CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402161531523054209

---  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
PRO 190 0.30 SER 96 -0.74 MET 160
SER 261 0.32 VAL 97 -0.87 MET 160
SER 166 0.77 PRO 98 -1.18 MET 160
SER 166 1.14 SER 99 -1.36 THR 256
THR 211 0.36 GLN 100 -0.81 VAL 97
THR 211 0.38 LYS 101 -0.67 ASP 186
ASN 210 0.41 THR 102 -0.76 ASP 186
ASN 210 0.53 TYR 103 -0.73 ASP 186
ASN 210 0.55 GLN 104 -0.80 ASP 186
ASN 210 0.65 GLY 105 -0.73 ASP 186
ASN 210 0.68 SER 106 -0.74 ASP 186
ASN 210 0.69 TYR 107 -0.77 ASP 186
ASN 210 0.58 GLY 108 -0.86 ASP 186
ASN 210 0.59 PHE 109 -0.79 ASP 186
ASN 210 0.49 ARG 110 -0.86 ASP 186
ASN 210 0.46 LEU 111 -0.96 LEU 188
ALA 159 0.43 GLY 112 -1.07 LEU 188
ALA 159 0.47 PHE 113 -1.21 LEU 188
SER 227 0.50 LEU 114 -1.29 LEU 188
GLY 226 0.36 VAL 122 -1.21 LEU 188
TYR 205 0.35 THR 123 -1.27 LEU 188
TYR 205 0.38 CYS 124 -1.32 LEU 188
GLY 226 0.34 THR 125 -1.24 LEU 188
GLY 226 0.30 TYR 126 -1.15 LEU 188
GLY 226 0.26 SER 127 -1.04 SER 185
GLY 226 0.22 PRO 128 -1.09 SER 185
GLY 226 0.20 ALA 129 -1.13 SER 185
SER 99 0.20 LEU 130 -1.00 SER 185
GLY 226 0.17 ASN 131 -0.94 SER 185
GLY 226 0.20 LYS 132 -0.94 LEU 188
GLY 226 0.25 MET 133 -1.08 LEU 188
GLY 226 0.25 MET 133 -1.08 LEU 188
GLY 226 0.27 PHE 134 -1.05 LEU 188
TYR 205 0.34 CYS 135 -1.12 LEU 188
TYR 205 0.35 GLN 136 -1.03 LEU 188
TYR 205 0.35 LEU 137 -1.02 PRO 191
TYR 205 0.39 ALA 138 -1.32 PRO 191
TYR 205 0.43 LYS 139 -1.25 LEU 188
TYR 205 0.52 THR 140 -1.53 LEU 188
TYR 205 0.58 CYS 141 -1.50 LEU 188
TYR 205 0.58 CYS 141 -1.50 LEU 188
TYR 205 0.59 PRO 142 -1.58 LEU 188
ALA 159 0.76 VAL 143 -1.29 LEU 188
ALA 159 0.66 GLN 144 -1.17 LEU 188
ARG 158 0.63 LEU 145 -0.97 LEU 188
ASN 210 0.57 TRP 146 -0.88 LEU 188
ASN 210 0.67 VAL 147 -0.84 ASP 186
TYR 220 0.64 ASP 148 -0.92 ASP 186
TYR 220 0.87 SER 149 -0.82 ASP 186
TYR 220 1.12 THR 150 -0.78 ASP 228
ASN 210 0.89 PRO 151 -1.19 PRO 223
ASN 210 0.95 PRO 152 -0.96 PRO 222
ASN 210 0.97 PRO 153 -1.00 PRO 222
ASN 210 1.07 GLY 154 -0.76 PRO 222
ASN 210 1.02 THR 155 -0.78 SER 99
ASN 210 0.88 ARG 156 -0.96 ALA 189
THR 150 0.68 VAL 157 -1.21 ALA 189
LEU 145 0.63 ARG 158 -1.15 SER 99
VAL 143 0.76 ALA 159 -1.14 ALA 189
VAL 143 0.54 MET 160 -1.18 PRO 98
VAL 143 0.40 ALA 161 -0.83 VAL 97
GLY 262 0.49 ILE 162 -0.62 VAL 97
