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CA distance fluctuations for 220926155553133140

---  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 123 0.63 MET 1 -0.24 GLN 142
PRO 123 0.70 GLU 2 -0.25 GLN 142
PRO 123 0.78 LEU 3 -0.21 GLN 142
PRO 123 0.75 ARG 4 -0.20 GLN 142
PRO 123 0.66 HIS 5 -0.20 GLN 142
PRO 123 0.69 THR 6 -0.18 GLN 142
PRO 123 0.66 PRO 7 -0.16 GLN 142
PRO 123 0.70 ALA 8 -0.13 GLN 142
PRO 123 0.66 ARG 9 -0.12 GLN 142
PRO 123 0.66 ASP 10 -0.14 GLN 142
PRO 123 0.74 LEU 11 -0.13 GLN 142
PRO 123 0.72 ASP 12 -0.11 GLN 142
PRO 123 0.67 LYS 13 -0.13 GLN 142
PRO 123 0.73 PHE 14 -0.16 GLN 142
PRO 123 0.77 ILE 15 -0.13 GLN 142
PRO 123 0.70 GLU 16 -0.11 GLN 142
PRO 123 0.67 ASP 17 -0.16 GLN 142
PRO 123 0.74 HIS 18 -0.20 GLN 142
PRO 123 0.81 LEU 19 -0.15 GLN 142
PRO 123 0.75 LEU 20 -0.10 GLN 142
PRO 123 0.70 PRO 21 -0.08 ASP 34
PRO 123 0.61 ASN 22 -0.09 ASP 17
PRO 123 0.53 THR 23 -0.07 LYS 113
PRO 123 0.49 CYS 24 -0.12 HIS 18
PRO 123 0.56 PHE 25 -0.14 HIS 18
PRO 123 0.58 ARG 26 -0.11 ASP 34
PRO 123 0.47 THR 27 -0.10 GLU 2
PRO 123 0.42 GLN 28 -0.18 GLY 71
PRO 123 0.48 VAL 29 -0.18 GLY 71
PRO 123 0.44 LYS 30 -0.13 ASP 34
PRO 123 0.33 GLU 31 -0.15 LYS 220
PRO 123 0.32 ALA 32 -0.18 LYS 220
PRO 123 0.36 ILE 33 -0.17 LYS 220
PRO 123 0.28 ASP 34 -0.15 LYS 220
PRO 123 0.20 ILE 35 -0.17 LYS 220
PRO 123 0.20 VAL 36 -0.18 LYS 220
PRO 123 0.22 CYS 37 -0.16 GLY 223
PRO 123 0.14 ARG 38 -0.15 GLY 223
ARG 125 0.08 PHE 39 -0.17 ARG 124
ARG 125 0.10 LEU 40 -0.17 ARG 124
ARG 125 0.09 LYS 41 -0.17 ARG 124
LYS 113 0.06 GLU 42 -0.21 ARG 124
ARG 53 0.05 ARG 43 -0.27 ARG 124
LEU 84 0.04 CYS 44 -0.31 ARG 124
ASP 89 0.05 PHE 45 -0.36 ARG 124
GLU 111 0.05 GLN 46 -0.36 ARG 124
ASP 89 0.05 GLY 47 -0.44 ARG 124
ASP 89 0.06 THR 48 -0.48 ARG 124
SER 178 0.04 ALA 49 -0.47 ARG 124
SER 178 0.04 ASP 50 -0.44 ARG 124
ARG 43 0.04 PRO 51 -0.36 ARG 124
THR 85 0.05 VAL 52 -0.34 ARG 124
ARG 43 0.05 ARG 53 -0.25 ARG 124
ARG 125 0.10 VAL 54 -0.16 ARG 124
PRO 123 0.16 SER 55 -0.14 GLY 223
PRO 123 0.25 LYS 56 -0.15 GLY 223
PRO 123 0.30 VAL 57 -0.16 GLY 223
