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***  GTP-BINDING 21-JAN-97 1MH1  ***

CA distance fluctuations for 2610071816113154659

---  normal mode 8  ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok
largest increasereflargest decrease
PRO 181 1.00 GLY 1 -0.11 ASN 43
PRO 181 0.79 SER 2 -0.13 LYS 132
PRO 181 0.55 PRO 1 -0.13 LYS 132
PRO 181 0.38 GLN 2 -0.14 LYS 132
PRO 181 0.25 ALA 3 -0.19 LYS 132
GLY 1 0.20 ILE 4 -0.19 LYS 132
GLY 1 0.12 LYS 5 -0.24 LYS 132
GLY 1 0.12 CYS 6 -0.25 LYS 128
GLY 1 0.09 VAL 7 -0.31 LYS 132
GLY 1 0.08 VAL 8 -0.34 LYS 128
GLY 1 0.07 VAL 9 -0.40 LYS 132
LEU 160 0.10 GLY 10 -0.44 LYS 132
LEU 160 0.12 ASP 11 -0.57 LYS 132
LEU 160 0.12 GLY 12 -0.70 LYS 132
LEU 160 0.18 ALA 13 -0.74 LYS 128
LEU 160 0.17 VAL 14 -0.53 LYS 128
LEU 160 0.19 GLY 15 -0.50 LYS 128
LEU 19 0.08 LYS 16 -0.45 LYS 128
GLY 60 0.10 THR 17 -0.50 LYS 128
ALA 13 0.11 CYS 18 -0.45 LYS 128
PRO 180 0.11 LEU 19 -0.33 LYS 128
PRO 180 0.12 LEU 20 -0.34 LYS 128
PRO 180 0.15 ILE 21 -0.36 LYS 128
PRO 180 0.18 SER 22 -0.28 LYS 128
PRO 180 0.20 TYR 23 -0.22 LYS 128
PRO 180 0.21 THR 24 -0.25 LYS 128
PRO 180 0.22 THR 25 -0.26 LYS 128
PRO 180 0.24 ASN 26 -0.21 LYS 128
PRO 180 0.20 ALA 27 -0.29 ASP 124
PRO 180 0.16 PHE 28 -0.38 ASP 124
PRO 180 0.14 PRO 29 -0.52 ASP 124
PRO 180 0.13 GLY 30 -0.66 ASP 124
PRO 180 0.09 GLU 31 -0.86 ASP 124
PRO 34 0.12 TYR 32 -0.90 LYS 128
THR 25 0.08 ILE 33 -0.93 LYS 128
TYR 32 0.12 PRO 34 -0.82 LYS 128
TYR 32 0.06 THR 35 -0.67 LYS 128
ILE 33 0.05 VAL 36 -0.61 LYS 128
ALA 42 0.05 PHE 37 -0.51 LYS 128
VAL 44 0.06 ASP 38 -0.48 LYS 128
PRO 180 0.08 ASN 39 -0.39 LYS 128
PRO 180 0.13 TYR 40 -0.34 LYS 128
PRO 180 0.17 SER 41 -0.27 LYS 128
PRO 180 0.24 ALA 42 -0.20 LYS 128
PRO 181 0.33 ASN 43 -0.16 LYS 128
PRO 180 0.36 VAL 44 -0.09 LYS 132
PRO 180 0.46 MET 45 -0.11 ASN 107
PRO 180 0.46 VAL 46 -0.11 ASN 107
PRO 180 0.57 ASP 47 -0.18 ASN 107
PRO 180 0.80 GLY 48 -0.16 ASN 107
PRO 180 0.60 LYS 49 -0.18 ASN 107
PRO 181 0.51 PRO 50 -0.12 ASN 107
PRO 181 0.34 VAL 51 -0.12 LYS 132
PRO 181 0.30 ASN 52 -0.18 LYS 128
PRO 180 0.17 LEU 53 -0.20 LYS 128
PRO 180 0.10 GLY 54 -0.27 LYS 128
PRO 180 0.07 LEU 55 -0.31 LYS 128
