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CA distance fluctuations for 250309234104825728

---  normal mode 21  ---

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
LEU 130 0.88 SER 96 -1.24 ASN 210
LEU 130 1.06 VAL 97 -1.26 ASN 210
ARG 273 1.59 PRO 98 -0.84 GLY 105
ILE 255 1.49 SER 99 -1.24 SER 166
ASN 131 0.75 GLN 100 -1.14 ARG 174
GLU 258 0.62 LYS 101 -1.41 GLN 165
THR 125 0.34 THR 102 -1.22 SER 166
THR 125 0.38 TYR 103 -1.26 SER 166
THR 125 0.36 GLN 104 -1.06 SER 166
ASP 228 0.54 GLY 105 -1.07 SER 166
ASP 228 1.06 SER 106 -0.95 SER 166
ASP 228 1.07 SER 106 -0.94 SER 166
ASP 228 1.09 TYR 107 -0.78 SER 166
ASP 228 0.49 GLY 108 -0.86 SER 166
LEU 114 0.56 PHE 109 -0.82 LEU 257
THR 125 0.62 ARG 110 -0.85 LEU 257
THR 125 0.73 LEU 111 -0.82 LEU 257
THR 125 1.07 GLY 112 -1.21 CYS 229
THR 125 1.50 PHE 113 -1.48 SER 227
GLN 144 1.06 LEU 114 -1.62 TYR 126
PRO 151 0.90 HIS 115 -0.87 SER 227
PRO 151 0.99 SER 116 -0.69 GLY 262
PRO 98 0.88 VAL 122 -0.69 GLY 262
PRO 98 0.92 THR 123 -0.82 GLY 262
PRO 98 1.01 CYS 124 -0.73 GLY 262
PHE 113 1.50 THR 125 -0.68 SER 227
PRO 98 1.03 TYR 126 -1.62 LEU 114
PRO 98 1.10 SER 127 -1.54 SER 227
PRO 98 0.75 PRO 128 -1.67 SER 227
PRO 98 0.86 ALA 129 -1.69 ASP 228
PRO 98 1.21 LEU 130 -1.38 ASP 228
PRO 98 1.10 ASN 131 -1.20 SER 227
PRO 98 1.45 LYS 132 -0.97 SER 227
PRO 98 1.32 MET 133 -0.88 GLU 285
PRO 98 1.28 PHE 134 -0.70 SER 227
PRO 98 1.15 CYS 135 -0.82 GLY 262
PRO 98 1.02 GLN 136 -0.95 GLY 262
PRO 98 0.92 LEU 137 -1.14 GLY 262
PRO 98 0.75 ALA 138 -1.30 GLY 262
GLU 224 0.78 LYS 139 -1.13 GLY 262
GLU 224 0.78 LYS 139 -1.13 GLY 262
GLU 224 0.83 THR 140 -1.03 GLY 262
PRO 98 0.93 CYS 141 -0.86 GLY 262
PRO 151 0.84 PRO 142 -1.08 VAL 157
SER 99 0.85 VAL 143 -1.30 VAL 157
LEU 114 1.06 GLN 144 -1.40 VAL 157
LEU 114 0.75 LEU 145 -1.23 LEU 257
LEU 114 0.90 TRP 146 -1.08 LEU 257
LEU 114 0.75 VAL 147 -0.85 LEU 257
SER 227 0.55 ASP 148 -0.87 PRO 222
SER 227 1.13 SER 149 -0.66 PRO 153
SER 227 1.39 THR 150 -0.78 PRO 153
GLY 226 1.38 PRO 151 -0.57 PRO 98
GLY 226 1.72 PRO 152 -0.82 PRO 98
GLY 226 1.68 PRO 152 -0.73 PRO 98
ASP 228 1.31 PRO 153 -0.67 THR 150
ASN 200 1.19 PRO 153 -0.78 THR 150
SER 106 0.53 GLY 154 -1.15 GLU 204
SER 99 0.48 GLY 154 -0.92 GLU 204
SER 99 0.59 THR 155 -0.88 LEU 145
SER 99 0.67 ARG 156 -1.33 ILE 232
SER 99 0.89 VAL 157 -1.40 GLN 144
SER 99 1.00 ARG 158 -1.08 TYR 234
SER 99 1.37 ALA 159 -1.30 ILE 195
