CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402180056543250205

---  normal mode 11  ---

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 264 0.50 VAL 97 -1.27 PHE 212
THR 170 0.91 PRO 98 -0.52 THR 230
LEU 257 1.52 SER 99 -0.38 GLN 165
PRO 222 0.59 GLN 100 -0.62 THR 230
PRO 222 0.65 LYS 101 -0.51 THR 230
PRO 222 0.76 THR 102 -0.46 THR 230
PRO 222 0.86 TYR 103 -0.56 THR 230
PRO 222 1.00 GLN 104 -0.48 THR 230
PRO 222 0.97 GLY 105 -0.62 THR 230
PRO 222 0.93 SER 106 -0.59 THR 230
PRO 222 0.93 SER 106 -0.59 THR 230
PRO 222 1.12 TYR 107 -0.61 THR 230
PRO 222 1.05 GLY 108 -0.34 THR 230
PRO 222 1.35 PHE 109 -0.42 THR 230
PRO 222 1.03 ARG 110 -0.50 ALA 129
GLU 221 0.83 LEU 111 -0.70 ASN 131
SER 99 0.45 GLY 112 -0.84 ASN 131
SER 99 0.50 PHE 113 -0.82 ASP 228
SER 99 0.40 LEU 114 -1.07 ASP 228
GLY 187 0.39 HIS 115 -1.43 ASP 228
GLY 187 0.47 SER 116 -1.58 ASP 228
GLY 187 0.45 VAL 122 -1.60 ASP 228
GLY 187 0.53 THR 123 -1.57 GLU 224
GLY 187 0.47 CYS 124 -1.35 ASP 228
GLY 187 0.39 THR 125 -1.35 ASP 228
GLY 187 0.39 THR 125 -1.35 ASP 228
LYS 101 0.41 TYR 126 -1.09 ASP 228
LYS 101 0.43 SER 127 -0.97 ASP 228
LYS 101 0.49 PRO 128 -0.78 ASP 228
LYS 101 0.46 ALA 129 -0.73 ASP 228
LYS 101 0.49 LEU 130 -0.78 SER 227
LYS 101 0.59 ASN 131 -0.84 GLY 112
LYS 101 0.59 ASN 131 -0.84 GLY 112
LYS 101 0.45 LYS 132 -0.87 SER 227
LYS 101 0.36 MET 133 -0.96 SER 227
GLY 187 0.38 PHE 134 -1.17 SER 227
GLY 187 0.46 CYS 135 -1.30 GLU 224
GLY 187 0.52 GLN 136 -1.45 GLU 224
GLY 187 0.55 LEU 137 -1.38 GLU 224
GLY 187 0.70 ALA 138 -1.41 GLU 224
GLY 187 0.70 LYS 139 -1.61 GLU 224
GLY 187 0.70 LYS 139 -1.61 GLU 224
GLY 187 0.66 THR 140 -1.44 GLU 224
GLY 187 0.49 CYS 141 -1.20 GLU 224
GLY 187 0.49 CYS 141 -1.20 GLU 224
GLY 187 0.44 PRO 142 -0.91 GLU 224
GLU 221 0.49 VAL 143 -0.95 ALA 159
GLU 221 0.29 GLN 144 -1.28 ILE 255
GLU 221 0.64 LEU 145 -1.07 THR 256
PRO 222 0.83 TRP 146 -0.65 PRO 128
PRO 223 1.31 VAL 147 -0.59 PRO 128
PRO 223 0.92 ASP 148 -0.33 ALA 129
ASP 228 1.02 SER 149 -0.57 THR 230
ASP 228 1.07 THR 150 -1.16 CYS 229
PRO 222 1.31 PRO 151 -0.54 THR 230
SER 99 0.89 PRO 152 -0.61 THR 230
SER 99 0.90 PRO 152 -0.61 THR 230
SER 99 0.82 PRO 153 -0.63 THR 230
SER 99 0.86 PRO 153 -0.61 THR 230
SER 99 0.84 GLY 154 -0.87 THR 230
SER 99 0.85 GLY 154 -0.85 THR 230
SER 99 1.03 THR 155 -1.13 THR 230
SER 99 0.99 ARG 156 -1.38 THR 230
SER 99 1.13 VAL 157 -1.62 THR 231
