 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.66 59.77 -0.98 -0.14 26.35 87
    47 100046 GLU A, 100064 ILE A, 100063 LYS A 3.53 60.56 0.2 -0.04 17.8 90
    48 100046 GLU A, 100064 ILE A, 100063 LYS A 3.32 65.06 -0.97 0.09 33.18 84
    49 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 4.51 65.41 -0.93 -0.18 25.3 92
    50 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 4.82 65.84 -1.1 -0.35 25.3 80
    51 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 5.06 69.97 0.23 0.35 24.92 76
    52 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.93 70.81 -1 -0.3 25.73 67
    53 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.69 71.29 -1.5 -0.4 21.26 76
    54 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.43 71.46 -2.4 -0.78 21.56 90
    55 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.94 71.67 -2.03 -0.87 14.58 96
    56 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.75 71.89 -2.4 -0.78 21.56 90
    57 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.48 72.8 -0.94 -0.32 11.61 84
    58 100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B 3.46 73.23 -0.3 -0.21 13.67 77
    59 100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B 3.48 73.67 -0.3 -0.21 13.67 77
    60 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.52 75.18 -1.08 -0.27 25.25 79
    61 100063 LYS A, 100003 LEU B, 100001 ASP B 3.77 76.98 -1.2 -0.1 33.11 70
    62 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 4.02 77.98 -1.08 -0.27 25.25 79
    63 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.12 78.19 -1.56 -0.42 30.14 81
    64 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.9 79.1 -0.98 -0.43 25.3 83
    65 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.88 79.26 -0.2 -0.37 13.72 82
    66 100003 LEU B, 300070 ASP B, 100001 ASP B 2.99 81.27 -0.03 -0.23 17.74 70
    67 100003 LEU B, 300070 ASP B 2.24 84.4 0.15 0.05 24.92 70
    68 100003 LEU B, 300070 ASP B, 100026 SER B 2.18 86.87 -0.17 -0.29 17.17 85
    69 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.57 88.63 -1.25 -0.32 25.88 85
    70 300070 ASP B, 100026 SER B, 300024 ARG B 3.27 90.42 -2.93 -0.81 34.46 95
    71 300070 ASP B, 300024 ARG B, 100026 SER B 3.57 91.33 -2.8 -0.75 35.03 84
    72 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.78 93.35 -2.28 -0.76 26.69 92
    73 300024 ARG B, 100026 SER B, 300069 THR B 4.66 94.39 -1.87 -0.66 19.01 95
    74 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.6 95.6 -1.5 -0.7 15.11 95
    75 100026 SER B, 300069 THR B, 300026 SER B 4.51 98.85 -0.5 -0.79 2.81 107
    76 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.83 101.26 -0.46 -0.79 3.04 107
    77 100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B 5.05 101.57 -1.28 -0.92 2.99 100
    78 100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B 4.22 104.42 -1.35 -0.91 2.56 102
    79 100026 SER B, 100027 GLN B, 300028 SER B 5.35 105.1 -1.57 -0.96 2.86 100
    80 300027 GLN B, 100027 GLN B, 300028 SER B 5.66 105.75 -1.57 -0.96 2.86 100
    81 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B 5.95 106.7 -2.05 -0.99 3.03 95
    82 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.42 107.65 -2.05 -0.99 3.03 95
    83 100027 GLN B, 300028 SER B, 100028 SER B 5.2 111.25 -1.7 -1.01 2.29 106
    84 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.76 111.57 -2.4 -0.87 14.72 100
    85 100027 GLN B, 100028 SER B, 100093 ARG B 4.45 111.95 -2.93 -0.83 19.07 94
    86 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.27 112.87 -2.4 -0.87 14.72 100
    87 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.14 113.57 -2.3 -0.82 15.15 94
    88 100027 GLN B, 300028 SER B, 100093 ARG B 2.77 118.3 -2.93 -0.83 19.07 94
    89 300028 SER B, 100093 ARG B 2.84 119.02 -2.65 -0.7 26.84 100
    90 300028 SER B, 100093 ARG B, 100082 TYR C 3.03 120.14 -2.2 -0.09 18.43 83
    91 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 3.68 123.21 -2.78 -0.18 26.82 83
    92 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C 6.24 124.03 -2.3 -0.3 22.13 83
    93 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.67 124.67 -2.22 -0.27 22.47 72
    94 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C 6.94 124.91 -1.58 0.04 12.4 61
    95 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B 6.96 125.3 -2.4 0.12 22.12 66
    96 300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C 6.83 125.71 -2.4 0.12 22.12 66
    97 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C 6.61 126.41 -2.22 -0.27 22.47 72
    98 100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C 5.89 128.32 -1.58 0.04 12.4 61
    99 100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C 3.21 131.64 -2.43 -0.3 15.13 72
    100 100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C 3.06 132.35 -2.2 -0.78 15.57 83
    101 100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C 3.14 133.45 -2.43 -0.3 15.13 72
    102 100093 ARG B, 200082 TYR C, 100058 GLN C 3.87 134.45 -3.1 -0.14 19.05 72
    103 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.79 135.03 -2.53 -0.35 14.7 83
    104 100028 SER B, 100093 ARG B, 100058 GLN C 3.79 135.31 -2.93 -0.83 19.07 94
    105 100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C 3.65 136.41 -2.53 -0.35 14.7 83
    106 100028 SER B, 100093 ARG B, 200082 TYR C 3.58 136.79 -2.2 -0.09 18.43 83
    107 100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C 3.5 137.24 -2.78 -0.18 26.82 83
    108 100028 SER B, 200093 ARG B, 200082 TYR C 3.28 139.27 -2.2 -0.09 18.43 83
    109 200027 GLN B, 100028 SER B, 200093 ARG B 3.16 144.42 -2.93 -0.83 19.07 94
    110 200027 GLN B, 100028 SER B, 200093 ARG B, 200028 SER B 3.77 144.86 -2.3 -0.82 15.15 94
    111 200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B 3.99 145.08 -2.4 -0.87 14.72 100
    112 200027 GLN B, 200028 SER B, 200093 ARG B 4.22 145.43 -2.93 -0.83 19.07 94
    113 200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B 4.94 145.92 -2.4 -0.87 14.72 100
    114 200027 GLN B, 200028 SER B, 100028 SER B 5.36 149.53 -1.7 -1.01 2.29 106
    115 300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B 6.43 150.46 -2.05 -0.99 3.03 95
    116 100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B 6.24 151.61 -2.05 -0.99 3.03 95
    117 100027 GLN B, 200027 GLN B, 100028 SER B 5.9 152.29 -2.6 -1.06 2.91 95
    118 200027 GLN B, 100028 SER B, 200026 SER B 5.51 152.94 -1.57 -0.96 2.86 100
    119 200027 GLN B, 100028 SER B, 200026 SER B, 100069 THR B 4.14 155.6 -1.35 -0.91 2.56 102
    120 200027 GLN B, 100028 SER B, 200026 SER B, 100027 GLN B 5.1 155.81 -1.28 -0.92 2.99 100
    121 100026 SER B, 100028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B 4.51 158.74 -0.46 -0.79 3.04 107
    122 100026 SER B, 200026 SER B, 100069 THR B, 100027 GLN B 4.38 159.68 -0.48 -0.79 2.95 107
