CNRS Nantes University US2B US2B
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***  hng  ***

CA distance fluctuations for 24012217345632109

---  normal mode 9  ---

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 134 1.30 GLY 5 -0.10 VAL 102
PRO 134 1.14 ILE 6 -0.14 PRO 101
SER 135 1.12 ARG 7 -0.18 PRO 101
SER 135 1.02 ALA 8 -0.22 PRO 101
SER 135 1.00 ALA 9 -0.28 PRO 101
SER 135 1.01 THR 10 -0.29 PRO 101
LYS 137 0.90 SER 11 -0.34 PRO 101
LYS 137 1.11 GLN 12 -0.38 PRO 101
LYS 137 1.03 GLU 13 -0.40 PRO 101
LYS 137 0.82 ILE 14 -0.43 PRO 101
LYS 137 0.88 ASN 15 -0.47 PRO 101
LYS 137 0.95 GLU 16 -0.53 PRO 101
VAL 126 0.73 LEU 17 -0.56 PRO 101
LYS 137 0.56 THR 18 -0.54 PRO 101
LYS 137 0.57 TYR 19 -0.59 PRO 101
VAL 126 0.64 TYR 20 -0.67 PRO 101
VAL 126 0.57 THR 21 -0.60 PRO 101
VAL 123 0.39 THR 22 -0.59 PRO 101
VAL 123 0.40 LEU 23 -0.67 PRO 101
VAL 123 0.58 SER 24 -0.66 PRO 101
VAL 123 0.50 ALA 25 -0.56 PRO 101
VAL 123 0.40 ASN 26 -0.59 TYR 133
VAL 123 0.52 SER 27 -0.59 PRO 101
VAL 123 0.53 TYR 28 -0.52 TYR 133
VAL 123 0.42 CYS 29 -0.67 TYR 133
LEU 122 0.45 ARG 30 -0.72 GLN 129
LEU 122 0.38 THR 31 -0.88 GLN 129
LEU 122 0.37 VAL 32 -0.78 TYR 133
LEU 122 0.56 ILE 33 -0.67 GLN 129
LEU 122 0.57 PRO 34 -0.76 GLN 129
LEU 122 0.44 GLY 35 -0.94 GLN 129
ARG 160 0.47 ALA 36 -0.94 GLN 129
GLU 162 0.38 THR 37 -1.03 TYR 133
GLU 162 0.33 TRP 38 -0.99 TYR 133
GLU 162 0.30 ASP 39 -1.05 TYR 133
GLU 162 0.25 CYS 40 -0.90 TYR 133
ASP 61 0.23 ILE 41 -0.85 TYR 133
VAL 123 0.23 HIS 42 -0.76 TYR 133
GLU 162 0.27 CYS 43 -0.84 TYR 133
GLU 162 0.25 ASP 44 -0.90 TYR 133
GLU 162 0.25 ALA 45 -0.72 TYR 133
GLU 162 0.30 THR 46 -0.73 TYR 133
GLU 162 0.33 GLU 47 -0.94 TYR 133
GLU 162 0.37 ASP 48 -0.90 TYR 133
GLU 162 0.42 LEU 49 -0.75 TYR 133
GLU 162 0.52 LYS 50 -0.82 TYR 133
GLU 162 0.54 ILE 51 -0.77 TYR 133
GLU 162 0.68 ILE 52 -0.66 GLN 129
ARG 160 0.82 LYS 53 -0.69 GLN 129
LEU 122 0.88 THR 54 -0.59 GLN 129
LEU 122 0.99 TRP 55 -0.49 PRO 101
LEU 122 0.63 SER 56 -0.50 PRO 101
VAL 123 0.38 THR 57 -0.57 PRO 101
ARG 30 0.42 LEU 58 -0.54 THR 125
ARG 30 0.36 ILE 59 -0.45 PRO 101
VAL 123 0.57 TYR 60 -0.50 PRO 101
VAL 123 0.58 ASP 61 -0.51 PRO 101
VAL 123 0.78 THR 62 -0.62 PRO 101
VAL 123 0.74 ASN 63 -0.59 PRO 101
LEU 122 0.92 ALA 64 -0.64 PRO 101
LEU 122 0.64 MET 65 -0.70 PRO 101
ARG 160 0.59 VAL 66 -0.78 PRO 101
GLU 162 0.54 ALA 67 -0.77 PRO 101