PRO 123 0.43 VAL 58 -0.16 GLY 223
PRO 123 0.53 LYS 59 -0.15 GLY 223
PRO 123 0.66 GLY 60 -0.16 GLY 223
PRO 123 0.83 GLY 61 -0.15 GLY 223
PRO 123 0.88 SER 62 -0.11 GLN 216
PRO 123 0.72 SER 63 -0.11 GLY 223
PRO 123 0.67 GLY 64 -0.11 GLY 223
PRO 123 0.77 LYS 65 -0.08 GLY 223
PRO 123 0.75 GLY 66 -0.06 GLY 223
PRO 123 0.87 THR 67 -0.06 ASP 34
PRO 123 0.86 THR 68 -0.09 ILE 33
PRO 123 0.88 LEU 69 -0.14 GLN 142
PRO 123 0.76 ARG 70 -0.17 GLN 142
PRO 123 0.71 GLY 71 -0.26 GLN 142
SER 122 0.84 ARG 72 -0.24 VAL 144
PRO 123 0.84 SER 73 -0.21 GLN 216
PRO 123 0.73 ASP 74 -0.22 LYS 220
PRO 123 0.60 ALA 75 -0.21 GLY 223
PRO 123 0.63 ASP 76 -0.22 GLY 223
PRO 123 0.46 LEU 77 -0.21 GLY 223
PRO 123 0.40 VAL 78 -0.20 GLY 223
ARG 125 0.25 VAL 79 -0.18 GLY 223
PRO 123 0.20 PHE 80 -0.17 ASN 224
ARG 125 0.09 LEU 81 -0.19 GLU 126
THR 85 0.05 THR 82 -0.22 GLU 126
THR 85 0.05 LYS 83 -0.31 GLU 126
GLU 88 0.05 LEU 84 -0.27 GLU 126
LYS 83 0.05 THR 85 -0.23 GLU 126
PRO 123 0.07 SER 86 -0.17 GLU 126
PRO 123 0.14 PHE 87 -0.20 ASN 224
ILE 349 0.06 GLU 88 -0.23 GLU 126
THR 48 0.06 ASP 89 -0.33 GLU 126
ARG 125 0.05 GLN 90 -0.22 GLU 126
ILE 349 0.06 LEU 91 -0.21 ASN 224
ILE 349 0.06 ARG 92 -0.53 GLU 126
LYS 292 0.05 ARG 93 -0.56 GLU 126
ASN 307 0.05 ARG 94 -0.35 GLU 126
ASN 307 0.07 GLY 95 -0.54 GLU 126
ASN 307 0.06 GLU 96 -0.64 GLU 126
ASN 307 0.05 PHE 97 -0.44 ARG 124
PRO 128 0.06 ILE 98 -0.37 ARG 124
ASN 307 0.07 GLN 99 -0.60 ARG 124
ASN 307 0.06 GLU 100 -0.54 ARG 124
PRO 128 0.05 ILE 101 -0.37 ARG 124
ASN 307 0.06 ARG 102 -0.40 ARG 124
ASN 307 0.05 ARG 103 -0.54 ARG 124
ILE 101 0.04 GLN 104 -0.42 ARG 124
VAL 134 0.04 LEU 105 -0.31 ARG 124
VAL 134 0.04 GLU 106 -0.39 ARG 124
GLY 47 0.04 ALA 107 -0.42 ARG 124
GLN 46 0.05 CYS 108 -0.31 ARG 124
GLU 42 0.04 GLN 109 -0.29 ARG 124
GLY 47 0.04 ARG 110 -0.35 ARG 124
GLN 46 0.05 GLU 111 -0.30 ARG 124
GLU 42 0.05 GLN 112 -0.23 ARG 124
GLU 42 0.06 LYS 113 -0.20 ARG 124
GLU 42 0.05 PHE 114 -0.20 LYS 220
PHE 39 0.05 LYS 115 -0.21 LYS 220
ARG 125 0.05 VAL 116 -0.22 LYS 220
ARG 125 0.05 THR 117 -0.24 LYS 220