    123 100026 SER B, 200026 SER B, 100069 THR B 4.32 161.57 -0.5 -0.79 2.81 107
    124 100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B 4.64 162.84 -1.5 -0.7 15.11 95
    125 200026 SER B, 100069 THR B, 100024 ARG B 4.39 164.56 -1.87 -0.66 19.01 95
    126 200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B 3.71 165.77 -2.28 -0.76 26.69 92
    127 200026 SER B, 100024 ARG B, 100070 ASP B 3.59 166.51 -2.8 -0.75 35.03 84
    128 100024 ARG B, 100070 ASP B, 200026 SER B 3.22 168.58 -2.93 -0.81 34.46 95
    129 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B 2.46 170.38 -1.25 -0.32 25.88 85
    130 100070 ASP B, 200026 SER B, 200003 LEU B 2.09 173.4 -0.17 -0.29 17.17 85
    131 100070 ASP B, 200003 LEU B 2.29 175.95 0.15 0.05 24.92 70
    132 100070 ASP B, 200003 LEU B, 200001 ASP B 3.03 177.91 -0.03 -0.23 17.74 70
    133 100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B 3.83 178.86 -0.98 -0.43 25.3 83
    134 100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A 4.19 179.08 -1.56 -0.42 30.14 81
    135 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A 3.99 180.32 -1.08 -0.27 25.25 79
    136 200003 LEU B, 200001 ASP B, 200063 LYS A 3.67 182.13 -1.2 -0.1 33.11 70
    137 200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B 3.53 183.98 -1.08 -0.27 25.25 79
    138 200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A 3.63 184.38 -1.08 -0.2 13.67 84
    139 200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B 3.72 185.17 -0.94 -0.32 11.61 84
    140 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A 4.07 185.36 -2.4 -0.78 21.56 90
    141 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A 4.19 185.93 -2.03 -0.87 14.58 96
    142 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A 4.48 186.67 -2.4 -0.78 21.56 90
    143 200003 LEU B, 200063 LYS A, 200061 ASN A, 200098 PHE B, 200046 GLU A 4.54 187.7 -1.5 -0.4 21.26 76
    144 200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A 4.57 188.86 -1 -0.3 25.73 67
    145 200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A 4.47 191.42 0.23 0.35 24.92 76
    146 200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B 4.29 192.26 -1.1 -0.35 25.3 80
    147 200063 LYS A, 200046 GLU A, 200064 ILE A, 100020 SER B 4.19 193.02 -0.93 -0.18 25.3 92
    148 200063 LYS A, 200046 GLU A, 200064 ILE A 3.81 197.71 -0.97 0.09 33.18 84
    149 200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B 3.74 200.93 -0.98 -0.14 26.35 87
    150 200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A 3.58 204.2 -2 -0.04 38.51 86
    151 200046 GLU A, 100018 ARG B, 200040 ARG A 3.91 206.96 -4.17 -0.66 51.3 81
    152 200046 GLU A, 200064 ILE A, 200040 ARG A 4.12 207.47 -1.17 0.08 34.01 87
    153 200046 GLU A, 200040 ARG A 2.19 210.96 -4 -0.78 50.95 80
    154 200040 ARG A 0.21 217.1 -4.5 -0.42 52 83
    155 200040 ARG A, 200088 SER A 0.25 217.87 -2.45 -0.61 27.69 83
    156 200040 ARG A, 200088 SER A, 200091 SER A 0.5 218.28 -1.77 -0.67 19.59 83
    157 200040 ARG A, 200088 SER A, 200091 SER A 0.92 218.51 -1.9 -0.73 19.02 100
    158 200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A 1.45 218.78 -1.83 -0.57 14.66 86
    159 200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A 2.05 219.53 -1.73 -0.53 15.09 70
    160 200040 ARG A, 200088 SER A, 200041 PRO A 3.24 222.04 -2.17 -0.44 18.99 70
    161 200040 ARG A, 200041 PRO A, 200088 SER A 4.9 224.17 -2.3 -0.49 18.42 86
    162 200041 PRO A, 200088 SER A 4.86 225.09 -1.2 -0.53 1.63 87
    163 200091 SER A, 200041 PRO A, 200088 SER A 4.55 226.03 -1.07 -0.68 1.64 97
    164 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A 4.42 226.42 0.15 -0.22 1.26 86
    165 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A 4.23 226.95 0.02 0.3 1.25 69
    166 200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A 4.16 227.13 0.23 0.08 1.27 84
    167 200091 SER A, 200088 SER A, 200180 TYR A 4.08 227.33 -0.97 -0.28 1.65 94
    168 200091 SER A, 200088 SER A 4.07 227.57 -0.8 -0.97 1.67 117
    169 200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A 4.07 228.08 0.23 0.08 1.27 84
    170 200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A 4.09 228.85 -0.06 0.08 1.67 69
    171 200041 PRO A, 200175 LEU A, 200180 TYR A 4.12 233.23 0.3 0.72 1.11 54
    172 200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A 4.33 233.51 0.13 0.34 1.68 54
    173 200041 PRO A, 200175 LEU A, 200180 TYR A 4.42 234.21 0.3 0.72 1.11 54
    174 200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A 4.1 234.8 0.13 0.34 1.68 54
    175 200041 PRO A, 200180 TYR A, 200173 ALA A 3.66 237.01 -1.1 0.07 2.19 54
    176 200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A 3.39 239.27 -1.7 -0.23 14.12 61
    177 200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A 3.4 241.37 -1.78 -0.53 14.11 64
    178 200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B 3.45 241.92 -2.55 -0.52 14.11 74
    179 200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B 3.18 242.54 -2.55 -0.52 14.11 74
    180 200153 GLU A, 200172 PRO A, 200041 ASN B 3.01 242.94 -2.87 -0.67 18.29 79
    181 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B 2.4 246.36 -2.25 -0.7 14.56 79
    182 200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A 2.42 246.87 -1.95 -0.88 15.01 90
    183 200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A 2.47 247.26 -1.64 -0.86 12.68 90
    184 200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A 2.52 247.66 -0.8 -0.47 12.03 78
    185 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A 2.64 248.56 -0.13 -0.31 2.57 79
    186 200041 ASN B, 200171 PHE A, 200182 LEU A 2.76 248.75 -0.03 -0.14 2.3 79
    187 200041 ASN B, 200182 LEU A, 200170 THR A 2.78 249.03 -0.13 -0.13 1.72 88
    188 200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A 2.69 250.61 -0.2 -0.3 2.14 88
    189 200041 ASN B, 200170 THR A, 200155 VAL A 2.8 254.19 -1.53 -0.78 2.81 105
    190 200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A 3.17 254.4 -1.33 -0.78 2.52 106
    191 200041 ASN B, 200156 THR A, 200157 VAL A 3.21 254.68 -1.53 -0.78 2.81 105
    192 200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A 3.21 254.84 -1.33 -0.78 2.52 106
    193 200041 ASN B, 200170 THR A, 200157 VAL A 3.19 254.95 -1.53 -0.78 2.81 105
    194 200041 ASN B, 200170 THR A, 200155 VAL A 3.17 255.18 -1.53 -0.78 2.81 105
    195 200041 ASN B, 200170 THR A, 200157 VAL A 3.24 255.35 -1.53 -0.78 2.81 105
    196 200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A 3.18 255.74 -1.33 -0.78 2.52 106
    197 200041 ASN B, 200170 THR A, 200157 VAL A 3.21 255.89 -1.53 -0.78 2.81 105
    198 200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A 3.27 256.6 -1.33 -0.78 2.52 106
    199 200041 ASN B, 200156 THR A, 200157 VAL A 3.46 259.11 -1.53 -0.78 2.81 105
    200 200041 ASN B, 200156 THR A, 200157 VAL A, 200040 THR B 4.05 259.11 -1.25 -0.79 2.95 105

