CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404202233161534906

---  normal mode 7  ---

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 128 1.15 SER 96 -0.23 ARG 181
GLY 187 1.04 VAL 97 -0.15 GLN 167
LEU 201 1.22 PRO 98 -0.52 GLN 167
VAL 217 1.62 SER 99 -0.58 SER 166
ASP 208 0.94 GLN 100 -0.16 THR 256
ASP 208 1.30 LYS 101 -0.22 ALA 129
THR 211 1.35 THR 102 -0.18 ALA 129
ASP 208 1.57 TYR 103 -0.13 ALA 129
ASP 208 1.45 GLN 104 -0.13 ALA 129
ASP 208 1.58 GLY 105 -0.11 ALA 129
ASP 208 1.40 SER 106 -0.10 ALA 129
ASP 208 1.28 TYR 107 -0.12 LEU 201
ASP 208 1.25 GLY 108 -0.13 PRO 128
ASP 208 1.24 PHE 109 -0.14 LEU 201
ASP 208 1.07 ARG 110 -0.16 PRO 128
SER 96 0.97 LEU 111 -0.17 PRO 128
SER 96 1.03 GLY 112 -0.18 PRO 128
SER 96 0.98 PHE 113 -0.17 ASN 200
SER 96 0.99 LEU 114 -0.16 ASN 200
SER 96 0.71 VAL 122 -0.21 ASP 207
SER 96 0.62 THR 123 -0.26 ASP 207
SER 96 0.71 CYS 124 -0.20 TYR 205
SER 96 0.83 THR 125 -0.18 TYR 205
SER 96 0.93 TYR 126 -0.17 TYR 205
SER 96 1.01 SER 127 -0.14 TYR 205
SER 96 1.15 PRO 128 -0.19 LYS 101
SER 96 1.14 ALA 129 -0.22 LYS 101
SER 96 0.98 LEU 130 -0.19 LYS 101
SER 96 0.98 ASN 131 -0.19 LYS 101
SER 96 0.84 LYS 132 -0.15 TYR 205
SER 96 0.77 MET 133 -0.19 TYR 205
SER 96 0.77 MET 133 -0.19 TYR 205
SER 96 0.69 PHE 134 -0.18 TYR 205
SER 96 0.60 CYS 135 -0.24 ASP 207
VAL 97 0.59 GLN 136 -0.35 PHE 212
VAL 97 0.64 LEU 137 -0.49 PHE 212
VAL 97 0.74 ALA 138 -0.55 ASP 207
VAL 97 0.73 LYS 139 -0.41 ASP 207
VAL 97 0.73 THR 140 -0.31 TYR 205
SER 99 0.70 CYS 141 -0.26 TYR 205
SER 99 0.70 CYS 141 -0.26 TYR 205
SER 99 0.76 PRO 142 -0.23 TYR 205
SER 99 0.79 VAL 143 -0.21 ASN 200
SER 96 0.87 GLN 144 -0.23 ASN 200
ASP 208 0.87 LEU 145 -0.20 ASN 200
SER 96 0.98 TRP 146 -0.18 LEU 201
ASP 208 1.06 VAL 147 -0.15 LEU 201
ASN 210 1.06 ASP 148 -0.13 PRO 128
ASP 208 1.05 SER 149 -0.11 LEU 201
ASP 208 1.01 THR 150 -0.11 LEU 201
ASP 208 1.09 PRO 151 -0.25 PRO 222
SER 99 0.98 PRO 152 -0.15 GLU 221
SER 99 1.09 PRO 153 -0.14 GLU 221
SER 99 1.28 GLY 154 -0.11 GLU 221
SER 99 1.34 THR 155 -0.09 PRO 128
SER 99 1.61 ARG 156 -0.08 GLN 100
SER 99 1.47 VAL 157 -0.10 PHE 270
SER 99 1.38 ARG 158 -0.07 GLN 100