PHE 25 0.07 PHE 118 -0.21 GLY 223
GLN 121 0.26 GLU 119 -0.18 GLY 95
ARG 72 0.38 VAL 120 -0.32 PRO 128
GLN 229 0.66 GLN 121 -0.33 GLN 99
ASN 224 1.37 SER 122 -0.33 ARG 103
PRO 228 1.57 PRO 123 -0.30 GLU 96
LYS 225 1.13 ARG 124 -0.62 GLU 96
PRO 228 1.00 ARG 125 -0.30 GLU 96
GLY 310 0.80 GLU 126 -0.64 GLU 96
ASN 307 0.19 ASN 127 -0.29 ARG 92
ARG 125 0.16 PRO 128 -0.32 VAL 120
ARG 125 0.42 ARG 129 -0.28 ASN 224
ARG 125 0.45 GLY 130 -0.26 GLY 223
ARG 125 0.25 LEU 131 -0.22 GLY 223
GLN 121 0.41 SER 132 -0.27 GLY 223
GLN 121 0.27 PHE 133 -0.27 GLY 223
PRO 123 0.27 VAL 134 -0.29 LYS 220
PRO 123 0.22 LEU 135 -0.25 LYS 220
PRO 123 0.17 SER 136 -0.24 LYS 220
PRO 123 0.14 SER 137 -0.20 LYS 220
PRO 123 0.11 PRO 138 -0.20 GLU 2
PRO 123 0.18 GLN 139 -0.18 GLU 2
PRO 123 0.25 LEU 140 -0.20 GLU 2
PRO 123 0.30 GLN 141 -0.23 MET 1
PRO 123 0.35 GLN 142 -0.26 GLY 71
PRO 123 0.35 GLU 143 -0.26 LYS 220
PRO 123 0.43 VAL 144 -0.25 LYS 220
PRO 123 0.48 GLU 145 -0.29 LYS 220
PRO 123 0.46 PHE 146 -0.25 GLY 223
PRO 123 0.51 ASP 147 -0.27 GLY 223
ARG 125 0.36 VAL 148 -0.23 GLY 223
ARG 125 0.38 LEU 149 -0.23 ASN 224
ARG 125 0.21 PRO 150 -0.20 ASN 224
ARG 125 0.24 ALA 151 -0.20 ASN 224
ARG 125 0.18 PHE 152 -0.18 ASN 224
PRO 123 0.23 ASP 153 -0.17 ASN 224
PRO 123 0.27 ALA 154 -0.16 ASN 224
PRO 123 0.33 LEU 155 -0.14 ASN 224
PRO 123 0.26 GLY 156 -0.14 ASN 224
PRO 123 0.29 GLN 157 -0.12 ASN 224
PRO 123 0.37 TRP 158 -0.11 ASN 224
PRO 123 0.40 THR 159 -0.09 ASN 224
PRO 123 0.48 PRO 160 -0.08 ASN 224
PRO 123 0.50 GLY 161 -0.06 ASN 224
PRO 123 0.45 TYR 162 -0.08 ASN 224
PRO 123 0.46 LYS 163 -0.09 ASN 224
PRO 123 0.41 PRO 164 -0.11 ASN 224
PRO 123 0.33 ASN 165 -0.11 ASN 224
PRO 123 0.35 PRO 166 -0.12 ASN 224
PRO 123 0.27 GLU 167 -0.13 ASN 224
PRO 123 0.29 ILE 168 -0.15 ASN 224
PRO 123 0.36 TYR 169 -0.15 ASN 224
PRO 123 0.28 VAL 170 -0.15 ASN 224
PRO 123 0.21 GLN 171 -0.17 ASN 224
PRO 123 0.29 LEU 172 -0.19 ASN 224
PRO 123 0.31 ILE 173 -0.18 ASN 224
PRO 123 0.18 LYS 174 -0.18 ASN 224
PRO 123 0.14 GLU 175 -0.20 ASN 224
PRO 123 0.24 CYS 176 -0.23 ASN 224
PRO 123 0.20 LYS 177 -0.21 ASN 224
