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CA distance fluctuations for 250309233605806127

---  normal mode 22  ---

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
ASN 263 1.04 SER 96 -0.60 LEU 252
ASN 263 1.45 VAL 97 -0.74 LEU 252
ASN 263 1.35 PRO 98 -1.70 LEU 252
LEU 264 0.84 SER 99 -1.61 ILE 254
LEU 264 1.37 GLN 100 -0.93 PHE 270
SER 166 1.17 LYS 101 -0.60 PRO 222
SER 166 0.96 THR 102 -0.74 TYR 126
SER 166 0.81 TYR 103 -0.89 PRO 222
SER 166 0.72 GLN 104 -1.09 PRO 222
ASP 228 0.88 GLY 105 -1.12 PRO 222
THR 155 1.60 SER 106 -0.28 PRO 222
ARG 156 1.64 SER 106 -0.26 PRO 222
VAL 157 1.37 TYR 107 -0.73 PRO 222
ASP 228 0.83 GLY 108 -1.35 PRO 222
LEU 289 0.85 PHE 109 -1.29 PRO 222
LEU 289 0.89 ARG 110 -1.31 GLY 199
LEU 289 1.09 LEU 111 -1.53 TYR 220
ASN 131 1.29 GLY 112 -1.45 GLY 199
ASN 131 1.23 PHE 113 -1.11 TYR 220
GLU 224 1.41 LEU 114 -0.87 TYR 220
GLU 224 1.87 HIS 115 -0.65 ASP 228
GLU 224 1.70 SER 116 -0.73 ASP 228
VAL 225 1.61 VAL 122 -0.69 ASP 228
GLU 224 1.39 THR 123 -0.69 PRO 98
GLU 224 1.54 CYS 124 -0.80 PRO 98
GLU 224 1.46 THR 125 -0.88 PRO 98
GLU 224 1.33 TYR 126 -0.99 PRO 98
GLU 224 1.16 SER 127 -0.88 PRO 98
GLU 224 1.13 PRO 128 -0.92 GLN 100
GLY 112 1.17 ALA 129 -0.67 PRO 98
GLY 112 1.27 LEU 130 -0.73 PRO 98
VAL 143 1.42 ASN 131 -0.92 PRO 98
GLU 224 1.17 LYS 132 -1.08 PRO 98
GLU 224 1.30 MET 133 -1.12 PRO 98
GLU 224 1.27 PHE 134 -0.96 PRO 98
GLU 224 1.28 CYS 135 -0.88 PRO 98
GLY 226 1.19 GLN 136 -0.74 PRO 98
PRO 153 1.04 LEU 137 -0.66 PRO 98
PRO 153 1.22 ALA 138 -0.78 CYS 182
PRO 153 1.19 LYS 139 -0.71 CYS 182
PRO 153 1.19 LYS 139 -0.71 CYS 182
GLU 198 1.38 THR 140 -0.78 CYS 182
GLU 224 1.17 CYS 141 -0.73 TYR 220
PHE 270 1.19 PRO 142 -1.01 GLY 199
PHE 270 1.45 VAL 143 -1.50 GLY 199
ASN 131 1.23 GLN 144 -1.89 GLY 199
ASN 131 1.04 LEU 145 -1.50 GLY 199
ASN 131 0.90 TRP 146 -1.36 THR 155
LEU 289 0.82 VAL 147 -1.52 GLU 221
ASP 228 0.79 ASP 148 -1.70 PRO 223
CYS 229 1.37 SER 149 -1.20 PRO 222
LEU 114 0.92 THR 150 -1.57 ASN 263
SER 116 1.23 PRO 151 -0.82 ASN 263
PRO 222 0.91 PRO 152 -0.74 ASN 263
SER 116 0.98 PRO 152 -0.76 ASN 263
PRO 222 1.59 PRO 153 -1.28 THR 150
ASN 200 1.59 PRO 153 -0.92 THR 150
SER 106 1.35 GLY 154 -1.20 ASN 200
SER 106 1.34 GLY 154 -1.22 TRP 146
SER 106 1.60 THR 155 -1.36 VAL 147
SER 106 1.64 ARG 156 -1.25 ASN 200
TYR 107 1.37 VAL 157 -0.89 LEU 111
TYR 107 1.04 ARG 158 -0.72 SER 99