SER 99 1.04 ALA 159 -0.18 HIS 214
SER 99 0.79 MET 160 -0.16 HIS 214
SER 99 0.48 ALA 161 -0.15 VAL 172
ARG 213 0.62 ILE 162 -0.07 VAL 172
ARG 213 0.50 TYR 163 -0.15 MET 169
THR 211 0.52 LYS 164 -0.22 SER 99
THR 211 0.50 GLN 165 -0.44 SER 99
THR 211 0.63 SER 166 -0.58 SER 99
THR 211 0.63 SER 166 -0.58 SER 99
ARG 213 0.51 GLN 167 -0.52 PRO 98
ARG 213 0.53 HIS 168 -0.45 GLY 245
ARG 213 0.84 MET 169 -0.35 GLY 245
ARG 213 0.79 THR 170 -0.30 PRO 98
ARG 213 0.42 GLU 171 -0.22 GLY 245
HIS 214 0.33 VAL 172 -0.15 ALA 161
SER 99 0.31 VAL 173 -0.18 PHE 212
SER 99 0.44 ARG 174 -0.51 PHE 212
VAL 97 0.51 ARG 175 -0.76 PHE 212
VAL 97 0.48 CYS 176 -0.88 PHE 212
VAL 97 0.53 PRO 177 -1.14 PHE 212
VAL 97 0.61 HIS 178 -1.14 PHE 212
VAL 97 0.66 HIS 179 -1.07 PHE 212
VAL 97 0.68 GLU 180 -1.25 PHE 212
VAL 97 0.74 ARG 181 -1.49 PHE 212
VAL 97 0.95 SER 185 -1.01 PHE 212
SER 99 1.02 ASP 186 -0.75 PHE 212
VAL 97 1.04 GLY 187 -0.85 ASP 207
SER 99 1.15 LEU 188 -0.73 ASP 207
SER 99 1.11 ALA 189 -0.89 ASP 207
SER 99 0.91 PRO 190 -1.44 ASP 207
VAL 97 0.75 PRO 191 -1.48 ASP 207
SER 99 0.64 GLN 192 -1.13 ASP 207
SER 99 0.80 HIS 193 -0.83 ASP 207
SER 99 0.66 LEU 194 -0.56 ASP 207
SER 99 0.83 ILE 195 -0.39 ASP 207
SER 99 0.98 ARG 196 -0.62 TYR 205
SER 99 1.11 VAL 197 -0.58 TYR 205
SER 99 1.00 GLU 198 -0.52 TYR 205
PRO 98 1.10 GLY 199 -0.36 TYR 205
SER 99 1.16 ASN 200 -0.37 ILE 232
PRO 98 1.22 LEU 201 -0.31 GLU 224
SER 99 1.34 ARG 202 -0.17 THR 231
SER 99 1.39 VAL 203 -0.19 ILE 232
SER 99 1.47 GLU 204 -0.21 GLU 198
SER 99 1.27 TYR 205 -0.62 ARG 196
SER 99 1.27 LEU 206 -0.46 PRO 190
ASN 263 1.26 ASP 207 -1.48 PRO 191
GLY 105 1.58 ASP 208 -0.84 ARG 181
SER 106 1.28 ARG 209 -0.86 ARG 181
SER 106 1.26 ASN 210 -0.69 ARG 181
TYR 103 1.47 THR 211 -0.82 ARG 181
LEU 264 1.13 PHE 212 -1.49 ARG 181
MET 169 0.84 ARG 213 -0.71 GLN 192
SER 99 0.86 HIS 214 -0.30 ILE 195
SER 99 1.11 SER 215 -0.28 HIS 214
SER 99 1.31 VAL 216 -0.14 ALA 159
SER 99 1.62 VAL 217 -0.06 PHE 270
SER 99 1.61 VAL 218 -0.12 PHE 270
SER 99 1.53 PRO 219 -0.11 LEU 201
SER 99 1.34 TYR 220 -0.17 LEU 201
SER 99 1.16 GLU 221 -0.27 LEU 201
PRO 98 1.06 PRO 222 -0.26 LEU 201
PRO 98 1.03 PRO 223 -0.28 LEU 201