SER 99 1.10 MET 160 -1.61 ILE 195
THR 170 1.10 ALA 161 -1.04 GLU 285
THR 170 1.44 ILE 162 -1.15 ASN 288
PRO 98 0.97 TYR 163 -1.38 ASN 288
PRO 98 1.09 LYS 164 -1.46 ASN 288
ARG 249 1.02 GLN 165 -1.41 LYS 101
ARG 248 0.68 SER 166 -1.35 LYS 101
ARG 248 0.71 GLN 167 -1.15 SER 99
PRO 98 0.49 HIS 168 -1.20 ASN 288
LEU 130 0.58 MET 169 -1.31 LYS 101
ILE 162 1.44 THR 170 -0.79 ASN 288
HIS 214 0.97 GLU 171 -0.99 GLY 244
HIS 214 0.98 GLU 171 -0.99 GLY 244
HIS 193 0.82 VAL 172 -1.07 GLN 100
ILE 195 0.78 VAL 173 -1.32 GLY 245
MET 246 0.60 ARG 174 -1.31 LEU 264
GLU 221 0.47 ARG 175 -1.23 ASN 263
GLU 224 0.43 CYS 176 -1.16 ASN 263
GLU 224 0.46 PRO 177 -1.21 THR 211
GLU 224 0.58 HIS 178 -1.11 ASN 263
GLU 224 0.66 HIS 179 -1.16 ASN 263
GLU 224 0.59 GLU 180 -1.35 ASN 263
GLU 224 0.66 ARG 181 -1.24 ASN 263
GLU 224 0.82 CYS 182 -1.21 SER 261
GLU 224 1.04 SER 185 -1.41 GLY 262
GLU 224 1.41 ASP 186 -1.41 SER 261
GLU 224 1.25 GLY 187 -1.45 SER 261
GLU 221 1.37 LEU 188 -1.80 SER 261
GLU 221 0.93 ALA 189 -1.78 GLY 262
GLU 221 0.62 PRO 190 -1.91 ASN 263
GLU 224 0.73 PRO 191 -1.57 ASN 263
GLU 221 0.49 GLN 192 -1.55 ASN 263
GLU 221 0.50 GLN 192 -1.54 ASN 263
VAL 172 0.82 HIS 193 -1.38 GLY 262
PRO 98 0.63 LEU 194 -1.30 MET 160
VAL 173 0.78 ILE 195 -1.61 MET 160
GLU 221 1.07 ARG 196 -1.45 GLY 262
GLU 221 1.26 VAL 197 -1.31 GLY 262
GLU 221 1.27 GLU 198 -1.24 GLY 262
GLU 224 1.32 GLY 199 -1.04 GLY 262
GLU 221 1.63 ASN 200 -1.03 GLY 262
GLU 221 1.29 LEU 201 -1.04 SER 260
GLU 221 1.23 ARG 202 -1.28 SER 260
GLU 221 1.37 VAL 203 -1.49 SER 260
GLU 221 0.88 GLU 204 -1.68 SER 260
GLU 221 0.87 TYR 205 -1.47 ASN 263
THR 170 0.71 LEU 206 -1.52 LEU 264
THR 170 0.79 ASP 207 -1.62 LEU 264
VAL 217 0.73 ASP 208 -1.40 LEU 264
VAL 217 0.72 ARG 209 -1.13 ASN 263
ARG 158 0.67 ASN 210 -1.26 VAL 97
MET 160 0.60 THR 211 -1.21 PRO 177
THR 170 0.85 PHE 212 -1.41 GLN 192
THR 170 1.22 ARG 213 -1.36 LEU 264
THR 170 1.06 HIS 214 -1.57 LEU 264
THR 170 0.94 SER 215 -1.31 LEU 264
SER 99 1.02 VAL 216 -1.26 GLY 262
SER 99 0.88 VAL 217 -0.98 VAL 197
SER 99 0.84 VAL 218 -1.37 ILE 232
SER 99 0.68 PRO 219 -1.37 ILE 232
SER 99 0.73 TYR 220 -1.50 THR 231
ASN 200 1.61 GLU 221 -0.65 PRO 128
ASN 200 1.63 GLU 221 -0.65 PRO 128
ASN 200 1.15 PRO 222 -0.94 ALA 129
ASP 186 1.08 PRO 223 -1.07 PRO 128
ASP 186 1.41 GLU 224 -0.76 PRO 128
ASP 186 1.23 VAL 225 -1.01 ALA 129
PRO 152 1.72 GLY 226 -1.50 PRO 128