GLU 162 0.57 ARG 68 -0.78 PRO 101
GLU 162 0.44 GLY 69 -0.78 PRO 101
GLU 162 0.46 ASP 70 -0.74 PRO 101
GLU 162 0.34 SER 71 -0.72 PRO 101
GLN 12 0.43 GLU 72 -0.81 PRO 101
GLN 12 0.47 LYS 73 -0.84 PRO 101
GLN 12 0.59 THR 74 -0.96 PRO 101
GLU 16 0.56 ILE 75 -0.93 PRO 101
GLU 16 0.62 TYR 76 -1.02 PRO 101
VAL 126 0.56 ILE 77 -1.01 PRO 101
VAL 123 0.62 VAL 78 -0.86 PRO 101
VAL 123 0.95 PHE 79 -0.77 PRO 101
VAL 123 0.83 ARG 80 -0.60 PRO 101
VAL 123 0.82 GLY 81 -0.53 PRO 101
VAL 123 0.70 SER 82 -0.43 PRO 101
VAL 123 0.59 SER 83 -0.39 PRO 101
VAL 123 0.55 SER 84 -0.34 PRO 101
VAL 123 0.59 ILE 85 -0.36 PRO 101
VAL 123 0.51 ARG 86 -0.33 PRO 101
VAL 123 0.48 ASN 87 -0.31 PRO 101
VAL 123 0.54 TRP 88 -0.36 PRO 101
LEU 127 0.55 ILE 89 -0.37 PRO 101
LEU 127 0.49 ALA 90 -0.33 PRO 101
LEU 127 0.48 ASP 91 -0.34 PRO 101
LEU 127 0.57 LEU 92 -0.41 ASP 156
LEU 127 0.68 THR 93 -0.37 GLN 159
LEU 127 0.78 PHE 94 -0.46 GLN 159
LEU 127 0.78 VAL 95 -0.51 GLN 159
LEU 127 0.90 PRO 96 -0.64 GLN 159
LEU 127 0.83 VAL 97 -0.78 GLN 159
LEU 127 0.83 SER 98 -1.12 ASP 156
LEU 127 0.91 TYR 99 -1.38 ASP 156
LEU 127 0.69 PRO 100 -1.56 ASP 156
LYS 131 0.74 PRO 101 -1.51 ALA 154
LYS 131 0.87 VAL 102 -1.78 TYR 158
LYS 131 0.83 SER 103 -1.68 GLN 159
LYS 131 0.87 GLY 104 -1.67 GLN 159
LEU 127 1.11 THR 105 -1.24 GLN 159
LEU 127 1.04 LYS 106 -0.99 GLN 159
LEU 127 1.05 VAL 107 -0.73 ASP 156
LEU 127 0.92 HIS 108 -0.54 ASP 156
LEU 127 0.79 LYS 109 -0.53 ASP 156
VAL 123 0.76 GLY 110 -0.41 ASP 156
VAL 123 0.95 PHE 111 -0.59 PRO 100
VAL 123 0.91 LEU 112 -0.77 PRO 100
VAL 123 0.71 ASP 113 -0.67 PRO 100
VAL 123 0.90 SER 114 -0.67 PRO 100
VAL 123 1.13 TYR 115 -0.87 PRO 101
VAL 123 0.69 GLY 116 -0.91 PRO 100
VAL 123 0.46 GLU 117 -0.71 PRO 100
VAL 123 0.49 VAL 118 -0.81 PRO 101
VAL 123 0.55 GLN 119 -0.96 PRO 101
TRP 55 0.37 ASN 120 -0.84 TYR 136
ARG 160 0.57 GLU 121 -0.62 PRO 101
TRP 55 0.99 LEU 122 -0.88 PRO 101
THR 149 1.46 VAL 123 -1.14 TYR 136
ASP 156 1.72 ALA 124 -0.65 VAL 126
TYR 158 1.64 THR 125 -0.54 LEU 58
ALA 154 1.57 VAL 126 -0.65 ALA 124
ASN 186 1.83 LEU 127 -0.83 SER 135
SER 190 1.46 ASP 128 -0.63 THR 37
THR 191 1.15 GLN 129 -1.02 THR 37
GLY 192 1.43 PHE 130 -0.55 LYS 50
ASN 186 1.08 LYS 131 -0.47 THR 37
SER 190 0.85 GLN 132 -0.75 ASP 39
SER 190 0.93 TYR 133 -1.05 ASP 39
GLY 5 1.30 PRO 134 -0.76 LEU 127
GLY 5 1.18 SER 135 -0.83 LEU 127
GLN 12 1.00 TYR 136 -1.14 VAL 123
GLN 12 1.11 LYS 137 -1.05 PRO 101