GLY 150 0.04 TRP 56 -0.37 LYS 128
VAL 44 0.04 ASP 57 -0.44 LYS 128
LEU 20 0.05 THR 58 -0.49 LYS 128
THR 17 0.08 ALA 59 -0.60 LYS 128
THR 17 0.10 GLY 60 -0.62 LYS 132
THR 17 0.09 GLN 61 -0.76 LYS 132
THR 17 0.06 GLU 62 -0.74 LYS 132
TYR 32 0.08 ASP 63 -0.74 LYS 132
TYR 32 0.06 TYR 64 -0.64 LYS 132
PRO 99 0.05 ASP 65 -0.58 LYS 132
TYR 32 0.04 ARG 66 -0.54 LYS 132
GLY 150 0.05 LEU 67 -0.52 LYS 132
GLY 150 0.06 ARG 68 -0.48 LYS 132
GLY 150 0.07 PRO 69 -0.42 LYS 132
GLY 150 0.07 LEU 70 -0.41 LYS 132
GLY 150 0.07 SER 71 -0.39 LYS 132
GLY 150 0.09 TYR 72 -0.33 LYS 132
GLY 150 0.10 PRO 73 -0.30 LYS 132
GLY 150 0.11 GLN 74 -0.25 LYS 132
GLY 1 0.13 THR 75 -0.26 LYS 132
GLY 1 0.23 ASP 76 -0.28 CYS 178
GLY 1 0.22 VAL 77 -0.33 PRO 181
GLY 1 0.16 SER 78 -0.38 PRO 181
GLY 1 0.14 LEU 79 -0.37 PRO 181
GLY 1 0.12 ILE 80 -0.45 PRO 181
GLY 1 0.10 CYS 81 -0.39 PRO 181
LEU 160 0.11 PHE 82 -0.41 PRO 181
LEU 160 0.13 SER 83 -0.35 PRO 181
GLY 1 0.10 LEU 84 -0.34 PRO 181
ASP 47 0.08 VAL 85 -0.45 ILE 33
LEU 160 0.10 SER 86 -0.37 PRO 181
SER 86 0.09 PRO 87 -0.44 PRO 181
LEU 160 0.13 ALA 88 -0.45 PRO 181
LEU 160 0.13 SER 89 -0.44 PRO 181
GLY 1 0.10 PHE 90 -0.50 PRO 181
GLY 1 0.10 GLU 91 -0.55 PRO 181
LEU 160 0.11 ASN 92 -0.52 PRO 181
GLY 1 0.11 VAL 93 -0.57 PRO 181
GLY 1 0.12 ARG 94 -0.66 PRO 181
GLY 1 0.09 ALA 95 -0.60 PRO 181
GLY 1 0.08 LYS 96 -0.54 PRO 181
GLY 1 0.09 TRP 97 -0.53 PRO 181
GLY 1 0.12 TYR 98 -0.64 PRO 181
GLY 1 0.10 PRO 99 -0.64 PRO 181
GLY 1 0.09 GLU 100 -0.52 PRO 181
GLY 1 0.11 VAL 101 -0.53 PRO 181
ILE 149 0.14 ARG 102 -0.65 PRO 181
GLY 150 0.11 HIS 103 -0.58 PRO 181
GLY 150 0.12 HIS 104 -0.46 PRO 181
GLY 150 0.15 CYS 105 -0.48 PRO 181
GLY 150 0.21 PRO 106 -0.62 PRO 181
GLY 150 0.27 ASN 107 -0.70 PRO 181
GLY 1 0.23 THR 108 -0.57 PRO 181
GLY 1 0.28 PRO 109 -0.59 PRO 181
GLY 1 0.21 ILE 110 -0.58 PRO 181
GLY 1 0.21 ILE 111 -0.50 PRO 181
GLY 1 0.18 LEU 112 -0.52 PRO 181
GLY 1 0.15 VAL 113 -0.39 PRO 181
GLY 1 0.13 GLY 114 -0.37 PRO 181
LEU 160 0.09 THR 115 -0.29 PRO 181
ASP 47 0.10 LYS 116 -0.36 TYR 32
ASP 47 0.18 LEU 117 -0.31 TYR 32
ASP 47 0.18 ASP 118 -0.37 TYR 32
ASP 47 0.14 LEU 119 -0.59 TYR 32
ASP 47 0.20 ARG 120 -0.44 TYR 32
