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***  GTP-BINDING 21-JAN-97 1MH1  ***

CA distance fluctuations for 2610071816113154659

---  normal mode 7  ---

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
VAL 176 0.13 GLY 1 -0.82 PRO 180
ALA 175 0.07 SER 2 -0.68 PRO 180
ALA 175 0.07 PRO 1 -0.55 PRO 180
GLY 1 0.11 GLN 2 -0.49 PRO 180
ALA 175 0.08 ALA 3 -0.38 PRO 181
ALA 175 0.06 ILE 4 -0.25 CYS 178
GLY 54 0.03 LYS 5 -0.22 CYS 178
PRO 179 0.07 CYS 6 -0.14 CYS 178
PRO 179 0.09 VAL 7 -0.11 CYS 178
PRO 179 0.14 VAL 8 -0.08 LYS 132
PRO 181 0.16 VAL 9 -0.09 LYS 132
PRO 181 0.26 GLY 10 -0.10 LYS 132
PRO 181 0.28 ASP 11 -0.14 LYS 132
PRO 181 0.23 GLY 12 -0.18 LYS 132
PRO 181 0.27 ALA 13 -0.18 LYS 128
PRO 181 0.33 VAL 14 -0.14 LYS 128
PRO 181 0.27 GLY 15 -0.13 LYS 128
PRO 181 0.19 LYS 16 -0.12 LYS 128
PRO 179 0.11 THR 17 -0.13 LYS 128
PRO 181 0.17 CYS 18 -0.13 LYS 128
PRO 181 0.20 LEU 19 -0.09 LYS 128
PRO 179 0.11 LEU 20 -0.10 LYS 128
PRO 179 0.08 ILE 21 -0.11 LYS 128
PRO 181 0.14 SER 22 -0.09 LYS 128
PRO 179 0.12 TYR 23 -0.07 ASN 43
PRO 179 0.05 THR 24 -0.11 ASN 43
PRO 179 0.04 THR 25 -0.12 ASN 43
PRO 181 0.09 ASN 26 -0.09 ASN 43
PRO 181 0.11 ALA 27 -0.09 ASP 124
PRO 181 0.17 PHE 28 -0.12 ASP 124
PRO 181 0.11 PRO 29 -0.14 LYS 128
PRO 181 0.12 GLY 30 -0.17 ASP 124
PRO 181 0.16 GLU 31 -0.21 LYS 128
PRO 181 0.17 TYR 32 -0.22 LYS 128
PRO 181 0.11 ILE 33 -0.21 LYS 128
PRO 181 0.10 PRO 34 -0.19 LYS 128
PRO 179 0.07 THR 35 -0.16 LYS 128
PRO 179 0.05 VAL 36 -0.14 LYS 132
PRO 179 0.04 PHE 37 -0.12 LYS 132
PRO 179 0.03 ASP 38 -0.12 LYS 128
ASP 170 0.03 ASN 39 -0.17 PRO 181
ASP 170 0.04 TYR 40 -0.15 PRO 181
ASP 170 0.04 SER 41 -0.19 PRO 181
ARG 174 0.05 ALA 42 -0.16 PRO 181
ARG 174 0.05 ASN 43 -0.25 PRO 180
ARG 174 0.05 VAL 44 -0.19 PRO 180
ASP 47 0.05 MET 45 -0.21 PRO 180
GLY 164 0.08 VAL 46 -0.07 PRO 180
THR 167 0.15 ASP 47 -0.13 LEU 177
TYR 139 0.09 GLY 48 -0.33 PRO 180
ARG 174 0.10 LYS 49 -0.42 PRO 180
ARG 174 0.08 PRO 50 -0.42 PRO 180
ALA 175 0.07 VAL 51 -0.34 PRO 180
ALA 175 0.06 ASN 52 -0.32 PRO 180
ALA 175 0.04 LEU 53 -0.19 PRO 181
LYS 5 0.03 GLY 54 -0.21 PRO 181
PRO 179 0.04 LEU 55 -0.12 CYS 178
PRO 179 0.04 TRP 56 -0.12 CYS 178