    pore with bottle neck

    pore with local minimum

  16. show | | profile | lining residues
    Pore 16 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 200028 SER B, 69 THR B, 27 GLN B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300002 ILE B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300157 VAL A, 300156 THR A, 300040 THR B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 3 (12-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 14.62
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.24 0.13 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.2 1.95 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.31 4.01 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.6 4.22 -1.94 -0.69 11.94 88
    5 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.63 4.79 -2.25 -0.68 14.51 82
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.68 4.94 -1.78 -0.44 2.48 73
    7 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.64 5.44 -1.78 -0.44 2.48 73
    8 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.56 6.45 -1.78 -0.44 2.48 73
    9 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.49 7.25 -2.55 -0.52 14.11 74
    10 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.44 7.84 -2.55 -0.52 14.11 74
    11 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A 3.26 10.32 -1.78 -0.53 14.11 64
    12 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A 3.29 12.17 -1.7 -0.23 14.12 61
    13 100041 PRO A, 100173 ALA A, 100180 TYR A 3.78 14.16 -1.1 0.07 2.19 54
    14 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.44 14.68 0.13 0.34 1.68 54
    15 100041 PRO A, 100180 TYR A, 100175 LEU A 4.39 15.35 0.3 0.72 1.11 54
    16 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.39 15.69 0.13 0.34 1.68 54
    17 100041 PRO A, 100180 TYR A, 100175 LEU A 4.02 20.24 0.3 0.72 1.11 54
    18 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.02 20.89 -0.06 0.08 1.67 69
    19 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.03 21.28 0.02 0.3 1.25 69
    20 100180 TYR A, 100091 SER A, 100088 SER A 4.07 21.46 -0.97 -0.28 1.65 94
    21 100091 SER A, 100088 SER A 4.11 21.52 -0.8 -0.97 1.67 117
    22 100180 TYR A, 100091 SER A, 100088 SER A 4.17 21.83 -0.97 -0.28 1.65 94
    23 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.3 22.05 0.23 0.08 1.27 84
    24 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.37 22.7 0.02 0.3 1.25 69
    25 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.53 23.13 0.15 -0.22 1.26 86
    26 100041 PRO A, 100091 SER A, 100088 SER A 4.62 24.06 -1.07 -0.68 1.64 97
    27 100041 PRO A, 100088 SER A 4.82 25.14 -1.2 -0.53 1.63 87
    28 100041 PRO A, 100088 SER A, 100040 ARG A 4.8 27.6 -2.3 -0.49 18.42 86
    29 100041 PRO A, 100088 SER A, 100040 ARG A 3.35 29.71 -2.17 -0.44 18.99 70
    30 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.3 30.33 -1.73 -0.53 15.09 70
    31 100088 SER A, 100040 ARG A, 100091 SER A 0.78 31.49 -1.77 -0.67 19.59 83
    32 100088 SER A, 100040 ARG A 0.46 32.45 -2.45 -0.61 27.69 83
    33 100040 ARG A 0.3 39.24 -4.5 -0.42 52 83
    34 100040 ARG A, 100043 HIS A 2.11 40.21 -3.85 -0.08 51.8 87
    35 100040 ARG A, 100046 GLU A 2.69 43.39 -4 -0.78 50.95 80
    36 100040 ARG A, 100046 GLU A, 300018 ARG B 3.76 45.99 -4.17 -0.66 51.3 81
    37 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.49 49.55 -2 -0.04 38.51 86
    38 100046 GLU A, 300018 ARG B, 100064 ILE A 3.9 50.12 -1.17 0.08 34.01 87
    39 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.64 52.68 -0.98 -0.14 26.35 87
    40 100046 GLU A, 100064 ILE A, 100063 LYS A 3.47 53.45 0.2 -0.04 17.8 90
    41 100046 GLU A, 100064 ILE A, 100063 LYS A 3.17 58.39 -0.97 0.09 33.18 84
    42 100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B 5.01 59.12 -1.1 -0.35 25.3 80
    43 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 5.24 63.04 0.23 0.35 24.92 76
    44 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.93 63.91 -1 -0.3 25.73 67
    45 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.6 64.46 -1.5 -0.4 21.26 76
    46 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.26 64.71 -2.4 -0.78 21.56 90
    47 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.67 65.05 -2.03 -0.87 14.58 96
    48 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.62 65.26 -2.4 -0.78 21.56 90
    49 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.62 66.2 -0.94 -0.32 11.61 84
    50 100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B 3.73 66.61 -1.08 -0.2 13.67 84
    51 100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B 3.75 67.03 -0.3 -0.21 13.67 77
    52 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.72 68.48 -1.08 -0.27 25.25 79
    53 100063 LYS A, 100003 LEU B, 100001 ASP B 3.7 70.19 -1.2 -0.1 33.11 70
    54 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 3.74 71.2 -1.08 -0.27 25.25 79
    55 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.92 71.4 -1.56 -0.42 30.14 81
    56 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.97 72.39 -0.98 -0.43 25.3 83
    57 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.9 72.55 -0.2 -0.37 13.72 82
    58 100003 LEU B, 300070 ASP B, 100001 ASP B 3.04 74.73 -0.03 -0.23 17.74 70
    59 100003 LEU B, 300070 ASP B 2.11 77.72 0.15 0.05 24.92 70
    60 100003 LEU B, 300070 ASP B, 100026 SER B 2.07 80.07 -0.17 -0.29 17.17 85
    61 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.44 82.17 -1.25 -0.32 25.88 85
    62 300070 ASP B, 100026 SER B, 300024 ARG B 3.27 83.7 -2.93 -0.81 34.46 95
    63 300070 ASP B, 300024 ARG B, 100026 SER B 3.65 84.58 -2.8 -0.75 35.03 84
    64 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.68 86.45 -2.28 -0.76 26.69 92
    65 300024 ARG B, 100026 SER B, 300069 THR B 4.39 87.86 -1.87 -0.66 19.01 95
    66 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.86 88.61 -1.5 -0.7 15.11 95
    67 100026 SER B, 300069 THR B, 300026 SER B 4.31 91.26 -0.5 -0.79 2.81 107
    68 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B 4.34 92.17 -0.48 -0.79 2.95 107
    69 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.45 94.51 -0.46 -0.79 3.04 107
    70 100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B 5.08 94.65 -0.58 -0.84 2.52 112
    71 100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B 5.11 94.8 -1.28 -0.92 2.99 100
    72 100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B 4.17 97.83 -1.35 -0.91 2.56 102
    73 100026 SER B, 300028 SER B, 100027 GLN B 5.39 98.48 -1.57 -0.96 2.86 100
    74 300028 SER B, 100027 GLN B, 300027 GLN B 5.73 99.09 -2.6 -1.06 2.91 95
    75 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B 6.05 99.98 -2.05 -0.99 3.03 95
    76 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.52 100.83 -2.05 -0.99 3.03 95
    77 300028 SER B, 100027 GLN B, 100028 SER B 5.24 104.34 -1.7 -1.01 2.29 106
    78 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.75 104.89 -2.4 -0.87 14.72 100
    79 100027 GLN B, 100028 SER B, 100093 ARG B 4.66 105.29 -2.93 -0.83 19.07 94
    80 300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B 4.5 106.25 -2.4 -0.87 14.72 100
    81 300028 SER B, 100027 GLN B, 100093 ARG B 2.49 111.91 -2.93 -0.83 19.07 94
    82 300028 SER B, 100093 ARG B, 100082 TYR C 2.72 113.47 -2.2 -0.09 18.43 83
    83 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 3.48 113.83 -2.78 -0.18 26.82 83
    84 300028 SER B, 100082 TYR C, 300093 ARG B 3.71 114.16 -2.2 -0.09 18.43 83
    85 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.86 114.97 -2.53 -0.35 14.7 83
    86 300028 SER B, 300093 ARG B, 300058 GLN C 3.56 115.26 -2.93 -0.83 19.07 94
    87 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.47 115.89 -2.53 -0.35 14.7 83
    88 100082 TYR C, 300093 ARG B, 300058 GLN C 3.49 116.81 -3.1 -0.14 19.05 72
    89 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C 3.73 116.99 -2.43 -0.3 15.13 72
    90 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C 3.81 118.18 -2.43 -0.3 15.13 72
    91 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C 3.59 118.85 -2.2 -0.78 15.57 83
    92 300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C 3.43 122.45 -2.43 -0.3 15.13 72
    93 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C 4.71 123.37 -1.88 0.25 14.65 61
    94 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C 5.21 124.7 -1.58 0.04 12.4 61
    95 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.13 125.08 -2.4 0.12 22.12 66
    96 100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.71 125.59 -2.4 0.12 22.12 66
    97 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C 6.75 125.88 -2.22 -0.27 22.47 72
    98 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B 6.45 126.58 -2.22 -0.27 22.47 72