ILE 232 0.90 ALA 159 -0.95 SER 99
ILE 232 0.80 MET 160 -0.90 SER 99
LEU 289 0.88 ALA 161 -1.23 PRO 98
ASN 288 1.02 ILE 162 -1.08 PRO 98
ASN 288 1.23 TYR 163 -1.03 PRO 98
LEU 289 1.35 LYS 164 -0.93 PRO 98
LEU 289 1.23 GLN 165 -0.84 ARG 249
LYS 101 1.17 SER 166 -0.55 ARG 249
ASN 288 1.00 GLN 167 -0.54 ARG 249
ASN 288 1.19 HIS 168 -0.45 THR 211
ASN 288 1.03 MET 169 -0.33 PRO 98
ASN 288 0.88 THR 170 -0.66 THR 211
ASN 288 1.05 GLU 171 -0.90 THR 211
ASN 288 1.05 GLU 171 -0.90 THR 211
ASN 263 0.94 VAL 172 -0.58 PRO 190
ASN 288 0.88 VAL 173 -0.77 PRO 98
GLY 262 0.91 ARG 174 -0.61 PRO 98
PRO 153 0.82 ARG 175 -0.57 PRO 98
PRO 153 0.74 CYS 176 -0.42 SER 227
ASN 263 0.70 PRO 177 -0.53 SER 227
GLY 226 0.63 HIS 178 -0.68 SER 227
PRO 153 0.70 HIS 179 -0.74 ALA 138
PRO 153 0.72 GLU 180 -0.68 SER 227
PRO 153 0.61 ARG 181 -0.85 SER 227
PRO 153 0.58 CYS 182 -1.01 SER 227
PRO 153 0.91 SER 185 -0.93 ARG 196
PRO 153 1.01 ASP 186 -1.07 GLU 198
PRO 153 1.14 GLY 187 -0.74 SER 227
PRO 153 1.31 LEU 188 -0.68 VAL 203
PRO 153 1.15 ALA 189 -0.70 VAL 216
PRO 153 1.00 PRO 190 -0.67 HIS 214
PRO 153 0.90 PRO 191 -0.57 SER 227
PRO 153 0.87 GLN 192 -0.49 PRO 98
PRO 153 0.87 GLN 192 -0.49 PRO 98
PRO 153 0.96 HIS 193 -0.64 PRO 98
PRO 153 0.94 LEU 194 -0.72 PRO 98
PRO 153 1.03 ILE 195 -0.64 PRO 98
PRO 153 1.25 ARG 196 -0.93 SER 185
PRO 153 1.35 VAL 197 -0.90 SER 185
THR 140 1.38 GLU 198 -1.07 ASP 186
PRO 153 1.19 GLY 199 -1.89 GLN 144
PRO 153 1.59 ASN 200 -1.79 PRO 219
PRO 153 1.52 LEU 201 -1.08 GLY 154
PRO 153 1.43 ARG 202 -0.74 GLY 154
PRO 153 1.42 VAL 203 -0.98 ASP 186
PRO 153 1.19 GLU 204 -0.52 LEU 111
PRO 153 1.16 TYR 205 -0.47 SER 99
HIS 193 0.90 LEU 206 -0.56 SER 99
ARG 174 0.85 ASP 207 -0.41 TYR 205
GLY 262 1.19 ASP 208 -0.52 THR 170
SER 261 1.11 ARG 209 -0.42 GLU 171
SER 261 1.46 ASN 210 -0.61 GLU 171
ASN 263 1.47 THR 211 -0.90 GLU 171
GLY 262 1.12 PHE 212 -0.48 PRO 190
GLY 262 1.14 ARG 213 -0.52 PRO 190
GLY 262 0.92 HIS 214 -0.67 PRO 190
GLY 262 0.84 SER 215 -0.58 SER 99
PRO 153 1.04 VAL 216 -0.70 ALA 189
SER 106 1.07 VAL 217 -0.67 LEU 111
SER 106 1.21 VAL 218 -1.03 ASN 200
SER 106 1.46 PRO 219 -1.79 ASN 200
SER 106 1.34 TYR 220 -1.58 GLY 199
VAL 197 1.20 GLU 221 -1.50 VAL 147
VAL 197 1.18 GLU 221 -1.52 VAL 147
PRO 153 1.59 PRO 222 -1.52 LEU 265
PRO 151 1.15 PRO 223 -1.70 ASP 148
HIS 115 1.87 GLU 224 -0.87 GLY 154
VAL 122 1.61 VAL 225 -0.66 GLY 154
GLY 279 1.72 GLY 226 -0.53 GLY 154
