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CA distance fluctuations for 240415000348227985

---  normal mode 16  ---

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
PHE 270 0.47 VAL 97 -1.42 VAL 172
ILE 254 0.79 PRO 98 -1.15 ASN 288
THR 256 0.78 SER 99 -1.36 ASN 288
PHE 270 0.67 GLN 100 -1.50 ASN 288
PRO 152 0.70 LYS 101 -1.51 ARG 290
PRO 152 0.90 THR 102 -1.51 ARG 290
PRO 152 0.78 TYR 103 -1.39 LEU 289
PRO 152 0.92 GLN 104 -1.35 LEU 289
PRO 152 0.68 GLY 105 -1.24 LEU 289
PRO 153 0.82 SER 106 -1.11 LEU 289
PRO 152 0.86 TYR 107 -1.12 LEU 289
PRO 152 1.01 GLY 108 -1.15 LEU 289
PRO 152 1.08 PHE 109 -1.38 LEU 289
PRO 152 1.26 ARG 110 -1.47 LEU 289
PRO 152 1.34 LEU 111 -1.49 LEU 289
PRO 152 1.59 GLY 112 -1.45 ASN 131
PRO 152 1.31 PHE 113 -1.27 ASN 131
PRO 152 1.18 LEU 114 -0.91 THR 230
PRO 152 1.01 HIS 115 -0.82 ASP 186
PRO 151 1.10 SER 116 -0.84 ASP 186
PRO 151 1.28 SER 121 -0.68 GLY 187
PRO 151 1.08 VAL 122 -0.69 ASP 186
PRO 151 1.06 THR 123 -0.84 ASP 186
PRO 151 0.94 CYS 124 -0.88 ASP 186
PRO 152 0.94 THR 125 -0.78 ASP 186
PRO 152 1.01 TYR 126 -0.89 ASP 228
PRO 152 0.81 SER 127 -1.21 ASP 228
PRO 152 0.60 PRO 128 -1.55 CYS 229
ARG 282 0.53 ALA 129 -1.71 ASP 228
ASP 281 0.84 LEU 130 -1.46 CYS 229
PRO 152 0.47 ASN 131 -1.65 CYS 229
PRO 152 0.70 LYS 132 -1.46 GLU 286
PRO 152 0.78 MET 133 -1.02 GLU 285
PRO 152 0.73 PHE 134 -0.84 ASP 186
PRO 151 0.84 CYS 135 -0.91 ASP 186
PRO 151 0.91 GLN 136 -0.90 ASP 186
PRO 151 0.88 LEU 137 -0.94 GLY 187
PRO 151 0.93 ALA 138 -1.15 ASP 186
PRO 151 1.04 LYS 139 -1.20 ASP 186
PRO 151 1.05 THR 140 -1.27 ASP 186
PRO 152 0.96 CYS 141 -1.16 ASP 186
PRO 152 1.12 PRO 142 -0.96 ASP 186
PRO 152 1.27 VAL 143 -1.13 LEU 289
PRO 152 1.48 GLN 144 -1.33 ALA 159
PRO 152 1.40 LEU 145 -1.32 LEU 289
PRO 152 1.58 TRP 146 -1.31 LEU 289
PRO 152 1.28 VAL 147 -1.36 LEU 257
PRO 152 0.81 ASP 148 -1.32 TYR 220
PRO 152 0.51 SER 149 -1.46 THR 155
ASP 228 0.60 THR 150 -1.18 ASN 210
SER 121 1.28 PRO 151 -0.23 ASN 210
GLY 112 1.59 PRO 152 -0.31 ASN 210
SER 106 0.82 PRO 153 -0.90 ARG 202
ASP 228 0.70 GLY 154 -1.05 GLU 204
LEU 188 0.65 THR 155 -1.46 SER 149
LEU 188 0.62 ARG 156 -1.31 VAL 147
LEU 188 0.72 VAL 157 -1.32 LEU 145
THR 170 0.64 ARG 158 -1.29 GLN 144
PRO 98 0.57 ALA 159 -1.33 GLN 144
THR 170 0.60 MET 160 -1.29 LEU 289