ILE 349 0.08 SER 178 -0.21 ASN 224
ILE 349 0.08 ARG 179 -0.24 ASN 224
GLU 126 0.23 GLY 180 -0.25 ASN 224
GLU 126 0.33 LYS 181 -0.28 ASN 224
ARG 125 0.48 GLU 182 -0.25 ASN 224
ARG 125 0.64 GLY 183 -0.28 ASN 224
ARG 125 0.56 GLU 184 -0.29 ASN 224
ARG 125 0.49 PHE 185 -0.25 ASN 224
ARG 125 0.63 SER 186 -0.24 ASN 224
ARG 125 0.56 THR 187 -0.23 ASN 224
PRO 123 0.41 CYS 188 -0.20 ASN 224
PRO 123 0.53 PHE 189 -0.17 ASN 224
PRO 123 0.62 THR 190 -0.17 ASN 224
PRO 123 0.56 GLU 191 -0.13 ASN 224
PRO 123 0.62 LEU 192 -0.11 ASN 224
PRO 123 0.75 GLN 193 -0.11 ASN 224
PRO 123 0.72 ARG 194 -0.10 GLY 223
PRO 123 0.72 ARG 194 -0.10 GLY 223
PRO 123 0.66 ASP 195 -0.08 GLY 223
PRO 123 0.74 PHE 196 -0.06 GLY 223
PRO 123 0.79 LEU 197 -0.05 GLY 223
PRO 123 0.70 ARG 198 -0.06 GLY 223
PRO 123 0.66 ASN 199 -0.05 GLY 223
PRO 123 0.72 ARG 200 -0.05 ILE 349
PRO 123 0.70 PRO 201 -0.05 ILE 349
PRO 123 0.71 THR 202 -0.04 GLN 142
PRO 123 0.74 LYS 203 -0.06 GLN 142
PRO 123 0.80 LEU 204 -0.05 GLN 142
PRO 123 0.83 LYS 205 -0.05 GLN 142
PRO 123 0.83 SER 206 -0.08 GLN 142
PRO 123 0.88 LEU 207 -0.09 GLN 142
PRO 123 0.97 ILE 208 -0.08 GLN 142
PRO 123 0.95 ARG 209 -0.11 GLN 142
PRO 123 0.94 LEU 210 -0.13 GLN 142
PRO 123 1.05 VAL 211 -0.11 GLN 142
PRO 123 1.14 LYS 212 -0.13 SER 73
PRO 123 1.04 HIS 213 -0.18 SER 73
PRO 123 1.05 TRP 214 -0.16 GLU 143
PRO 123 1.22 TYR 215 -0.16 GLU 145
PRO 123 1.18 GLN 216 -0.23 GLU 145
PRO 123 1.01 THR 217 -0.23 GLU 145
PRO 123 1.07 CYS 218 -0.21 GLU 145
SER 122 1.16 LYS 219 -0.26 GLU 145
SER 122 0.93 LYS 220 -0.29 VAL 134
PRO 123 0.86 THR 221 -0.25 VAL 134
PRO 123 0.99 HIS 222 -0.22 VAL 134
SER 122 1.08 GLY 223 -0.27 VAL 134
SER 122 1.37 ASN 224 -0.29 GLU 184
PRO 123 1.21 LYS 225 -0.25 LYS 181
PRO 123 1.41 LEU 226 -0.21 GLY 183
PRO 123 1.45 PRO 227 -0.19 GLY 183
PRO 123 1.57 PRO 228 -0.21 GLY 183
PRO 123 1.46 GLN 229 -0.12 SER 186
PRO 123 1.26 TYR 230 -0.11 SER 186
PRO 123 1.23 ALA 231 -0.08 SER 186
PRO 123 1.20 LEU 232 -0.07 GLU 143
PRO 123 1.10 GLU 233 -0.05 GLN 142
PRO 123 1.02 LEU 234 -0.04 GLY 223
PRO 123 1.01 LEU 235 -0.05 GLN 142