    99 300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B 6.06 127.4 -2.3 -0.3 22.13 83
    100 300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B 4.06 130.34 -2.78 -0.18 26.82 83
    101 300093 ARG B, 300082 TYR C, 28 SER B 2.88 132.23 -2.2 -0.09 18.43 83
    102 300093 ARG B, 28 SER B 2.6 132.94 -2.65 -0.7 26.84 100
    103 300027 GLN B, 300093 ARG B, 28 SER B 2.44 137.35 -2.93 -0.83 19.07 94
    104 300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B 4.42 137.89 -2.3 -0.82 15.15 94
    105 300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B 4.69 138.41 -2.4 -0.87 14.72 100
    106 300028 SER B, 300027 GLN B, 300093 ARG B 4.85 138.73 -2.93 -0.83 19.07 94
    107 300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B 4.83 139.19 -2.4 -0.87 14.72 100
    108 300028 SER B, 300027 GLN B, 28 SER B 4.93 143 -1.7 -1.01 2.29 106
    109 100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B 6.37 143.91 -2.05 -0.99 3.03 95
    110 300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B 5.93 145.05 -2.05 -0.99 3.03 95
    111 300027 GLN B, 27 GLN B, 28 SER B 5.65 145.7 -2.6 -1.06 2.91 95
    112 300026 SER B, 300027 GLN B, 28 SER B 5.35 146.31 -1.57 -0.96 2.86 100
    113 300026 SER B, 300027 GLN B, 28 SER B, 69 THR B 4.21 148.85 -1.35 -0.91 2.56 102
    114 300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B 5.12 149 -1.28 -0.92 2.99 100
    115 300026 SER B, 28 SER B, 69 THR B, 27 GLN B 5.13 149.29 -0.58 -0.84 2.52 112
    116 300026 SER B, 28 SER B, 69 THR B, 27 GLN B, 26 SER B 4.57 152.29 -0.46 -0.79 3.04 107
    117 300026 SER B, 69 THR B, 27 GLN B, 26 SER B 4.43 153.17 -0.48 -0.79 2.95 107
    118 300026 SER B, 69 THR B, 26 SER B 4.36 154.9 -0.5 -0.79 2.81 107
    119 300026 SER B, 69 THR B, 26 SER B, 24 ARG B 4.64 156.03 -1.5 -0.7 15.11 95
    120 300026 SER B, 69 THR B, 24 ARG B 4.46 157.64 -1.87 -0.66 19.01 95
    121 300026 SER B, 69 THR B, 24 ARG B, 70 ASP B 3.77 158.93 -2.28 -0.76 26.69 92
    122 300026 SER B, 24 ARG B, 70 ASP B 3.61 159.83 -2.8 -0.75 35.03 84
    123 24 ARG B, 70 ASP B, 300026 SER B 3.25 161.77 -2.93 -0.81 34.46 95
    124 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B 2.42 163.93 -1.25 -0.32 25.88 85
    125 70 ASP B, 300026 SER B, 300003 LEU B 2.1 166.29 -0.17 -0.29 17.17 85
    126 70 ASP B, 300003 LEU B 2.13 169.22 0.15 0.05 24.92 70
    127 70 ASP B, 300003 LEU B, 300001 ASP B 3.05 171.11 -0.03 -0.23 17.74 70
    128 70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B 3.87 171.24 -0.2 -0.37 13.72 82
    129 70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B 3.95 172.11 -0.98 -0.43 25.3 83
    130 70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A 3.9 172.55 -1.56 -0.42 30.14 81
    131 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A 3.68 173.88 -1.08 -0.27 25.25 79
    132 300003 LEU B, 300001 ASP B, 300063 LYS A 3.64 175.59 -1.2 -0.1 33.11 70
    133 300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B 3.71 176.91 -1.08 -0.27 25.25 79
    134 300003 LEU B, 300063 LYS A, 300097 THR B, 300002 ILE B 3.84 177.32 -0.3 -0.21 13.67 77
    135 300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A 3.85 177.7 -1.08 -0.2 13.67 84
    136 300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B 3.71 178.46 -0.94 -0.32 11.61 84
    137 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 3.68 178.65 -2.4 -0.78 21.56 90
    138 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 3.68 179.06 -2.03 -0.87 14.58 96
    139 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.19 179.63 -2.4 -0.78 21.56 90
    140 300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.54 180.52 -1.5 -0.4 21.26 76
    141 300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A 4.92 181.58 -1 -0.3 25.73 67
    142 300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A 5.3 184.81 0.23 0.35 24.92 76
    143 300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B 5.35 185.71 -1.1 -0.35 25.3 80
    144 300063 LYS A, 300046 GLU A, 300064 ILE A 2.98 190.86 -0.97 0.09 33.18 84
    145 300046 GLU A, 300064 ILE A, 300063 LYS A 3.24 191.6 0.2 -0.04 17.8 90
    146 300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B 3.43 193.98 -0.98 -0.14 26.35 87
    147 300046 GLU A, 300064 ILE A, 18 ARG B 3.85 194.53 -1.17 0.08 34.01 87
    148 300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A 3.54 197.51 -2 -0.04 38.51 86
    149 300046 GLU A, 18 ARG B, 300040 ARG A 3.95 200.14 -4.17 -0.66 51.3 81
    150 300046 GLU A, 300064 ILE A, 300040 ARG A 3.92 201.17 -1.17 0.08 34.01 87
    151 300046 GLU A, 300040 ARG A 2.92 203.41 -4 -0.78 50.95 80
    152 300040 ARG A 0.71 210.6 -4.5 -0.42 52 83
    153 300040 ARG A, 300088 SER A 0.73 211.26 -2.45 -0.61 27.69 83
    154 300040 ARG A, 300088 SER A, 300091 SER A 0.92 211.62 -1.77 -0.67 19.59 83
    155 300040 ARG A, 300088 SER A, 300091 SER A 1.24 211.84 -1.9 -0.73 19.02 100
    156 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A 1.66 212.09 -1.83 -0.57 14.66 86
    157 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A 2.15 212.8 -1.73 -0.53 15.09 70
    158 300040 ARG A, 300088 SER A, 300041 PRO A 3.17 215.17 -2.17 -0.44 18.99 70
    159 300040 ARG A, 300041 PRO A, 300088 SER A 4.77 217.25 -2.3 -0.49 18.42 86
    160 300041 PRO A, 300088 SER A 4.8 218.5 -1.2 -0.53 1.63 87
    161 300091 SER A, 300041 PRO A, 300088 SER A 4.55 219.39 -1.07 -0.68 1.64 97
    162 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A 4.46 219.76 0.15 -0.22 1.26 86
    163 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.3 220.25 0.02 0.3 1.25 69
    164 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.24 220.43 0.23 0.08 1.27 84
    165 300091 SER A, 300088 SER A, 300180 TYR A 4.13 220.62 -0.97 -0.28 1.65 94
    166 300091 SER A, 300088 SER A 4.08 220.81 -0.8 -0.97 1.67 117
    167 300091 SER A, 300088 SER A, 300180 TYR A 4.04 221.21 -0.97 -0.28 1.65 94
    168 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.02 221.87 0.02 0.3 1.25 69
    169 300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A 4.01 222.71 -0.06 0.08 1.67 69
    170 300041 PRO A, 300175 LEU A, 300180 TYR A 4.01 226.59 0.3 0.72 1.11 54
    171 300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A 4.36 226.85 0.13 0.34 1.68 54
    172 300041 PRO A, 300175 LEU A, 300180 TYR A 4.41 227.5 0.3 0.72 1.11 54
    173 300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A 4.44 228.31 0.13 0.34 1.68 54
    174 300041 PRO A, 300180 TYR A, 300173 ALA A 3.8 230.46 -1.1 0.07 2.19 54
    175 300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A 3.29 232.18 -1.7 -0.23 14.12 61
    176 300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A 3.27 234.59 -1.78 -0.53 14.11 64
    177 300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B 3.41 235.13 -2.55 -0.52 14.11 74
    178 300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B 3.31 235.67 -2.55 -0.52 14.11 74
    179 300153 GLU A, 300172 PRO A, 300041 ASN B 3.12 236.42 -2.87 -0.67 18.29 79
    180 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B 2.43 239.73 -2.25 -0.7 14.56 79
    181 300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A 2.39 240.21 -1.95 -0.88 15.01 90
    182 300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A 2.39 240.57 -0.8 -0.47 12.03 78
    183 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A 2.41 240.97 -0.8 -0.47 12.03 78
    184 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A 2.59 241.75 -0.13 -0.31 2.57 79
    185 300041 ASN B, 300182 LEU A, 300171 PHE A 2.75 242.11 -0.03 -0.14 2.3 79
    186 300041 ASN B, 300182 LEU A, 300170 THR A 2.78 242.36 -0.13 -0.13 1.72 88
    187 300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A 2.53 243.76 -0.2 -0.3 2.14 88
    188 300041 ASN B, 300170 THR A, 300155 VAL A 2.53 247.32 -1.53 -0.78 2.81 105
    189 300041 ASN B, 300170 THR A, 300155 VAL A, 300157 VAL A 2.93 247.63 -1.25 -0.79 2.95 105
    190 300041 ASN B, 300157 VAL A, 300156 THR A 3.03 247.89 -1.53 -0.78 2.81 105
    191 300041 ASN B, 300170 THR A, 300157 VAL A, 300156 THR A 3.19 248.19 -1.33 -0.78 2.52 106
    192 300041 ASN B, 300170 THR A, 300157 VAL A 3.2 248.28 -1.53 -0.78 2.81 105
    193 300041 ASN B, 300170 THR A, 300155 VAL A 3.17 248.49 -1.53 -0.78 2.81 105
    194 300041 ASN B, 300170 THR A, 300157 VAL A 3.22 248.66 -1.53 -0.78 2.81 105
    195 300041 ASN B, 300170 THR A, 300157 VAL A, 300156 THR A 3.19 249.09 -1.33 -0.78 2.52 106
    196 300170 THR A, 300157 VAL A, 300156 THR A 3.22 249.27 -0.6 -0.78 2.23 107
    197 300041 ASN B, 300170 THR A, 300157 VAL A, 300156 THR A 3.28 249.58 -1.33 -0.78 2.52 106
    198 300041 ASN B, 300157 VAL A, 300156 THR A 3.37 252.43 -1.53 -0.78 2.81 105
    199 300041 ASN B, 300157 VAL A, 300156 THR A, 300040 THR B 4.05 252.43 -1.25 -0.79 2.95 105