GLU 16 0.79 VAL 138 -1.24 PRO 101
GLU 16 0.78 ALA 139 -1.11 PRO 101
VAL 126 1.07 VAL 140 -1.07 PRO 101
VAL 126 0.91 THR 141 -0.86 PRO 101
VAL 123 0.85 GLY 142 -0.76 PRO 101
VAL 123 0.77 HIS 143 -0.61 PRO 101
VAL 123 0.80 SER 144 -0.51 PRO 101
VAL 123 0.94 LEU 145 -0.53 PRO 101
VAL 123 1.01 GLY 146 -0.69 PRO 101
VAL 123 1.01 GLY 147 -0.70 PRO 101
VAL 123 1.14 ALA 148 -0.65 PRO 101
VAL 123 1.46 THR 149 -0.84 PRO 101
VAL 123 1.27 ALA 150 -1.01 PRO 101
VAL 126 1.35 LEU 151 -0.90 PRO 101
VAL 123 1.41 LEU 152 -1.07 TYR 99
VAL 123 1.30 CYS 153 -1.45 PRO 101
VAL 126 1.57 ALA 154 -1.51 PRO 101
ALA 124 1.56 LEU 155 -1.43 VAL 102
ALA 124 1.72 ASP 156 -1.56 PRO 100
THR 125 1.57 LEU 157 -1.46 PRO 101
THR 125 1.64 TYR 158 -1.78 VAL 102
THR 125 1.46 GLN 159 -1.68 SER 103
THR 125 1.37 ARG 160 -1.57 SER 103
THR 125 1.31 GLU 161 -1.54 SER 103
THR 125 1.10 GLU 162 -1.33 SER 103
THR 125 1.04 GLY 163 -1.25 SER 103
THR 125 1.21 LEU 164 -1.29 SER 103
THR 125 1.25 SER 165 -1.21 VAL 102
PHE 130 1.13 SER 166 -0.92 VAL 102
SER 135 1.10 SER 167 -0.85 VAL 102
SER 135 0.76 ASN 168 -0.99 PRO 101
VAL 126 1.08 LEU 169 -1.12 PRO 101
VAL 126 1.18 PHE 170 -0.97 PRO 101
VAL 126 1.34 LEU 171 -0.94 PRO 101
VAL 126 1.03 TYR 172 -0.78 PRO 101
VAL 126 0.99 THR 173 -0.68 PRO 101
VAL 126 0.79 GLN 174 -0.56 PRO 101
LEU 127 0.79 GLY 175 -0.46 PRO 101
LEU 127 0.91 GLN 176 -0.49 PRO 101
LEU 127 0.98 PRO 177 -0.35 PRO 101
LEU 127 1.14 ARG 178 -0.33 GLN 159
LEU 127 1.13 VAL 179 -0.44 GLN 159
LEU 127 1.24 GLY 180 -0.59 GLN 159
LEU 127 1.32 ASN 181 -0.59 GLN 159
LEU 127 1.50 PRO 182 -0.49 GLN 159
LEU 127 1.49 ALA 183 -0.65 GLN 159
LEU 127 1.47 PHE 184 -0.71 GLN 159
LEU 127 1.66 ALA 185 -0.43 GLN 159
LEU 127 1.83 ASN 186 -0.34 GLN 159
LEU 127 1.64 TYR 187 -0.52 GLY 104
LEU 127 1.62 VAL 188 -0.54 GLY 104
LEU 127 1.79 VAL 189 -0.36 GLY 104
LEU 127 1.63 SER 190 -0.49 GLY 104
LEU 127 1.40 THR 191 -0.73 GLY 104
PHE 130 1.43 GLY 192 -0.57 SER 103
VAL 126 1.43 ILE 193 -0.81 VAL 102
VAL 126 1.25 PRO 194 -0.68 VAL 102
VAL 126 1.33 TYR 195 -0.68 VAL 102
VAL 126 1.08 ARG 196 -0.58 PRO 101
LEU 127 1.03 ARG 197 -0.50 PRO 101
LEU 127 0.87 THR 198 -0.46 PRO 101
LEU 127 0.84 VAL 199 -0.39 PRO 101
LEU 127 0.71 ASN 200 -0.36 PRO 101
LEU 127 0.74 GLU 201 -0.28 PRO 101
LEU 127 0.75 ARG 202 -0.24 PRO 101
LEU 127 0.74 ASP 203 -0.30 PRO 101
LEU 127 0.78 ILE 204 -0.25 PRO 101
