CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402180056543250205

---  normal mode 13  ---

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 190 1.11 VAL 97 -0.69 LEU 130
VAL 172 0.69 PRO 98 -1.23 THR 170
SER 166 1.03 SER 99 -1.59 THR 155
LYS 164 1.00 GLN 100 -0.59 THR 170
GLN 165 0.95 LYS 101 -0.67 VAL 97
GLN 165 0.79 THR 102 -0.69 LEU 188
ASN 210 0.67 TYR 103 -0.80 LEU 188
ALA 129 0.73 GLN 104 -0.86 LEU 188
ASN 210 0.75 GLY 105 -0.94 LEU 188
ASN 210 0.77 SER 106 -1.02 LEU 188
ASN 210 0.77 SER 106 -1.02 LEU 188
ALA 129 0.85 TYR 107 -1.19 SER 99
ALA 129 1.00 GLY 108 -0.89 LEU 188
PRO 128 0.87 PHE 109 -0.94 SER 99
ASN 131 0.96 ARG 110 -0.70 LEU 188
PHE 270 1.10 LEU 111 -0.55 LEU 188
PRO 128 1.01 GLY 112 -0.50 SER 99
ASN 200 1.23 PHE 113 -0.55 SER 99
ASN 200 1.35 LEU 114 -0.52 SER 99
ASN 200 1.03 HIS 115 -0.43 SER 99
TYR 205 0.83 SER 116 -0.55 PRO 151
TYR 205 0.67 VAL 122 -0.45 VAL 225
TYR 205 0.70 THR 123 -0.59 GLU 224
TYR 205 0.76 CYS 124 -0.47 PRO 151
CYS 229 0.88 THR 125 -0.29 PRO 151
CYS 229 0.88 THR 125 -0.29 PRO 151
CYS 229 1.19 TYR 126 -0.35 VAL 97
CYS 229 1.48 SER 127 -0.50 VAL 97
CYS 229 1.82 PRO 128 -0.58 VAL 97
ASP 228 1.82 ALA 129 -0.67 VAL 97
ASP 228 1.56 LEU 130 -0.74 LYS 164
CYS 229 1.25 ASN 131 -0.65 VAL 97
ASP 228 1.24 ASN 131 -0.65 VAL 97
ASP 228 1.02 LYS 132 -0.45 VAL 97
CYS 229 0.86 MET 133 -0.29 THR 170
ASP 228 0.73 PHE 134 -0.30 PRO 151
TYR 205 0.61 CYS 135 -0.49 GLU 224
TYR 205 0.55 GLN 136 -0.71 GLU 224
TYR 205 0.48 LEU 137 -0.87 GLU 224
TYR 205 0.60 ALA 138 -1.06 GLU 224
TYR 205 0.78 LYS 139 -0.96 GLU 224
TYR 205 0.78 LYS 139 -0.96 GLU 224
TYR 205 1.05 THR 140 -0.84 PRO 151
TYR 205 1.04 CYS 141 -0.69 PRO 151
TYR 205 1.04 CYS 141 -0.69 PRO 151
TYR 205 1.12 PRO 142 -0.71 PRO 151
VAL 216 1.05 VAL 143 -0.72 SER 99
ALA 159 1.29 GLN 144 -0.59 SER 99
ALA 159 1.12 LEU 145 -0.78 SER 99
VAL 218 1.04 TRP 146 -0.63 LEU 188
TYR 220 1.18 VAL 147 -0.79 SER 99
PRO 222 1.48 ASP 148 -0.80 SER 99
PRO 222 1.14 SER 149 -1.04 LEU 188
ASN 210 1.04 THR 150 -1.64 CYS 229
ASN 210 1.03 PRO 151 -1.55 LEU 188
ASN 210 1.17 PRO 152 -1.54 LEU 188
ASN 210 1.17 PRO 152 -1.58 LEU 188
ASN 210 1.21 PRO 153 -1.53 LEU 188
ASN 210 1.10 PRO 153 -1.61 GLY 187
ASN 210 1.33 GLY 154 -1.46 LEU 188
ASN 210 1.28 GLY 154 -1.49 LEU 188
ASN 210 1.24 THR 155 -1.61 LEU 188
ASN 210 1.24 ARG 156 -1.48 SER 99
ASN 210 1.03 VAL 157 -1.41 VAL 197
THR 211 1.03 ARG 158 -1.05 ALA 189