    pore with bottle neck

    pore with local minimum

  17. show | | profile | lining residues
    Pore 17 profile

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100079 GLY C, 28 SER B, 200028 SER B, 69 THR B, 27 GLN B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 4 (12-8)
    Hydropathy: -1.4
    Hydrophobicity: -0.43
    Polarity: 14.35
    Mutability: 86

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.26 0.27 -1.33 -0.78 2.52 106
    2 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.45 -1.53 -0.78 2.81 105
    3 100170 THR A, 100041 ASN B, 100155 VAL A 3.19 0.62 -1.53 -0.78 2.81 105
    4 100157 VAL A, 100170 THR A, 100041 ASN B 3.2 0.77 -1.53 -0.78 2.81 105
    5 100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B 3.19 1.05 -1.33 -0.78 2.52 106
    6 100156 THR A, 100157 VAL A, 100041 ASN B 3.04 1.59 -1.53 -0.78 2.81 105
    7 100170 THR A, 100041 ASN B, 100155 VAL A 2.62 5.8 -1.53 -0.78 2.81 105
    8 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A 2.61 6.54 -0.2 -0.3 2.14 88
    9 100170 THR A, 100041 ASN B, 100182 LEU A 2.8 6.87 -0.13 -0.13 1.72 88
    10 100041 ASN B, 100182 LEU A, 100171 PHE A 2.76 7.23 -0.03 -0.14 2.3 79
    11 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A 2.57 7.96 -0.13 -0.31 2.57 79
    12 100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A 2.4 8.49 -0.8 -0.47 12.03 78
    13 100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.32 8.97 -0.8 -0.47 12.03 78
    14 100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A 2.26 9.54 -1.95 -0.88 15.01 90
    15 100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A 2.24 12.84 -2.25 -0.7 14.56 79
    16 100041 ASN B, 100153 GLU A, 100172 PRO A 3.13 13.2 -2.87 -0.67 18.29 79
    17 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.33 13.76 -2.55 -0.52 14.11 74
    18 100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A 3.6 14.67 -2.55 -0.52 14.11 74
    19 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A 3.4 16.96 -1.78 -0.53 14.11 64
    20 100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A 3.35 18.88 -1.7 -0.23 14.12 61
    21 100173 ALA A, 100041 PRO A, 100180 TYR A 3.49 20.95 -1.1 0.07 2.19 54
    22 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.09 21.36 0.13 0.34 1.68 54
    23 100041 PRO A, 100180 TYR A, 100175 LEU A 4.38 22.07 0.3 0.72 1.11 54
    24 100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A 4.4 22.43 0.13 0.34 1.68 54
    25 100041 PRO A, 100180 TYR A, 100175 LEU A 4.3 27.21 0.3 0.72 1.11 54
    26 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.26 27.8 -0.06 0.08 1.67 69
    27 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.22 28.12 0.23 0.08 1.27 84
    28 100180 TYR A, 100091 SER A, 100088 SER A 4.18 28.23 -0.97 -0.28 1.65 94
    29 100091 SER A, 100088 SER A 4.17 28.32 -0.8 -0.97 1.67 117
    30 100180 TYR A, 100091 SER A, 100088 SER A 4.17 28.49 -0.97 -0.28 1.65 94
    31 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A 4.2 28.97 0.23 0.08 1.27 84
    32 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.32 29.34 0.02 0.3 1.25 69
    33 100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A 4.44 29.78 0.15 -0.22 1.26 86
    34 100041 PRO A, 100091 SER A, 100088 SER A 4.58 30.75 -1.07 -0.68 1.64 97
    35 100041 PRO A, 100088 SER A 4.94 31.89 -1.2 -0.53 1.63 87
    36 100041 PRO A, 100088 SER A, 100040 ARG A 4.51 33.93 -2.3 -0.49 18.42 86
    37 100041 PRO A, 100088 SER A, 100040 ARG A 3 36.29 -2.17 -0.44 18.99 70
    38 100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A 2.38 36.98 -1.73 -0.53 15.09 70
    39 100088 SER A, 100040 ARG A, 100091 SER A 1.85 38.11 -1.77 -0.67 19.59 83
    40 100088 SER A, 100040 ARG A 1.81 39.07 -2.45 -0.61 27.69 83
    41 100040 ARG A 1.85 44.91 -4.5 -0.42 52 83
    42 100040 ARG A, 100043 HIS A 2.59 46.14 -3.85 -0.08 51.8 87
    43 100040 ARG A, 100046 GLU A 2.83 50.39 -4 -0.78 50.95 80
    44 100040 ARG A, 100046 GLU A, 300018 ARG B 3.68 52.52 -4.17 -0.66 51.3 81
    45 100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A 3.55 56.4 -2 -0.04 38.51 86
    46 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A 3.66 59.77 -0.98 -0.14 26.35 87
    47 100046 GLU A, 100064 ILE A, 100063 LYS A 3.53 60.56 0.2 -0.04 17.8 90
    48 100046 GLU A, 100064 ILE A, 100063 LYS A 3.32 65.06 -0.97 0.09 33.18 84
    49 100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B 4.51 65.41 -0.93 -0.18 25.3 92
    50 100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B 4.82 65.84 -1.1 -0.35 25.3 80
    51 100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B 5.06 69.97 0.23 0.35 24.92 76
    52 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B 4.93 70.81 -1 -0.3 25.73 67
    53 100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A 4.69 71.29 -1.5 -0.4 21.26 76
    54 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 4.43 71.46 -2.4 -0.78 21.56 90
    55 100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.94 71.67 -2.03 -0.87 14.58 96
    56 100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B 3.75 71.89 -2.4 -0.78 21.56 90
    57 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B 3.48 72.8 -0.94 -0.32 11.61 84
    58 100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B 3.46 73.23 -0.3 -0.21 13.67 77
    59 100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B 3.48 73.67 -0.3 -0.21 13.67 77
    60 100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B 3.52 75.18 -1.08 -0.27 25.25 79
    61 100063 LYS A, 100003 LEU B, 100001 ASP B 3.77 76.98 -1.2 -0.1 33.11 70
    62 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B 4.02 77.98 -1.08 -0.27 25.25 79
    63 100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 4.12 78.19 -1.56 -0.42 30.14 81
    64 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B 3.9 79.1 -0.98 -0.43 25.3 83
    65 100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B 3.88 79.26 -0.2 -0.37 13.72 82