LEU 127 0.82 VAL 205 -0.31 PRO 101
LEU 127 0.97 PRO 206 -0.31 PRO 101
LEU 127 0.97 HIS 207 -0.22 GLN 159
LEU 127 0.94 LEU 208 -0.26 GLN 159
LEU 127 0.96 PRO 209 -0.31 GLN 159
LEU 127 0.96 PRO 210 -0.29 GLN 159
LEU 127 1.06 ALA 211 -0.31 GLN 159
LEU 127 1.01 ALA 212 -0.33 GLN 159
LEU 127 1.01 PHE 213 -0.39 GLN 159
LEU 127 1.14 GLY 214 -0.43 GLN 159
LEU 127 1.22 PHE 215 -0.44 GLN 159
LEU 127 1.35 LEU 216 -0.38 GLN 159
LEU 127 1.38 HIS 217 -0.31 GLN 159
LEU 127 1.53 ALA 218 -0.29 VAL 102
LEU 127 1.37 GLY 219 -0.42 VAL 102
LEU 127 1.25 SER 220 -0.33 VAL 102
LEU 127 1.11 GLU 221 -0.33 PRO 101
LEU 127 0.95 TYR 222 -0.35 PRO 101
LEU 127 0.88 TRP 223 -0.31 PRO 101
LEU 127 0.74 ILE 224 -0.32 PRO 101
LEU 127 0.74 THR 225 -0.26 PRO 101
LEU 127 0.63 ASP 226 -0.27 PRO 101
LEU 127 0.54 ASN 227 -0.30 PRO 101
LYS 137 0.52 SER 228 -0.27 PRO 101
LYS 137 0.60 PRO 229 -0.26 PRO 101
LYS 137 0.62 GLU 230 -0.29 PRO 101
SER 135 0.71 THR 231 -0.27 PRO 101
SER 135 0.79 VAL 232 -0.28 PRO 101
PHE 130 0.88 GLN 233 -0.24 PRO 101
PHE 130 1.01 VAL 234 -0.24 PRO 101
PHE 130 1.13 CYS 235 -0.20 PRO 101
PHE 130 1.29 THR 236 -0.20 VAL 102
PHE 130 1.40 SER 237 -0.14 VAL 102
LEU 127 1.50 ASP 238 -0.21 VAL 102
LEU 127 1.55 LEU 239 -0.19 GLN 159
LEU 127 1.38 GLU 240 -0.20 GLN 159
LEU 127 1.25 THR 241 -0.15 GLN 159
LEU 127 1.12 SER 242 -0.15 GLN 159
LEU 127 1.06 ASP 243 -0.11 GLN 159
LEU 127 1.00 CYS 244 -0.20 PRO 101
LEU 127 0.96 SER 245 -0.20 PRO 101
LEU 127 1.02 ASN 246 -0.16 GLN 159
LEU 127 0.95 SER 247 -0.13 GLN 159
LEU 127 0.85 ILE 248 -0.13 PRO 101
LEU 127 0.89 VAL 249 -0.16 GLN 159
LEU 127 0.83 PRO 250 -0.17 GLN 159
LEU 127 0.75 PHE 251 -0.14 GLN 159
LEU 127 0.74 THR 252 -0.18 PRO 101
LEU 127 0.65 SER 253 -0.23 PRO 101
LEU 127 0.60 VAL 254 -0.26 PRO 101
LEU 127 0.52 LEU 255 -0.29 PRO 101
LEU 127 0.60 ASP 256 -0.32 PRO 101
LEU 127 0.61 HIS 257 -0.36 PRO 101
VAL 123 0.52 LEU 258 -0.39 PRO 101
VAL 123 0.48 SER 259 -0.40 PRO 101
VAL 126 0.53 TYR 260 -0.45 PRO 101
VAL 126 0.49 PHE 261 -0.44 PRO 101
VAL 126 0.40 GLY 262 -0.41 PRO 101
VAL 123 0.40 ILE 263 -0.46 PRO 101
VAL 123 0.44 ASN 264 -0.43 TYR 133
VAL 123 0.53 THR 265 -0.47 PRO 101
VAL 123 0.56 GLY 266 -0.44 PRO 101
VAL 123 0.48 LEU 267 -0.49 TYR 133
VAL 123 0.42 CYS 268 -0.59 TYR 133

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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).
Last modification: April 25th, 2023.