PRO 123 0.96 THR 236 -0.06 GLN 142
PRO 123 0.89 VAL 237 -0.04 GLN 142
PRO 123 0.86 TYR 238 -0.04 GLN 142
PRO 123 0.85 ALA 239 -0.06 GLN 142
PRO 123 0.80 TRP 240 -0.05 GLN 142
PRO 123 0.75 GLU 241 -0.05 GLN 347
PRO 123 0.73 GLN 242 -0.05 GLN 347
PRO 123 0.73 GLY 243 -0.05 GLN 142
PRO 123 0.70 SER 244 -0.05 GLN 142
PRO 123 0.69 ARG 245 -0.05 GLN 347
PRO 123 0.67 LYS 246 -0.04 GLN 142
PRO 123 0.66 THR 247 -0.04 ASN 22
PRO 123 0.66 ASP 248 -0.06 GLN 142
PRO 123 0.69 PHE 249 -0.07 GLN 142
PRO 123 0.71 SER 250 -0.08 GLN 142
PRO 123 0.77 THR 251 -0.09 GLN 142
PRO 123 0.76 ALA 252 -0.11 GLN 142
PRO 123 0.75 GLN 253 -0.09 GLN 142
PRO 123 0.82 GLY 254 -0.08 GLN 142
PRO 123 0.87 PHE 255 -0.11 GLN 142
PRO 123 0.83 GLN 256 -0.10 GLN 142
PRO 123 0.84 THR 257 -0.08 GLN 142
PRO 123 0.93 VAL 258 -0.09 GLN 142
PRO 123 0.92 LEU 259 -0.10 GLN 142
PRO 123 0.85 GLU 260 -0.09 GLN 142
PRO 123 0.90 LEU 261 -0.08 GLN 142
PRO 123 0.98 VAL 262 -0.09 GLU 143
PRO 123 0.88 LEU 263 -0.09 GLU 143
PRO 123 0.84 LYS 264 -0.07 GLU 143
PRO 123 0.92 HIS 265 -0.06 GLU 143
PRO 123 0.82 GLN 266 -0.05 GLU 143
PRO 123 0.78 LYS 267 -0.05 GLN 142
PRO 123 0.85 LEU 268 -0.04 GLN 142
PRO 123 0.80 CYS 269 -0.03 GLN 142
PRO 123 0.83 ILE 270 -0.03 ASN 224
PRO 123 0.77 PHE 271 -0.05 ASN 224
PRO 123 0.71 TRP 272 -0.05 ASN 224
PRO 123 0.62 GLU 273 -0.06 ASN 224
PRO 123 0.62 ALA 274 -0.06 ASN 224
PRO 123 0.56 TYR 275 -0.09 ASN 224
PRO 123 0.52 TYR 276 -0.09 ASN 224
PRO 123 0.51 ASP 277 -0.08 ASN 224
PRO 123 0.47 PHE 278 -0.08 ASN 224
PRO 123 0.41 THR 279 -0.08 ASN 224
PRO 123 0.36 ASN 280 -0.10 ASN 224
PRO 123 0.34 PRO 281 -0.10 ASN 224
PRO 123 0.33 VAL 282 -0.12 ASN 224
PRO 123 0.41 VAL 283 -0.12 ASN 224
PRO 123 0.45 GLY 284 -0.09 GLY 311
PRO 123 0.42 ARG 285 -0.11 GLY 311
PRO 123 0.46 CYS 286 -0.14 GLY 311
PRO 123 0.56 MET 287 -0.11 GLY 311
PRO 123 0.53 LEU 288 -0.09 GLY 311
PRO 123 0.52 GLN 289 -0.13 GLY 311
PRO 123 0.63 GLN 290 -0.15 GLY 311
PRO 123 0.66 LEU 291 -0.08 GLY 311
PRO 123 0.61 LYS 292 -0.07 GLY 311
PRO 123 0.68 LYS 293 -0.09 GLY 311
PRO 123 0.74 PRO 294 -0.04 THR 313