PRO 152 1.61 SER 227 -1.67 PRO 128
PRO 152 1.35 ASP 228 -1.69 ALA 129
PRO 151 1.28 CYS 229 -1.43 PRO 128
PRO 151 0.98 THR 230 -1.38 TYR 220
PRO 151 1.03 THR 231 -1.50 TYR 220
SER 99 0.96 ILE 232 -1.37 PRO 219
PRO 151 0.83 HIS 233 -1.28 VAL 218
GLU 221 0.83 TYR 234 -1.08 GLY 262
GLU 221 0.81 ASN 235 -1.17 GLY 262
PRO 98 0.90 TYR 236 -1.21 MET 160
PRO 98 0.76 MET 237 -1.33 GLY 262
PRO 98 0.88 CYS 238 -1.17 GLY 262
PRO 98 0.89 CYS 238 -1.17 GLY 262
PRO 98 1.01 ASN 239 -1.01 GLY 262
PRO 98 1.18 SER 240 -0.89 ALA 161
PRO 98 0.98 SER 241 -0.84 GLY 262
PRO 98 0.71 CYS 242 -0.95 GLY 262
PRO 98 0.51 MET 243 -0.92 ASN 263
GLU 224 0.32 GLY 244 -1.05 VAL 173
PRO 98 0.39 GLY 245 -1.32 VAL 173
PRO 98 0.74 MET 246 -1.12 ASN 288
PRO 98 0.79 ASN 247 -0.90 ASN 288
PRO 98 1.11 ARG 248 -1.05 THR 284
PRO 98 1.17 ARG 249 -1.41 ASN 288
PRO 98 1.49 PRO 250 -1.61 ASN 288
PRO 98 1.40 ILE 251 -1.39 ASN 288
PRO 98 1.17 LEU 252 -1.30 GLU 285
SER 99 1.31 THR 253 -1.09 GLU 285
SER 99 1.38 ILE 254 -1.00 LEU 289
SER 99 1.49 ILE 255 -0.97 LEU 289
SER 99 0.98 THR 256 -0.87 LEU 289
SER 99 0.79 LEU 257 -1.23 LEU 145
LYS 101 0.62 GLU 258 -1.02 GLU 204
LYS 101 0.50 ASP 259 -1.49 GLU 204
LYS 101 0.39 SER 260 -1.68 GLU 204
SER 106 0.32 SER 261 -1.80 LEU 188
LYS 101 0.27 GLY 262 -1.78 ALA 189
SER 106 0.37 ASN 263 -1.91 PRO 190
LYS 101 0.52 LEU 264 -1.62 ASP 207
SER 106 0.67 LEU 265 -1.00 LEU 206
ASP 228 0.54 GLY 266 -0.98 SER 166
THR 230 0.42 ARG 267 -1.09 MET 169
SER 99 0.86 ASN 268 -1.08 LEU 289
SER 99 0.88 ASN 268 -1.07 LEU 289
SER 99 1.11 SER 269 -1.25 LEU 289
PRO 98 1.12 PHE 270 -1.04 LEU 289
PRO 98 1.52 GLU 271 -1.32 GLU 285
PRO 98 1.52 GLU 271 -1.33 GLU 285
PRO 98 1.56 VAL 272 -1.58 GLU 285
PRO 98 1.59 ARG 273 -1.24 GLU 285
PRO 98 1.29 VAL 274 -0.86 GLY 262
PRO 98 1.13 CYS 275 -0.84 GLY 262
PRO 98 0.97 ALA 276 -0.84 GLY 262
PRO 98 0.96 CYS 277 -0.68 GLY 262
PRO 98 1.08 PRO 278 -0.68 GLY 262
PRO 98 0.97 GLY 279 -0.53 GLY 262
PRO 98 0.81 ARG 280 -0.58 GLY 262
PRO 98 0.83 ASP 281 -1.01 ARG 273
PRO 98 0.99 ARG 282 -0.73 SER 227
PRO 98 0.75 ARG 283 -0.65 VAL 272
PRO 98 0.52 THR 284 -1.16 ARG 249
PRO 128 0.59 GLU 285 -1.58 VAL 272
PRO 128 0.70 GLU 286 -1.19 VAL 272
PRO 128 0.44 GLU 287 -1.31 PRO 250
PRO 128 0.36 ASN 288 -1.61 PRO 250
PRO 128 0.34 LEU 289 -1.42 LYS 164

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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 8th, 2025.