GLN 144 1.29 ALA 159 -0.78 SER 99
GLN 144 0.99 MET 160 -0.88 THR 170
GLN 144 0.78 ALA 161 -0.64 THR 170
GLN 144 0.59 ILE 162 -0.58 THR 170
GLN 100 0.63 TYR 163 -0.70 GLU 285
GLN 100 1.00 LYS 164 -0.74 LEU 130
LYS 101 0.95 GLN 165 -0.88 GLU 285
SER 99 1.03 SER 166 -0.81 GLU 286
SER 99 0.90 GLN 167 -0.73 THR 211
SER 99 0.90 GLN 167 -0.73 THR 211
MET 246 0.97 HIS 168 -0.88 ARG 213
GLY 244 0.67 MET 169 -0.61 GLU 286
GLY 244 0.96 THR 170 -1.23 PRO 98
GLY 245 1.06 GLU 171 -1.36 ARG 213
VAL 97 0.82 VAL 172 -0.79 GLU 285
VAL 97 0.59 VAL 173 -0.67 GLU 285
GLU 171 0.73 ARG 174 -0.68 LEU 201
GLU 171 0.75 ARG 175 -0.82 LEU 201
GLU 171 0.75 ARG 175 -0.82 LEU 201
GLU 171 0.94 CYS 176 -0.87 LEU 201
GLU 171 0.84 PRO 177 -1.07 LEU 201
GLU 171 0.70 HIS 178 -1.01 LEU 201
VAL 97 0.66 HIS 179 -0.95 GLU 224
VAL 97 0.81 GLU 180 -1.16 LEU 201
VAL 97 0.78 ARG 181 -1.23 LEU 201
GLY 187 0.80 CYS 182 -1.28 GLU 224
GLY 187 0.80 CYS 182 -1.28 GLU 224
CYS 182 0.80 GLY 187 -1.76 PRO 222
VAL 97 0.43 LEU 188 -1.77 TYR 220
VAL 97 0.53 ALA 189 -1.75 VAL 218
VAL 97 1.11 PRO 190 -1.21 ASN 200
VAL 97 0.99 PRO 191 -1.23 GLU 224
VAL 97 0.99 GLN 192 -1.12 VAL 203
VAL 97 0.71 HIS 193 -0.97 VAL 203
VAL 97 0.51 LEU 194 -0.71 GLU 224
HIS 214 0.60 ILE 195 -0.68 GLU 224
LEU 206 1.00 ARG 196 -1.08 VAL 157
TYR 205 1.43 VAL 197 -1.41 VAL 157
TYR 205 1.38 GLU 198 -1.17 PRO 151
TYR 205 0.96 GLY 199 -1.53 TYR 220
LEU 114 1.35 ASN 200 -1.21 PRO 190
THR 230 0.86 LEU 201 -1.23 ARG 181
THR 231 0.98 ARG 202 -1.16 PRO 190
THR 231 1.14 VAL 203 -1.19 PRO 190
ILE 232 1.23 GLU 204 -1.18 SER 261
VAL 197 1.43 TYR 205 -1.11 SER 261
VAL 197 1.05 LEU 206 -0.99 ASN 263
GLN 144 0.73 ASP 207 -0.79 GLU 171
VAL 217 1.06 ASP 208 -0.79 GLU 171
SER 260 1.06 ARG 209 -0.59 GLN 167
SER 260 1.60 ASN 210 -0.55 GLN 167
GLU 258 1.19 THR 211 -0.73 GLN 167
VAL 97 0.88 PHE 212 -0.75 HIS 168
GLN 144 0.73 ARG 213 -1.36 GLU 171
GLN 144 0.85 HIS 214 -0.74 THR 170
GLN 144 0.99 SER 215 -0.84 THR 170
GLN 144 0.98 SER 215 -0.85 THR 170
ILE 232 1.26 VAL 216 -0.87 GLY 262
ASP 208 1.06 VAL 217 -1.25 ALA 189
LEU 145 1.11 VAL 218 -1.75 ALA 189
VAL 147 0.95 PRO 219 -1.61 ALA 189
VAL 147 1.18 TYR 220 -1.77 LEU 188
VAL 147 1.08 GLU 221 -1.60 GLY 187
ASP 148 1.48 PRO 222 -1.76 GLY 187
PRO 128 1.36 PRO 223 -1.50 GLY 187
ALA 129 0.74 GLU 224 -1.32 GLY 187
SER 149 0.61 VAL 225 -1.23 CYS 182
ALA 129 1.16 GLY 226 -1.31 GLY 187