PRO 123 0.83 ARG 295 -0.04 GLU 143
PRO 123 0.92 PRO 296 -0.04 GLU 143
PRO 123 0.88 VAL 297 -0.04 ASN 224
PRO 123 0.95 ILE 298 -0.05 ASN 224
PRO 123 0.84 LEU 299 -0.08 ASN 224
PRO 123 0.85 ASP 300 -0.11 ASN 224
PRO 123 0.75 PRO 301 -0.09 ASN 224
PRO 123 0.67 ALA 302 -0.13 ASN 224
PRO 123 0.63 ASP 303 -0.16 ASN 224
PRO 123 0.60 PRO 304 -0.14 ASN 224
PRO 123 0.58 THR 305 -0.17 ASN 224
PRO 123 0.75 GLY 306 -0.19 GLY 310
PRO 123 0.89 ASN 307 -0.11 ASN 224
PRO 123 1.08 VAL 308 -0.13 GLY 306
PRO 123 1.10 GLY 309 -0.12 GLY 306
PRO 123 1.12 GLY 310 -0.20 GLY 183
PRO 123 0.95 GLY 311 -0.17 GLU 182
ARG 124 1.03 ASP 312 -0.18 GLY 180
PRO 123 0.93 THR 313 -0.13 GLY 180
ARG 124 0.93 HIS 314 -0.17 GLY 180
PRO 123 1.15 SER 315 -0.18 LYS 181
PRO 123 1.08 TRP 316 -0.12 LYS 181
PRO 123 0.93 GLN 317 -0.12 LYS 181
PRO 123 0.99 ARG 318 -0.15 LYS 181
PRO 123 1.10 LEU 319 -0.13 VAL 134
PRO 123 0.96 ALA 320 -0.11 VAL 134
PRO 123 0.86 GLN 321 -0.13 VAL 134
PRO 123 0.92 GLU 322 -0.15 VAL 134
PRO 123 0.92 ALA 323 -0.13 GLU 143
PRO 123 0.81 ARG 324 -0.13 GLU 143
PRO 123 0.78 VAL 325 -0.15 GLU 143
PRO 123 0.82 TRP 326 -0.15 GLU 143
PRO 123 0.77 LEU 327 -0.13 GLN 142
PRO 123 0.70 GLY 328 -0.14 GLN 142
PRO 123 0.71 TYR 329 -0.16 GLN 142
PRO 123 0.68 PRO 330 -0.16 GLN 142
PRO 123 0.74 CYS 331 -0.15 GLN 142
PRO 123 0.73 CYS 332 -0.13 GLN 142
PRO 123 0.66 LYS 333 -0.13 GLN 142
PRO 123 0.62 ASN 334 -0.12 GLN 142
PRO 123 0.57 LEU 335 -0.13 GLN 142
PRO 123 0.54 ASP 336 -0.12 GLN 142
PRO 123 0.57 GLY 337 -0.13 GLN 142
PRO 123 0.60 SER 338 -0.12 GLN 142
PRO 123 0.66 LEU 339 -0.11 GLN 142
PRO 123 0.67 VAL 340 -0.10 GLN 142
PRO 123 0.69 GLY 341 -0.09 GLN 142
PRO 123 0.74 ALA 342 -0.08 GLN 142
PRO 123 0.73 TRP 343 -0.07 GLN 142
PRO 123 0.69 THR 344 -0.06 GLN 142
PRO 123 0.72 MET 345 -0.05 GLN 142
PRO 123 0.67 LEU 346 -0.04 GLN 142
PRO 123 0.67 GLN 347 -0.05 ARG 245
PRO 123 0.68 LYS 348 -0.04 PRO 201
PRO 123 0.63 ILE 349 -0.05 ARG 200

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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: October 18th, 2018.