SER 99 0.99 ARG 158 -1.64 ILE 232
SER 99 0.82 ALA 159 -1.40 ILE 232
THR 170 0.58 MET 160 -1.00 ILE 232
GLU 221 0.49 ALA 161 -0.74 ILE 232
GLU 221 0.49 ILE 162 -0.68 SER 227
GLU 221 0.41 TYR 163 -0.79 SER 227
GLU 221 0.40 LYS 164 -0.75 SER 227
GLU 221 0.35 GLN 165 -0.79 SER 227
PRO 98 0.51 SER 166 -0.63 SER 227
THR 211 0.50 GLN 167 -0.79 SER 227
THR 211 0.50 GLN 167 -0.79 SER 227
THR 211 0.58 HIS 168 -0.86 ASN 247
PRO 98 0.69 MET 169 -0.62 SER 227
PRO 98 0.91 THR 170 -0.58 GLY 244
THR 211 0.87 GLU 171 -0.77 GLY 244
GLU 221 0.36 VAL 172 -1.19 VAL 97
GLU 221 0.35 VAL 173 -0.86 VAL 97
GLU 221 0.35 ARG 174 -0.97 VAL 97
GLU 221 0.31 ARG 175 -0.98 SER 227
GLU 221 0.31 ARG 175 -0.98 SER 227
GLU 221 0.27 CYS 176 -1.04 SER 227
GLU 221 0.25 PRO 177 -0.99 SER 227
GLU 285 0.21 HIS 178 -1.10 SER 227
GLU 285 0.23 HIS 179 -1.09 SER 227
GLU 221 0.24 GLU 180 -0.93 SER 227
GLU 221 0.19 ARG 181 -0.94 SER 227
ALA 276 0.27 CYS 182 -1.01 SER 227
ALA 276 0.27 CYS 182 -1.01 SER 227
GLY 199 0.79 GLY 187 -0.64 VAL 97
GLY 199 0.64 LEU 188 -0.59 VAL 97
VAL 203 0.40 ALA 189 -0.68 GLU 224
ALA 138 0.29 PRO 190 -0.95 VAL 97
ALA 138 0.32 PRO 191 -0.91 VAL 97
GLU 221 0.33 GLN 192 -1.05 VAL 97
GLU 221 0.38 HIS 193 -0.86 VAL 97
GLU 221 0.39 LEU 194 -0.91 SER 227
GLU 221 0.47 ILE 195 -0.90 GLU 224
SER 99 0.58 ARG 196 -0.90 GLU 224
SER 99 0.76 VAL 197 -0.87 GLU 224
GLY 187 0.74 GLU 198 -1.01 GLU 224
GLY 187 0.79 GLY 199 -0.92 GLU 224
SER 99 0.71 ASN 200 -0.67 GLU 224
SER 99 0.61 LEU 201 -0.52 GLU 224
SER 99 0.64 ARG 202 -0.62 SER 260
SER 99 0.62 VAL 203 -0.68 SER 261
SER 99 0.49 GLU 204 -0.89 SER 261
SER 99 0.40 TYR 205 -0.77 ILE 232
THR 170 0.40 LEU 206 -0.81 ILE 232
THR 170 0.41 ASP 207 -0.80 VAL 97
THR 170 0.59 ASP 208 -0.80 VAL 97
THR 170 0.50 ARG 209 -0.82 VAL 97
GLU 171 0.62 ASN 210 -0.86 VAL 97
GLU 171 0.87 THR 211 -1.12 VAL 97
GLU 171 0.52 PHE 212 -1.27 VAL 97
GLU 171 0.54 ARG 213 -0.99 VAL 97
THR 170 0.39 HIS 214 -0.80 ILE 232
THR 170 0.51 SER 215 -1.02 ILE 232
THR 170 0.52 SER 215 -1.03 ILE 232
SER 99 0.60 VAL 216 -1.14 ILE 232
SER 99 0.75 VAL 217 -1.26 ILE 232
SER 99 0.84 VAL 218 -1.10 THR 231
SER 99 0.89 PRO 219 -0.98 THR 231
SER 99 1.16 TYR 220 -1.02 THR 150
SER 99 1.35 GLU 221 -0.36 THR 150
SER 99 1.39 PRO 222 -0.33 LEU 114
VAL 147 1.31 PRO 223 -0.96 LEU 114
SER 149 0.60 GLU 224 -1.61 LYS 139
THR 150 0.38 VAL 225 -0.95 ALA 276
SER 149 0.30 GLY 226 -0.92 ALA 276