    66 100003 LEU B, 300070 ASP B, 100001 ASP B 2.99 81.27 -0.03 -0.23 17.74 70
    67 100003 LEU B, 300070 ASP B 2.24 84.4 0.15 0.05 24.92 70
    68 100003 LEU B, 300070 ASP B, 100026 SER B 2.18 86.87 -0.17 -0.29 17.17 85
    69 100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B 2.57 88.63 -1.25 -0.32 25.88 85
    70 300070 ASP B, 100026 SER B, 300024 ARG B 3.27 90.42 -2.93 -0.81 34.46 95
    71 300070 ASP B, 300024 ARG B, 100026 SER B 3.57 91.33 -2.8 -0.75 35.03 84
    72 300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B 3.78 93.35 -2.28 -0.76 26.69 92
    73 300024 ARG B, 100026 SER B, 300069 THR B 4.66 94.39 -1.87 -0.66 19.01 95
    74 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B 4.6 95.6 -1.5 -0.7 15.11 95
    75 100026 SER B, 300069 THR B, 300026 SER B 4.51 98.85 -0.5 -0.79 2.81 107
    76 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B 4.83 101.26 -0.46 -0.79 3.04 107
    77 100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B 5.05 101.57 -1.28 -0.92 2.99 100
    78 100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B 4.22 104.42 -1.35 -0.91 2.56 102
    79 100026 SER B, 100027 GLN B, 300028 SER B 5.35 105.1 -1.57 -0.96 2.86 100
    80 300027 GLN B, 100027 GLN B, 300028 SER B 5.66 105.75 -1.57 -0.96 2.86 100
    81 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B 5.95 106.7 -2.05 -0.99 3.03 95
    82 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B 6.41 107.65 -2.05 -0.99 3.03 95
    83 100027 GLN B, 300028 SER B, 100028 SER B 5.21 111.25 -1.7 -1.01 2.29 106
    84 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.75 111.57 -2.4 -0.87 14.72 100
    85 100027 GLN B, 100028 SER B, 100093 ARG B 4.4 111.97 -2.93 -0.83 19.07 94
    86 100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B 4.21 112.93 -2.4 -0.87 14.72 100
    87 100027 GLN B, 300028 SER B, 100093 ARG B 2.78 118.18 -2.93 -0.83 19.07 94
    88 300028 SER B, 100093 ARG B 2.79 118.9 -2.65 -0.7 26.84 100
    89 300028 SER B, 100093 ARG B, 100082 TYR C 2.88 120.4 -2.2 -0.09 18.43 83
    90 300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B 3.44 120.76 -2.78 -0.18 26.82 83
    91 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.64 121.67 -2.53 -0.35 14.7 83
    92 300028 SER B, 300093 ARG B, 300058 GLN C 3.82 121.98 -2.93 -0.83 19.07 94
    93 300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C 3.75 122.65 -2.53 -0.35 14.7 83
    94 100082 TYR C, 300093 ARG B, 300058 GLN C 3.76 123.6 -3.1 -0.14 19.05 72
    95 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C 3.72 123.78 -2.43 -0.3 15.13 72
    96 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C 3.36 125.17 -2.43 -0.3 15.13 72
    97 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C 3.43 125.8 -2.2 -0.78 15.57 83
    98 300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C 3.78 129.31 -2.43 -0.3 15.13 72
    99 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C 5.35 130.26 -1.88 0.25 14.65 61
    100 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C 5.67 131.52 -1.58 0.04 12.4 61
    101 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.25 131.75 -2.4 0.12 22.12 66
    102 100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C 6.47 132.16 -2.4 0.12 22.12 66
    103 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100079 GLY C 6.78 132.45 -1.58 0.04 12.4 61
    104 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B 6.44 133.57 -2.22 -0.27 22.47 72
    105 300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B 6.21 134.01 -2.3 -0.3 22.13 83
    106 300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B 3.95 137.11 -2.78 -0.18 26.82 83
    107 300093 ARG B, 300082 TYR C, 28 SER B 3.25 139.15 -2.2 -0.09 18.43 83
    108 300093 ARG B, 28 SER B 3.13 139.88 -2.65 -0.7 26.84 100
    109 300027 GLN B, 300093 ARG B, 28 SER B 3.07 144.46 -2.93 -0.83 19.07 94
    110 300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B 3.84 144.88 -2.3 -0.82 15.15 94
    111 300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B 4.05 145.08 -2.4 -0.87 14.72 100
    112 300028 SER B, 300027 GLN B, 300093 ARG B 4.27 145.42 -2.93 -0.83 19.07 94
    113 300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B 4.94 145.92 -2.4 -0.87 14.72 100
    114 300028 SER B, 300027 GLN B, 28 SER B 5.35 149.53 -1.7 -1.01 2.29 106
    115 100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B 6.44 150.46 -2.05 -0.99 3.03 95
    116 300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B 6.24 151.6 -2.05 -0.99 3.03 95
    117 300027 GLN B, 27 GLN B, 28 SER B 5.9 152.28 -2.6 -1.06 2.91 95
    118 300026 SER B, 300027 GLN B, 28 SER B 5.5 152.94 -1.57 -0.96 2.86 100
    119 300026 SER B, 300027 GLN B, 28 SER B, 69 THR B 4.14 155.6 -1.35 -0.91 2.56 102
    120 300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B 5.1 155.81 -1.28 -0.92 2.99 100
    121 300026 SER B, 28 SER B, 69 THR B, 27 GLN B, 26 SER B 4.51 158.73 -0.46 -0.79 3.04 107
    122 300026 SER B, 69 THR B, 27 GLN B, 26 SER B 4.38 159.68 -0.48 -0.79 2.95 107
    123 300026 SER B, 69 THR B, 26 SER B 4.32 161.57 -0.5 -0.79 2.81 107
    124 300026 SER B, 69 THR B, 26 SER B, 24 ARG B 4.64 162.83 -1.5 -0.7 15.11 95
    125 300026 SER B, 69 THR B, 24 ARG B 4.39 164.56 -1.87 -0.66 19.01 95
    126 300026 SER B, 69 THR B, 24 ARG B, 70 ASP B 3.71 165.77 -2.28 -0.76 26.69 92
    127 300026 SER B, 24 ARG B, 70 ASP B 3.59 166.51 -2.8 -0.75 35.03 84
    128 24 ARG B, 70 ASP B, 300026 SER B 3.22 168.58 -2.93 -0.81 34.46 95
    129 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B 2.46 170.38 -1.25 -0.32 25.88 85
    130 70 ASP B, 300026 SER B, 300003 LEU B 2.09 173.4 -0.17 -0.29 17.17 85
    131 70 ASP B, 300003 LEU B 2.29 175.94 0.15 0.05 24.92 70
    132 70 ASP B, 300003 LEU B, 300001 ASP B 3.03 177.91 -0.03 -0.23 17.74 70
    133 70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B 3.83 178.86 -0.98 -0.43 25.3 83