PRO 179 0.08 ASP 57 -0.11 LYS 128
PRO 179 0.08 THR 58 -0.12 LYS 132
PRO 179 0.09 ALA 59 -0.14 LYS 132
PRO 181 0.16 GLY 60 -0.15 LYS 132
PRO 181 0.15 GLN 61 -0.18 LYS 132
PRO 181 0.14 GLU 62 -0.16 LYS 132
PRO 179 0.08 ASP 63 -0.16 LYS 132
PRO 179 0.07 TYR 64 -0.14 LYS 132
PRO 179 0.08 ASP 65 -0.13 LYS 132
PRO 179 0.05 ARG 66 -0.12 LYS 132
PRO 179 0.03 LEU 67 -0.11 LYS 132
PRO 179 0.05 ARG 68 -0.11 LYS 132
PRO 179 0.03 PRO 69 -0.12 CYS 178
ASP 38 0.02 LEU 70 -0.18 PRO 181
ASP 38 0.02 SER 71 -0.15 PRO 181
ASP 38 0.02 TYR 72 -0.16 CYS 178
GLY 150 0.02 PRO 73 -0.24 PRO 181
GLY 1 0.03 GLN 74 -0.29 PRO 181
GLY 1 0.04 THR 75 -0.22 CYS 178
GLY 1 0.08 ASP 76 -0.24 CYS 178
PRO 179 0.15 VAL 77 -0.11 CYS 178
PRO 179 0.18 SER 78 -0.06 CYS 178
PRO 179 0.23 LEU 79 -0.05 LYS 132
PRO 181 0.29 ILE 80 -0.05 LYS 132
PRO 181 0.34 CYS 81 -0.06 LYS 132
PRO 181 0.43 PHE 82 -0.07 LYS 132
PRO 181 0.47 SER 83 -0.07 LYS 128
PRO 181 0.59 LEU 84 -0.06 TYR 32
PRO 181 0.58 VAL 85 -0.10 TYR 32
PRO 181 0.53 SER 86 -0.10 LYS 132
PRO 181 0.59 PRO 87 -0.06 GLN 61
PRO 181 0.50 ALA 88 -0.11 LYS 132
PRO 181 0.44 SER 89 -0.10 LYS 132
PRO 181 0.53 PHE 90 -0.05 LYS 132
PRO 181 0.52 GLU 91 -0.04 LYS 132
PRO 181 0.41 ASN 92 -0.08 LYS 132
PRO 181 0.42 VAL 93 -0.05 LYS 132
PRO 181 0.45 ARG 94 -0.03 LYS 132
PRO 181 0.39 ALA 95 -0.06 LYS 132
PRO 181 0.29 LYS 96 -0.08 LYS 132
PRO 181 0.27 TRP 97 -0.07 LYS 132
PRO 181 0.30 TYR 98 -0.04 LYS 132
PRO 181 0.24 PRO 99 -0.05 LYS 132
PRO 181 0.15 GLU 100 -0.07 LYS 132
PRO 179 0.14 VAL 101 -0.06 CYS 178
PRO 180 0.16 ARG 102 -0.05 CYS 178
PRO 179 0.09 HIS 103 -0.08 CYS 178
PRO 179 0.05 HIS 104 -0.12 CYS 178
PRO 179 0.06 CYS 105 -0.14 CYS 178
GLY 1 0.08 PRO 106 -0.11 CYS 178
GLY 1 0.11 ASN 107 -0.10 CYS 178
PRO 179 0.12 THR 108 -0.12 CYS 178
PRO 179 0.27 PRO 109 -0.04 GLU 171
PRO 179 0.31 ILE 110 -0.03 VAL 168
PRO 180 0.38 ILE 111 -0.03 VAL 168
PRO 181 0.44 LEU 112 -0.02 GLY 150
PRO 181 0.43 VAL 113 -0.02 LYS 128
PRO 181 0.52 GLY 114 -0.03 LEU 19
PRO 181 0.45 THR 115 -0.05 LYS 128
PRO 181 0.47 LYS 116 -0.08 CYS 18
PRO 181 0.57 LEU 117 -0.05 TYR 32
PRO 181 0.55 ASP 118 -0.06 GLU 31
PRO 181 0.57 LEU 119 -0.11 TYR 32
PRO 181 0.68 ARG 120 -0.09 TYR 32
PRO 181 0.70 ASP 121 -0.08 TYR 32