SER 99 0.48 TYR 163 -0.46 SER 185
SER 99 0.74 LYS 164 -0.59 SER 185
SER 99 0.97 GLN 165 -0.56 SER 185
SER 99 1.14 SER 166 -0.52 ASP 186
SER 99 1.14 SER 166 -0.52 ASP 186
SER 99 0.84 GLN 167 -0.43 ASP 186
SER 99 0.64 HIS 168 -0.37 ASP 186
SER 99 0.62 MET 169 -0.39 ASP 186
PRO 190 0.48 THR 170 -0.36 ALA 161
GLN 192 0.57 GLU 171 -0.48 THR 211
GLY 262 0.64 VAL 172 -0.26 THR 211
GLY 262 0.49 VAL 173 -0.25 SER 185
GLY 262 0.42 ARG 174 -0.39 PHE 212
GLY 262 0.33 ARG 175 -0.29 LEU 201
GLY 262 0.31 CYS 176 -0.34 PHE 212
GLY 245 0.27 PRO 177 -0.46 PHE 212
ALA 189 0.45 HIS 178 -0.28 PHE 212
ALA 189 0.63 HIS 179 -0.36 CYS 242
ALA 189 0.37 GLU 180 -0.51 MET 237
ALA 189 0.49 ARG 181 -0.55 LEU 201
ARG 181 0.10 SER 185 -1.13 ALA 129
ARG 181 0.13 ASP 186 -1.05 ALA 129
ARG 209 0.31 GLY 187 -1.08 VAL 122
ARG 209 0.48 LEU 188 -1.58 PRO 142
HIS 179 0.63 ALA 189 -1.36 VAL 218
ASP 207 0.86 PRO 190 -0.96 ALA 138
ASP 207 0.48 PRO 191 -1.32 ALA 138
VAL 172 0.57 GLN 192 -0.60 LEU 201
HIS 179 0.50 HIS 193 -0.54 PRO 98
TYR 205 0.41 LEU 194 -0.46 PRO 98
TYR 205 0.73 ILE 195 -0.65 PRO 98
TYR 205 0.89 ARG 196 -0.82 PRO 98
TYR 205 0.88 VAL 197 -1.12 ALA 189
TYR 205 0.56 GLU 198 -0.97 LEU 188
GLY 226 0.36 GLY 199 -0.96 LEU 188
THR 231 0.72 ASN 200 -0.85 ALA 189
GLU 224 0.79 LEU 201 -0.88 PRO 190
THR 230 0.61 ARG 202 -0.85 ALA 189
ILE 232 0.66 VAL 203 -1.07 ALA 189
ILE 232 0.67 GLU 204 -0.72 SER 99
ARG 196 0.89 TYR 205 -0.65 PRO 98
PRO 190 0.57 LEU 206 -0.81 PRO 98
PRO 190 0.86 ASP 207 -0.52 PRO 98
GLY 262 1.17 ASP 208 -0.44 SER 96
SER 261 1.50 ARG 209 -0.36 PRO 177
SER 261 1.84 ASN 210 -0.39 PRO 177
GLY 262 1.54 THR 211 -0.48 GLU 171
GLY 262 1.12 PHE 212 -0.46 PRO 177
GLY 262 0.83 ARG 213 -0.45 SER 96
GLY 262 0.56 HIS 214 -0.64 PRO 98
ILE 232 0.54 SER 215 -0.95 PRO 98
ILE 232 0.80 VAL 216 -1.19 ALA 189
ILE 232 0.78 VAL 217 -1.26 ALA 189
THR 230 0.70 VAL 218 -1.36 ALA 189
THR 150 0.80 PRO 219 -1.08 ALA 189
THR 150 1.12 TYR 220 -1.06 ALA 189
SER 149 0.66 GLU 221 -0.88 LEU 188
LEU 201 0.51 PRO 222 -1.14 PRO 151
LEU 201 0.67 PRO 223 -1.19 PRO 151
LEU 201 0.79 GLU 224 -0.91 LEU 188
LEU 201 0.65 VAL 225 -0.86 PRO 151
LEU 201 0.65 GLY 226 -0.84 PRO 151
LEU 201 0.65 SER 227 -0.94 PRO 151
LEU 201 0.54 ASP 228 -1.07 PRO 151
LEU 201 0.55 CYS 229 -1.03 PRO 151