SER 149 0.84 SER 227 -1.01 CYS 182
SER 149 0.96 ASP 228 -0.73 SER 116
SER 149 1.37 CYS 229 -1.21 GLY 199
TYR 107 1.14 THR 230 -1.20 GLY 199
PHE 270 1.04 THR 231 -1.38 GLY 199
ILE 255 1.27 ILE 232 -1.11 GLY 199
PHE 270 0.99 HIS 233 -0.82 CYS 182
PRO 153 1.00 TYR 234 -0.77 CYS 182
PRO 153 1.09 ASN 235 -0.90 CYS 182
PRO 153 0.99 TYR 236 -0.68 PRO 98
PRO 153 1.05 MET 237 -0.66 PRO 98
PRO 153 0.89 CYS 238 -0.81 PRO 98
PRO 153 0.89 CYS 238 -0.81 PRO 98
GLY 226 1.02 ASN 239 -0.73 PRO 98
GLY 226 1.03 SER 240 -0.78 PRO 98
GLY 226 1.08 SER 241 -0.65 PRO 98
GLY 226 0.94 CYS 242 -0.53 PRO 98
GLY 226 0.89 MET 243 -0.39 PRO 98
ASN 288 0.85 GLY 244 -0.27 SER 227
ASN 288 0.90 GLY 245 -0.37 PRO 98
ASN 288 1.09 MET 246 -0.61 PRO 98
ASN 288 1.04 ASN 247 -0.57 PRO 98
THR 284 1.15 GLN 248 -0.73 PRO 98
ASN 288 1.52 ARG 249 -0.87 PRO 98
ASN 288 1.54 PRO 250 -1.09 PRO 98
ASN 288 1.20 ILE 251 -1.46 PRO 98
LEU 289 1.10 LEU 252 -1.70 PRO 98
ILE 232 1.05 THR 253 -1.46 PRO 98
ILE 232 1.07 ILE 254 -1.61 SER 99
ILE 232 1.27 ILE 255 -1.15 SER 99
TYR 107 0.92 THR 256 -0.74 SER 99
TYR 107 1.12 LEU 257 -0.89 ARG 110
SER 106 1.01 GLU 258 -1.05 VAL 147
PRO 98 1.08 ASP 259 -1.50 VAL 147
SER 106 1.05 SER 260 -1.21 VAL 147
ASN 210 1.46 SER 261 -1.36 THR 150
THR 211 1.42 GLY 262 -1.30 THR 150
THR 211 1.47 ASN 263 -1.57 THR 150
GLN 100 1.37 LEU 264 -1.20 THR 150
PRO 98 1.19 LEU 265 -1.52 PRO 222
THR 230 0.74 GLY 266 -0.89 PRO 222
SER 166 0.74 ARG 267 -0.69 PRO 222
ASN 268 1.01 ASN 268 -0.79 TYR 126
ASN 268 1.01 ASN 268 -0.79 TYR 126
LEU 289 0.96 SER 269 -0.88 SER 99
VAL 143 1.45 PHE 270 -1.21 PRO 98
LEU 289 1.11 GLU 271 -1.40 PRO 98
LEU 289 1.11 GLU 271 -1.40 PRO 98
GLU 285 1.11 VAL 272 -1.34 PRO 98
GLU 285 1.19 ARG 273 -1.08 PRO 98
GLY 226 1.14 VAL 274 -0.94 PRO 98
GLY 226 1.25 CYS 275 -0.80 PRO 98
GLY 226 1.29 ALA 276 -0.68 PRO 98
GLY 226 1.46 CYS 277 -0.72 PRO 98
GLY 226 1.50 PRO 278 -0.83 PRO 98
GLY 226 1.72 GLY 279 -0.78 PRO 98
GLY 226 1.51 ARG 280 -0.60 PRO 98
GLY 226 1.40 ASP 281 -0.58 PRO 98
GLY 226 1.48 ARG 282 -0.74 PRO 98
GLY 226 1.38 ARG 283 -0.54 PRO 98
GLY 226 1.22 THR 284 -0.31 PRO 98
PRO 250 1.27 GLU 285 -0.23 PRO 98
GLY 226 1.21 GLU 286 -0.32 PRO 98
ARG 249 1.18 GLU 287 -0.18 ASP 228
PRO 250 1.54 ASN 288 -0.06 ARG 280
PRO 250 1.41 LEU 289 -0.05 GLU 287

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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.