THR 170 0.38 ALA 161 -1.26 LEU 289
THR 211 0.59 ILE 162 -1.45 ASN 288
THR 211 0.73 TYR 163 -1.49 ASN 288
THR 211 0.66 LYS 164 -1.67 ASN 288
THR 211 0.80 GLN 165 -1.60 ASN 288
THR 211 0.94 SER 166 -1.54 ASN 288
THR 211 1.10 GLN 167 -1.32 ASN 288
THR 211 1.25 HIS 168 -1.35 ASN 288
THR 211 1.28 MET 169 -1.50 ASN 288
THR 211 1.52 THR 170 -1.23 ASN 288
THR 211 1.23 GLU 171 -1.23 ASN 288
ARG 249 0.56 VAL 172 -1.42 VAL 97
ARG 249 0.43 VAL 173 -1.10 ASN 288
LEU 201 0.38 ARG 174 -1.00 ASN 288
PRO 151 0.46 ARG 175 -0.91 SER 261
PRO 151 0.46 CYS 176 -0.83 SER 261
LEU 201 0.50 PRO 177 -0.79 SER 261
PRO 151 0.63 HIS 178 -0.82 GLY 187
PRO 151 0.68 HIS 179 -0.95 GLY 187
PRO 151 0.63 GLU 180 -0.92 SER 261
PRO 151 0.75 ARG 181 -0.84 SER 261
PRO 190 0.69 ASP 186 -1.52 ASN 235
GLU 224 1.41 GLY 187 -0.95 HIS 179
ASN 200 1.66 LEU 188 -0.72 SER 261
LEU 201 1.19 ALA 189 -1.15 SER 261
LEU 201 0.94 PRO 190 -1.29 SER 261
LEU 201 0.79 PRO 191 -1.05 SER 261
LEU 201 0.66 GLN 192 -1.09 SER 261
VAL 203 0.59 HIS 193 -1.13 GLY 262
PRO 151 0.51 LEU 194 -1.04 GLY 262
PRO 151 0.55 ILE 195 -1.10 GLY 262
PRO 151 0.65 ARG 196 -1.20 ASP 186
PRO 151 0.68 VAL 197 -1.35 ASP 186
PRO 151 0.85 GLU 198 -1.22 ASP 186
LEU 188 1.34 GLY 199 -0.77 ASP 186
LEU 188 1.66 ASN 200 -0.77 LEU 289
LEU 188 1.24 LEU 201 -0.74 PRO 153
GLY 187 1.03 ARG 202 -0.90 PRO 153
ALA 189 0.93 VAL 203 -0.90 SER 260
THR 170 0.58 GLU 204 -1.23 SER 260
THR 170 0.67 TYR 205 -1.25 GLY 262
THR 170 0.83 LEU 206 -1.54 SER 261
THR 170 1.01 ASP 207 -1.69 SER 261
THR 170 1.40 ASP 208 -1.49 SER 261
THR 170 1.22 ARG 209 -1.30 SER 261
THR 170 1.34 ASN 210 -1.18 THR 150
THR 170 1.52 THR 211 -1.19 ASN 263
THR 170 1.20 PHE 212 -1.26 SER 261
THR 170 1.09 ARG 213 -1.28 ASN 263
THR 170 0.78 HIS 214 -1.56 GLY 262
THR 170 0.75 SER 215 -1.63 GLY 262
THR 170 0.61 VAL 216 -1.30 GLY 262
THR 170 0.62 VAL 217 -1.09 LEU 289
LEU 188 0.85 VAL 218 -1.08 ILE 232
GLY 187 0.85 PRO 219 -1.06 ASP 148
LEU 188 1.15 TYR 220 -1.32 ASP 148
LEU 188 1.25 GLU 221 -0.98 ASP 148
LEU 188 1.09 PRO 222 -1.05 ALA 129
LEU 188 1.13 PRO 223 -1.27 ALA 129
GLY 187 1.41 GLU 224 -0.97 ALA 129
GLY 187 1.34 VAL 225 -0.97 ALA 129
GLY 187 0.79 GLY 226 -1.32 ALA 129
LEU 188 0.78 SER 227 -1.58 ALA 129
PRO 152 0.77 ASP 228 -1.71 ALA 129
PRO 152 0.96 CYS 229 -1.65 ASN 131