    134 70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A 4.19 179.08 -1.56 -0.42 30.14 81
    135 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A 3.99 180.32 -1.08 -0.27 25.25 79
    136 300003 LEU B, 300001 ASP B, 300063 LYS A 3.67 182.13 -1.2 -0.1 33.11 70
    137 300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B 3.53 183.98 -1.08 -0.27 25.25 79
    138 300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A 3.63 184.38 -1.08 -0.2 13.67 84
    139 300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B 3.72 185.17 -0.94 -0.32 11.61 84
    140 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.07 185.36 -2.4 -0.78 21.56 90
    141 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.19 185.93 -2.03 -0.87 14.58 96
    142 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.48 186.67 -2.4 -0.78 21.56 90
    143 300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A 4.54 187.7 -1.5 -0.4 21.26 76
    144 300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A 4.57 188.86 -1 -0.3 25.73 67
    145 300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A 4.47 191.42 0.23 0.35 24.92 76
    146 300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B 4.29 192.26 -1.1 -0.35 25.3 80
    147 300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B 4.19 193.01 -0.93 -0.18 25.3 92
    148 300063 LYS A, 300046 GLU A, 300064 ILE A 3.81 197.71 -0.97 0.09 33.18 84
    149 300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B 3.74 200.92 -0.98 -0.14 26.35 87
    150 300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A 3.58 204.19 -2 -0.04 38.51 86
    151 300046 GLU A, 18 ARG B, 300040 ARG A 3.91 206.96 -4.17 -0.66 51.3 81
    152 300046 GLU A, 300064 ILE A, 300040 ARG A 4.12 207.47 -1.17 0.08 34.01 87
    153 300046 GLU A, 300040 ARG A 2.19 210.96 -4 -0.78 50.95 80
    154 300040 ARG A 0.21 217.1 -4.5 -0.42 52 83
    155 300040 ARG A, 300088 SER A 0.25 217.86 -2.45 -0.61 27.69 83
    156 300040 ARG A, 300088 SER A, 300091 SER A 0.5 218.27 -1.77 -0.67 19.59 83
    157 300040 ARG A, 300088 SER A, 300091 SER A 0.92 218.51 -1.9 -0.73 19.02 100
    158 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A 1.45 218.78 -1.83 -0.57 14.66 86
    159 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A 2.05 219.53 -1.73 -0.53 15.09 70
    160 300040 ARG A, 300088 SER A, 300041 PRO A 3.24 222.04 -2.17 -0.44 18.99 70
    161 300040 ARG A, 300041 PRO A, 300088 SER A 4.9 224.17 -2.3 -0.49 18.42 86
    162 300041 PRO A, 300088 SER A 4.86 225.08 -1.2 -0.53 1.63 87
    163 300091 SER A, 300041 PRO A, 300088 SER A 4.55 226.03 -1.07 -0.68 1.64 97
    164 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A 4.42 226.42 0.15 -0.22 1.26 86
    165 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.23 226.95 0.02 0.3 1.25 69
    166 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.16 227.13 0.23 0.08 1.27 84
    167 300091 SER A, 300088 SER A, 300180 TYR A 4.08 227.32 -0.97 -0.28 1.65 94
    168 300091 SER A, 300088 SER A 4.07 227.57 -0.8 -0.97 1.67 117
    169 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A 4.07 228.08 0.23 0.08 1.27 84
    170 300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A 4.09 228.85 -0.06 0.08 1.67 69
    171 300041 PRO A, 300175 LEU A, 300180 TYR A 4.12 233.23 0.3 0.72 1.11 54
    172 300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A 4.33 233.51 0.13 0.34 1.68 54
    173 300041 PRO A, 300175 LEU A, 300180 TYR A 4.42 234.21 0.3 0.72 1.11 54
    174 300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A 4.1 234.79 0.13 0.34 1.68 54
    175 300041 PRO A, 300180 TYR A, 300173 ALA A 3.66 237.01 -1.1 0.07 2.19 54
    176 300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A 3.39 239.27 -1.7 -0.23 14.12 61
    177 300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A 3.4 241.37 -1.78 -0.53 14.11 64
    178 300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B 3.45 241.92 -2.55 -0.52 14.11 74
    179 300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B 3.18 242.54 -2.55 -0.52 14.11 74
    180 300153 GLU A, 300172 PRO A, 300041 ASN B 3.01 242.93 -2.87 -0.67 18.29 79
    181 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B 2.4 246.36 -2.25 -0.7 14.56 79
    182 300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A 2.42 246.87 -1.95 -0.88 15.01 90
    183 300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A 2.47 247.26 -1.64 -0.86 12.68 90
    184 300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A 2.52 247.66 -0.8 -0.47 12.03 78
    185 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A 2.64 248.56 -0.13 -0.31 2.57 79
    186 300041 ASN B, 300171 PHE A, 300182 LEU A 2.76 248.75 -0.03 -0.14 2.3 79
    187 300041 ASN B, 300182 LEU A, 300170 THR A 2.78 249.03 -0.13 -0.13 1.72 88
    188 300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A 2.69 250.61 -0.2 -0.3 2.14 88
    189 300041 ASN B, 300170 THR A, 300155 VAL A 2.8 254.19 -1.53 -0.78 2.81 105
    190 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 3.17 254.4 -1.33 -0.78 2.52 106
    191 300041 ASN B, 300156 THR A, 300157 VAL A 3.21 254.68 -1.53 -0.78 2.81 105
    192 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 3.21 254.84 -1.33 -0.78 2.52 106
    193 300041 ASN B, 300170 THR A, 300157 VAL A 3.19 254.95 -1.53 -0.78 2.81 105
    194 300041 ASN B, 300170 THR A, 300155 VAL A 3.17 255.18 -1.53 -0.78 2.81 105
    195 300041 ASN B, 300170 THR A, 300157 VAL A 3.24 255.35 -1.53 -0.78 2.81 105
    196 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 3.18 255.74 -1.33 -0.78 2.52 106
    197 300041 ASN B, 300170 THR A, 300157 VAL A 3.21 255.89 -1.53 -0.78 2.81 105
    198 300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A 3.27 256.6 -1.33 -0.78 2.52 106
    199 300041 ASN B, 300156 THR A, 300157 VAL A 3.46 259.11 -1.53 -0.78 2.81 105
    200 300041 ASN B, 300156 THR A, 300157 VAL A, 300040 THR B 4.05 259.11 -1.25 -0.79 2.95 105