VAL 218 0.70 THR 230 -1.05 LEU 188
ASN 200 0.72 THR 231 -1.28 LEU 188
VAL 216 0.80 ILE 232 -1.25 LEU 188
TYR 205 0.69 HIS 233 -1.40 LEU 188
TYR 205 0.84 TYR 234 -1.13 LEU 188
TYR 205 0.68 ASN 235 -1.02 LEU 188
TYR 205 0.53 TYR 236 -0.80 PRO 191
TYR 205 0.36 MET 237 -1.01 PRO 191
TYR 205 0.27 CYS 238 -0.65 PRO 191
TYR 205 0.27 CYS 238 -0.64 PRO 191
GLY 262 0.26 ASN 239 -0.59 LEU 188
GLY 262 0.28 SER 240 -0.56 LEU 188
GLY 262 0.26 SER 241 -0.47 GLY 187
GLY 262 0.27 CYS 242 -0.36 HIS 179
GLY 262 0.32 MET 243 -0.35 SER 185
SER 99 0.37 GLY 244 -0.41 SER 185
SER 99 0.37 GLY 245 -0.35 SER 185
SER 99 0.42 MET 246 -0.42 SER 185
SER 99 0.50 ASN 247 -0.53 SER 185
SER 99 0.42 ARG 248 -0.54 SER 185
SER 99 0.50 ARG 249 -0.52 SER 185
SER 99 0.44 PRO 250 -0.60 SER 185
GLY 262 0.32 ILE 251 -0.55 LEU 188
GLY 262 0.31 LEU 252 -0.63 LEU 188
VAL 143 0.34 THR 253 -0.79 ALA 189
THR 211 0.39 ILE 254 -0.81 ALA 189
THR 211 0.39 ILE 254 -0.81 ALA 189
GLN 144 0.52 ILE 255 -0.97 ALA 189
ASN 210 0.67 THR 256 -1.36 SER 99
ASN 210 0.66 THR 256 -1.35 SER 99
ASN 210 0.82 LEU 257 -1.10 SER 99
ASN 210 1.08 GLU 258 -1.08 SER 99
ASN 210 1.30 ASP 259 -0.77 SER 99
ASN 210 1.44 SER 260 -0.65 SER 99
ASN 210 1.84 SER 261 -0.52 SER 99
ASN 210 1.57 GLY 262 -0.70 SER 99
ASN 210 1.41 ASN 263 -0.68 SER 99
ASN 210 1.04 LEU 264 -1.01 SER 99
ASN 210 0.92 LEU 265 -0.88 SER 99
ASN 210 0.73 GLY 266 -0.88 SER 99
ASN 210 0.59 ARG 267 -0.88 SER 99
ASN 210 0.44 ASN 268 -0.74 ALA 189
ASN 210 0.31 SER 269 -0.72 LEU 188
ASN 210 0.22 PHE 270 -0.87 LEU 188
GLY 262 0.20 GLU 271 -0.81 LEU 188
GLY 262 0.21 VAL 272 -0.88 LEU 188
GLY 262 0.21 VAL 272 -0.88 LEU 188
GLY 262 0.22 ARG 273 -0.83 LEU 188
TYR 205 0.32 VAL 274 -0.81 LEU 188
TYR 205 0.26 CYS 275 -0.81 LEU 188
TYR 205 0.26 ALA 276 -0.83 LEU 188
GLY 226 0.27 CYS 277 -0.91 GLY 187
GLY 226 0.27 CYS 277 -0.91 GLY 187
GLY 226 0.28 PRO 278 -1.01 LEU 188
GLY 226 0.29 GLY 279 -1.07 GLY 187
GLY 226 0.26 ARG 280 -1.04 GLY 187
GLY 226 0.24 ASP 281 -0.92 GLY 187
GLY 226 0.25 ARG 282 -0.98 GLY 187
GLY 226 0.24 ARG 283 -1.07 GLY 187
SER 99 0.22 THR 284 -0.98 SER 185
SER 99 0.27 GLU 285 -0.96 SER 185
GLY 226 0.21 GLU 286 -1.08 SER 185
SER 99 0.23 GLU 287 -1.11 SER 185

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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.