LEU 188 0.96 THR 230 -1.23 PRO 128
PRO 152 1.08 THR 231 -1.05 LEU 289
PRO 152 0.95 ILE 232 -1.08 VAL 218
PRO 151 0.88 HIS 233 -1.08 ASP 186
PRO 152 0.79 TYR 234 -1.36 ASP 186
PRO 151 0.82 ASN 235 -1.52 ASP 186
PRO 151 0.72 TYR 236 -1.09 ASP 186
PRO 151 0.73 MET 237 -0.87 GLY 187
PRO 151 0.66 CYS 238 -0.89 GLY 187
PRO 151 0.66 CYS 238 -0.89 GLY 187
PRO 151 0.66 ASN 239 -0.85 GLY 187
PRO 151 0.55 SER 240 -0.83 GLU 285
LEU 130 0.58 SER 241 -0.76 GLY 187
PRO 151 0.52 CYS 242 -0.76 GLY 187
VAL 172 0.40 MET 243 -0.95 ASN 288
VAL 172 0.55 GLY 244 -0.96 THR 284
VAL 172 0.53 GLY 245 -0.88 GLU 287
VAL 172 0.49 MET 246 -0.89 THR 284
THR 211 0.57 ASN 247 -1.12 THR 284
LEU 130 0.49 ARG 248 -1.27 THR 284
THR 211 0.64 ARG 249 -1.31 GLU 287
THR 211 0.52 PRO 250 -1.29 GLU 287
PRO 152 0.46 ILE 251 -1.32 GLU 285
PRO 98 0.61 LEU 252 -1.46 GLU 285
PRO 98 0.61 THR 253 -1.36 LEU 289
PRO 98 0.79 ILE 254 -1.57 LEU 289
PRO 98 0.68 ILE 255 -1.51 LEU 289
SER 99 0.78 THR 256 -1.44 LEU 289
LEU 188 0.61 LEU 257 -1.36 VAL 147
SER 99 0.47 GLU 258 -1.28 VAL 147
PRO 153 0.62 ASP 259 -1.15 THR 150
PRO 222 0.42 SER 260 -1.34 LEU 206
SER 106 0.34 SER 261 -1.69 ASP 207
PRO 153 0.20 GLY 262 -1.63 SER 215
PRO 153 0.40 ASN 263 -1.28 ARG 213
PRO 153 0.40 LEU 264 -1.22 LEU 289
PRO 153 0.68 LEU 265 -1.21 LEU 289
PRO 152 0.66 GLY 266 -1.39 LEU 289
PRO 152 0.72 ARG 267 -1.57 LEU 289
PRO 152 0.90 ASN 268 -1.81 LEU 289
PRO 152 0.83 SER 269 -1.86 LEU 289
GLN 100 0.67 PHE 270 -1.29 GLU 285
PRO 152 0.61 GLU 271 -1.75 GLU 285
PRO 152 0.64 VAL 272 -1.50 GLU 285
PRO 152 0.61 ARG 273 -1.12 GLU 285
PRO 151 0.69 VAL 274 -0.79 ASP 186
PRO 151 0.76 CYS 275 -0.80 GLY 187
PRO 151 0.87 ALA 276 -0.85 GLY 187
PRO 151 0.89 CYS 277 -0.70 GLY 187
PRO 151 0.85 PRO 278 -0.72 ASP 186
PRO 151 0.92 GLY 279 -0.73 ASP 228
PRO 151 0.89 ARG 280 -0.73 ASP 228
LEU 130 0.84 ASP 281 -0.76 ASP 228
LEU 130 0.81 ARG 282 -0.94 ASP 228
PRO 151 0.78 ARG 283 -0.90 ASP 228
PRO 151 0.63 THR 284 -1.28 PRO 250
PRO 151 0.35 GLU 285 -1.75 GLU 271
PRO 151 0.41 GLU 286 -1.46 LYS 132
PRO 151 0.49 GLU 287 -1.47 GLN 165
PRO 151 0.14 ASN 288 -1.67 LYS 164
ASN 288 0.05 LEU 289 -1.86 SER 269
SER 121 0.19 ARG 290 -1.51 LYS 101

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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.