SER 149 0.46 SER 227 -1.68 ALA 276
THR 150 1.07 ASP 228 -1.60 VAL 122
SER 99 0.32 CYS 229 -1.22 VAL 157
GLY 187 0.17 THR 230 -1.63 LEU 257
GLY 187 0.23 THR 231 -1.62 VAL 157
GLY 199 0.45 ILE 232 -1.64 ARG 158
GLY 187 0.54 HIS 233 -0.91 GLU 224
SER 99 0.62 TYR 234 -1.00 GLU 224
GLY 187 0.52 ASN 235 -1.20 GLU 224
GLY 187 0.43 TYR 236 -1.15 GLU 224
GLY 187 0.43 MET 237 -1.13 GLU 224
GLY 187 0.31 CYS 238 -1.20 SER 227
GLY 187 0.31 CYS 238 -1.20 SER 227
GLY 187 0.32 ASN 239 -1.33 SER 227
GLU 285 0.31 SER 240 -1.24 SER 227
GLU 285 0.33 SER 241 -1.30 SER 227
GLU 285 0.26 CYS 242 -1.24 SER 227
GLU 285 0.25 MET 243 -1.15 SER 227
GLU 221 0.26 GLY 244 -1.03 SER 227
GLU 221 0.29 GLY 245 -1.03 SER 227
GLU 221 0.30 MET 246 -1.06 SER 227
GLU 285 0.29 ASN 247 -1.12 SER 227
GLU 285 0.36 ARG 248 -1.16 SER 227
GLU 285 0.31 ARG 249 -1.03 SER 227
GLU 221 0.33 PRO 250 -0.99 SER 227
GLU 221 0.39 ILE 251 -0.89 SER 227
GLU 221 0.47 LEU 252 -0.75 SER 227
GLU 221 0.47 LEU 252 -0.75 SER 227
GLU 221 0.56 THR 253 -0.83 GLN 144
SER 99 0.70 ILE 254 -0.88 GLN 144
SER 99 0.70 ILE 254 -0.88 GLN 144
SER 99 1.13 ILE 255 -1.28 GLN 144
SER 99 1.49 THR 256 -1.40 THR 230
SER 99 1.50 THR 256 -1.40 THR 230
SER 99 1.52 LEU 257 -1.63 THR 230
SER 99 1.17 GLU 258 -1.39 THR 230
SER 99 1.18 GLU 258 -1.39 THR 230
SER 99 0.95 ASP 259 -1.10 THR 230
SER 99 0.75 SER 260 -0.99 THR 230
THR 170 0.64 SER 261 -0.93 THR 230
THR 170 0.78 GLY 262 -1.09 THR 230
THR 170 0.75 ASN 263 -1.00 THR 230
SER 99 1.02 LEU 264 -1.05 THR 230
SER 99 1.24 LEU 265 -1.03 THR 230
SER 99 1.47 GLY 266 -0.99 THR 230
SER 99 1.36 ARG 267 -0.91 THR 230
GLU 221 0.89 ASN 268 -0.65 LEU 145
GLU 221 0.76 SER 269 -0.58 LEU 145
GLN 100 0.53 PHE 270 -0.81 GLN 144
GLN 100 0.45 GLU 271 -0.82 SER 227
GLN 100 0.45 GLU 271 -0.82 SER 227
GLU 221 0.33 VAL 272 -0.98 SER 227
GLU 285 0.31 ARG 273 -1.17 SER 227
GLY 187 0.36 VAL 274 -1.29 SER 227
GLY 187 0.39 CYS 275 -1.48 SER 227
GLY 187 0.43 ALA 276 -1.68 SER 227
GLY 187 0.40 CYS 277 -1.60 SER 227
GLY 187 0.40 PRO 278 -1.40 SER 227
GLY 187 0.36 GLY 279 -1.37 ASP 228
GLY 187 0.34 ARG 280 -1.39 SER 227
GLY 187 0.34 ASP 281 -1.33 SER 227
LYS 101 0.33 ARG 282 -1.18 SER 227
LYS 101 0.31 ARG 283 -1.15 SER 227
ARG 248 0.31 THR 284 -1.16 SER 227
ARG 248 0.36 GLU 285 -1.06 SER 227
LYS 101 0.35 GLU 286 -0.97 SER 227

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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.