PRO 181 0.64 ASP 122 -0.13 GLU 31
PRO 181 0.70 LYS 123 -0.14 GLU 31
PRO 181 0.63 ASP 124 -0.20 GLU 31
PRO 181 0.60 THR 125 -0.19 TYR 32
PRO 181 0.70 ILE 126 -0.15 TYR 32
PRO 181 0.71 GLU 127 -0.18 TYR 32
PRO 181 0.62 LYS 128 -0.22 TYR 32
PRO 181 0.64 LEU 129 -0.17 TYR 32
PRO 181 0.73 LYS 130 -0.15 TYR 32
PRO 181 0.67 GLU 131 -0.20 ILE 33
PRO 181 0.63 LYS 132 -0.19 ILE 33
PRO 181 0.71 LYS 133 -0.14 ILE 33
PRO 181 0.69 LEU 134 -0.11 ILE 33
PRO 181 0.76 THR 135 -0.10 TYR 32
PRO 181 0.72 PRO 136 -0.08 TYR 32
PRO 181 0.74 ILE 137 -0.05 TYR 32
PRO 181 0.84 THR 138 -0.05 TYR 32
PRO 181 0.85 TYR 139 -0.04 TYR 32
PRO 181 0.95 PRO 140 -0.04 TYR 32
PRO 181 0.84 GLN 141 -0.04 TYR 32
PRO 181 0.73 GLY 142 -0.03 TYR 32
PRO 181 0.78 LEU 143 -0.04 ARG 163
PRO 181 0.81 ALA 144 -0.03 ARG 163
PRO 181 0.66 MET 145 -0.02 ARG 163
PRO 181 0.61 ALA 146 -0.03 GLY 164
PRO 181 0.67 LYS 147 -0.04 GLY 164
PRO 181 0.62 GLU 148 -0.02 GLY 164
PRO 181 0.48 ILE 149 -0.02 GLY 164
PRO 180 0.48 GLY 150 -0.03 GLY 164
PRO 180 0.49 ALA 151 -0.03 VAL 168
PRO 180 0.59 VAL 152 -0.04 VAL 168
PRO 180 0.63 LYS 153 -0.04 VAL 168
PRO 181 0.59 TYR 154 -0.04 GLY 164
PRO 181 0.55 LEU 155 -0.05 GLY 164
PRO 181 0.57 GLU 156 -0.04 CYS 157
PRO 181 0.48 CYS 157 -0.04 GLU 156
PRO 181 0.42 SER 158 -0.04 LYS 128
PRO 181 0.31 ALA 159 -0.07 LYS 128
PRO 181 0.33 LEU 160 -0.08 ASP 124
PRO 181 0.39 THR 161 -0.04 ASN 43
PRO 181 0.34 GLN 162 -0.04 ASN 43
PRO 181 0.46 ARG 163 -0.04 LEU 143
PRO 181 0.46 GLY 164 -0.05 LEU 155
PRO 181 0.32 LEU 165 -0.04 LEU 155
PRO 181 0.25 LYS 166 -0.03 LYS 153
PRO 180 0.35 THR 167 -0.04 VAL 152
PRO 179 0.31 VAL 168 -0.04 LYS 153
PRO 179 0.22 PHE 169 -0.03 PRO 109
PRO 179 0.25 ASP 170 -0.04 PRO 109
PRO 179 0.43 GLU 171 -0.04 PRO 109
PRO 179 0.29 ALA 172 -0.04 PRO 109
PRO 179 0.19 ILE 173 -0.04 CYS 178
PRO 179 0.38 ARG 174 -0.08 ALA 175
PRO 179 0.44 ALA 175 -0.08 ARG 174
PRO 179 0.16 VAL 176 -0.15 CYS 178
LYS 153 0.13 LEU 177 -0.20 CYS 178
LYS 153 0.23 CYS 178 -0.26 GLN 74
LYS 153 0.56 PRO 179 -0.27 GLY 1
PRO 140 0.65 PRO 180 -0.82 GLY 1
PRO 140 0.95 PRO 181 -0.71 GLY 1

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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.