    pore with bottle neck

    pore with local minimum

  18. show | | profile | lining residues
    Pore 18 profile

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200002 ILE B, 200061 ASN A, 200098 PHE B, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A, 200170 THR A, 200155 VAL A, 200157 VAL A, 200156 THR A, 200040 THR B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 3 (12-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 14.55
    Mutability: 87

    Lining residues

    show all | hide all

    # Res Btn Dist Hpa Hpb Pol Mut
    1 100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B 3.24 0.13 -2.03 -0.85 14.53 99
    2 100042 GLY A, 100040 THR B, 100165 ASP B 3.2 1.95 -1.53 -0.87 18.25 96
    3 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B 3.31 4.01 -2.03 -0.85 14.53 99
    4 100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.6 4.22 -1.94 -0.69 11.94 88
    5 100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A 3.63 4.79 -2.25 -0.68 14.51 82
    6 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.68 4.94 -1.78 -0.44 2.48 73
    7 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.64 5.44 -1.78 -0.44 2.48 73
    8 100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A 3.56 6.45 -1.78 -0.44 2.48 73
    9 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.49 7.25 -2.55 -0.52 14.11 74
    10 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A 3.44 7.84 -2.55 -0.52 14.11 74
    11 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A 3.26 10.32 -1.78 -0.53 14.11 64
    12 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A 3.29 12.17 -1.7 -0.23 14.12 61
    13 100041 PRO A, 100173 ALA A, 100180 TYR A 3.78 14.16 -1.1 0.07 2.19 54
    14 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.44 14.68 0.13 0.34 1.68 54
    15 100041 PRO A, 100180 TYR A, 100175 LEU A 4.39 15.35 0.3 0.72 1.11 54
    16 100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A 4.39 15.69 0.13 0.34 1.68 54
    17 100041 PRO A, 100180 TYR A, 100175 LEU A 4.02 20.24 0.3 0.72 1.11 54
    18 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A 4.02 20.89 -0.06 0.08 1.67 69
    19 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A 4.03 21.28 0.02 0.3 1.25 69
    20 100180 TYR A, 100091 SER A, 100088 SER A 4.07 21.46 -0.97 -0.28 1.65 94
    21 100091 SER A, 100088 SER A 4.11 21.52 -0.8 -0.97 1.67 117
    22