ASP 47 0.28 ASP 121 -0.45 TYR 32
ASP 47 0.21 ASP 122 -0.64 TYR 32
ASP 47 0.26 LYS 123 -0.67 TYR 32
PRO 140 0.17 ASP 124 -0.90 TYR 32
THR 138 0.12 THR 125 -0.89 TYR 32
TYR 139 0.25 ILE 126 -0.69 TYR 32
PRO 140 0.28 GLU 127 -0.74 TYR 32
PRO 140 0.15 LYS 128 -0.93 ILE 33
THR 138 0.16 LEU 129 -0.72 ILE 33
PRO 140 0.30 LYS 130 -0.65 ILE 33
PRO 140 0.23 GLU 131 -0.78 ILE 33
PRO 140 0.13 LYS 132 -0.76 GLN 61
PRO 140 0.24 LYS 133 -0.55 ILE 33
PRO 140 0.17 LEU 134 -0.47 ILE 33
THR 138 0.25 THR 135 -0.42 ILE 33
TYR 139 0.16 PRO 136 -0.36 ILE 33
THR 135 0.16 ILE 137 -0.39 PRO 181
LYS 130 0.29 THR 138 -0.38 PRO 181
LYS 130 0.27 TYR 139 -0.41 PRO 181
LYS 130 0.30 PRO 140 -0.50 PRO 181
LYS 130 0.23 GLN 141 -0.52 PRO 181
GLY 1 0.19 GLY 142 -0.53 PRO 181
GLY 1 0.24 LEU 143 -0.60 PRO 181
GLY 1 0.21 ALA 144 -0.70 PRO 181
GLY 1 0.18 MET 145 -0.69 PRO 181
GLY 1 0.21 ALA 146 -0.71 PRO 181
GLY 1 0.22 LYS 147 -0.87 PRO 181
GLY 1 0.19 GLU 148 -0.88 PRO 181
GLY 1 0.19 ILE 149 -0.83 PRO 181
ASN 107 0.27 GLY 150 -0.93 PRO 181
GLY 1 0.24 ALA 151 -0.76 PRO 181
GLY 1 0.29 VAL 152 -0.74 PRO 181
GLY 1 0.27 LYS 153 -0.60 PRO 181
GLY 1 0.24 TYR 154 -0.52 PRO 181
GLY 1 0.20 LEU 155 -0.38 PRO 181
GLY 1 0.18 GLU 156 -0.30 PRO 181
ASP 47 0.16 CYS 157 -0.21 PRO 181
PRO 180 0.15 SER 158 -0.18 TYR 32
GLY 15 0.16 ALA 159 -0.22 LYS 128
GLY 15 0.19 LEU 160 -0.23 ASP 124
PRO 180 0.20 THR 161 -0.10 TYR 32
PRO 180 0.21 GLN 162 -0.07 LYS 128
PRO 180 0.24 ARG 163 -0.11 TYR 139
ASP 121 0.25 GLY 164 -0.14 PRO 181
PRO 180 0.20 LEU 165 -0.10 PRO 181
PRO 180 0.26 LYS 166 -0.07 THR 167
ASP 121 0.24 THR 167 -0.12 PRO 181
GLY 1 0.17 VAL 168 -0.21 PRO 181
PRO 180 0.16 PHE 169 -0.11 LYS 128
PRO 180 0.24 ASP 170 -0.06 VAL 152
GLY 1 0.26 GLU 171 -0.24 PRO 181
GLY 1 0.24 ALA 172 -0.24 PRO 181
GLY 1 0.29 ILE 173 -0.11 LYS 132
GLY 1 0.36 ARG 174 -0.17 PRO 181
GLY 1 0.36 ALA 175 -0.39 PRO 181
GLY 1 0.41 VAL 176 -0.29 PRO 179
GLY 1 0.55 LEU 177 -0.29 THR 108
GLY 1 0.66 CYS 178 -0.41 ASN 107
GLY 1 0.61 PRO 179 -0.45 ASN 107
GLY 48 0.80 PRO 180 -0.49 ASN 107
GLY 1 1.00 PRO 181 -0.93 GLY 150

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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.