ALA 129 1.48 SER 227 -1.21 GLY 187
ALA 129 1.82 ASP 228 -1.08 GLY 187
PRO 128 1.82 CYS 229 -1.64 THR 150
ASN 200 1.24 THR 230 -1.32 PRO 151
ASN 200 1.25 THR 231 -0.92 PRO 151
VAL 216 1.26 ILE 232 -1.01 SER 99
TYR 205 1.40 HIS 233 -0.96 PRO 151
TYR 205 1.30 TYR 234 -0.88 SER 99
TYR 205 0.96 ASN 235 -0.84 GLU 224
TYR 205 0.60 TYR 236 -0.77 GLU 224
LEU 206 0.45 MET 237 -0.92 GLU 224
GLU 171 0.48 CYS 238 -0.78 GLU 224
GLU 171 0.48 CYS 238 -0.78 GLU 224
HIS 168 0.47 ASN 239 -0.65 GLU 224
HIS 168 0.56 SER 240 -0.71 GLU 285
HIS 168 0.63 SER 241 -0.80 GLU 285
HIS 168 0.69 CYS 242 -0.68 GLU 285
HIS 168 0.80 MET 243 -0.72 GLU 285
THR 170 0.96 GLY 244 -0.76 LEU 201
GLU 171 1.06 GLY 245 -0.67 LEU 201
HIS 168 0.97 MET 246 -0.78 GLU 285
HIS 168 0.94 ASN 247 -0.88 GLU 285
GLN 167 0.71 ARG 248 -1.04 GLU 285
GLN 167 0.82 ARG 249 -0.98 GLU 285
ASP 228 0.58 PRO 250 -0.80 GLU 285
LEU 111 0.62 ILE 251 -0.57 GLU 285
LEU 111 0.75 LEU 252 -0.55 THR 170
LEU 111 0.75 LEU 252 -0.55 THR 170
LEU 111 0.92 THR 253 -0.60 THR 170
LEU 111 0.74 ILE 254 -0.67 THR 170
LEU 111 0.74 ILE 254 -0.67 THR 170
TRP 146 0.92 ILE 255 -1.00 VAL 197
THR 211 1.03 THR 256 -1.05 VAL 197
THR 211 1.03 THR 256 -1.05 VAL 197
ASN 210 1.06 LEU 257 -1.47 SER 99
ASN 210 1.26 GLU 258 -1.53 SER 99
ASN 210 1.26 GLU 258 -1.53 SER 99
ASN 210 1.36 ASP 259 -1.45 SER 99
ASN 210 1.60 SER 260 -1.25 SER 99
ASN 210 1.48 SER 261 -1.18 GLU 204
ASN 210 1.44 GLY 262 -1.17 ALA 189
ASN 210 1.18 ASN 263 -1.06 SER 99
ASN 210 1.04 LEU 264 -1.08 SER 99
ASN 210 0.99 LEU 265 -1.30 SER 99
ASN 210 0.88 GLY 266 -1.10 SER 99
THR 211 0.82 ARG 267 -0.87 LEU 188
THR 211 0.69 ASN 268 -0.78 VAL 197
LEU 111 0.69 SER 269 -0.62 TYR 234
LEU 111 1.10 PHE 270 -0.53 THR 170
ASP 228 0.75 GLU 271 -0.43 THR 170
ASP 228 0.75 GLU 271 -0.43 THR 170
ASP 228 0.64 VAL 272 -0.36 ASN 235
ASP 228 0.61 ARG 273 -0.42 GLU 285
ASP 228 0.46 VAL 274 -0.53 GLU 224
ASP 228 0.48 CYS 275 -0.55 GLU 224
ASP 228 0.42 ALA 276 -0.64 VAL 225
ASP 228 0.55 CYS 277 -0.51 VAL 225
ASP 228 0.68 PRO 278 -0.36 VAL 225
ASP 228 0.80 GLY 279 -0.24 PRO 151
ASP 228 0.83 ARG 280 -0.29 SER 241
ASP 228 0.93 ASP 281 -0.55 SER 241
ASP 228 1.12 ARG 282 -0.47 PRO 250
ASP 228 1.20 ARG 283 -0.55 GLN 165
ASP 228 1.13 THR 284 -0.86 ARG 248
ASP 228 1.22 GLU 285 -1.04 ARG 248
ASP 228 1.40 GLU 286 -0.85 GLN 165

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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.