PRO 98 1.14 GLU 224 -0.31 LEU 201
PRO 98 1.14 VAL 225 -0.25 LEU 201
PRO 98 1.02 GLY 226 -0.23 LEU 201
PRO 98 0.95 SER 227 -0.24 LEU 201
SER 96 1.00 ASP 228 -0.21 LEU 201
SER 96 0.93 CYS 229 -0.23 LEU 201
SER 99 0.94 THR 230 -0.28 LEU 201
SER 99 0.93 THR 231 -0.32 ASN 200
SER 99 1.04 ILE 232 -0.37 ASN 200
SER 99 0.94 HIS 233 -0.34 TYR 205
SER 99 0.92 TYR 234 -0.36 TYR 205
SER 99 0.78 ASN 235 -0.41 ASP 207
SER 99 0.65 TYR 236 -0.44 ASP 207
VAL 97 0.65 MET 237 -0.65 ASP 207
VAL 97 0.55 CYS 238 -0.61 PHE 212
VAL 97 0.55 CYS 238 -0.61 PHE 212
VAL 97 0.47 ASN 239 -0.49 PHE 212
VAL 97 0.35 SER 240 -0.33 PHE 212
VAL 97 0.34 SER 241 -0.44 PHE 212
VAL 97 0.39 CYS 242 -0.60 PHE 212
VAL 97 0.31 MET 243 -0.42 PHE 212
VAL 97 0.19 GLY 244 -0.45 HIS 168
VAL 97 0.16 GLY 245 -0.45 HIS 168
GLN 100 0.15 MET 246 -0.46 GLN 167
SER 96 0.26 ASN 247 -0.49 GLN 167
SER 96 0.31 ARG 248 -0.38 HIS 168
SER 96 0.31 ARG 249 -0.40 HIS 168
SER 96 0.44 PRO 250 -0.23 HIS 168
SER 96 0.43 ILE 251 -0.14 ILE 195
SER 96 0.53 LEU 252 -0.15 ILE 195
ASP 208 0.54 THR 253 -0.18 ILE 195
ASP 208 0.79 ILE 254 -0.08 ILE 254
ASP 208 0.79 ILE 254 -0.08 ILE 254
ASP 208 0.87 ILE 255 -0.11 VAL 216
ASP 208 1.11 THR 256 -0.16 GLN 100
ASP 208 1.11 THR 256 -0.16 GLN 100
ASP 208 1.17 LEU 257 -0.13 GLN 100
SER 99 1.24 GLU 258 -0.11 GLN 100
SER 99 1.20 ASP 259 -0.09 GLN 100
SER 99 1.28 SER 260 -0.07 GLN 100
SER 99 1.12 SER 261 -0.06 GLN 100
ASP 207 1.23 GLY 262 -0.07 GLN 100
ASP 207 1.26 ASN 263 -0.09 GLN 100
ASP 208 1.48 LEU 264 -0.13 GLN 100
ASP 208 1.55 LEU 265 -0.12 GLN 100
ASP 208 1.55 GLY 266 -0.12 GLN 100
ASP 208 1.38 ARG 267 -0.14 GLN 100
ASP 208 1.13 ASN 268 -0.12 ASN 200
ASP 208 0.87 SER 269 -0.12 ILE 195
SER 96 0.79 PHE 270 -0.19 ILE 195
SER 96 0.70 GLU 271 -0.18 ILE 195
SER 96 0.61 VAL 272 -0.23 ILE 195
SER 96 0.61 VAL 272 -0.23 ILE 195
SER 96 0.54 ARG 273 -0.18 ASP 207
SER 96 0.45 VAL 274 -0.29 ASP 207
SER 96 0.46 CYS 275 -0.33 PHE 212
VAL 97 0.52 ALA 276 -0.39 PHE 212
SER 96 0.56 CYS 277 -0.29 PHE 212
SER 96 0.56 CYS 277 -0.29 PHE 212
SER 96 0.66 PRO 278 -0.20 ASP 207
SER 96 0.75 GLY 279 -0.16 ASP 207
SER 96 0.70 ARG 280 -0.17 GLN 167
SER 96 0.67 ASP 281 -0.20 GLN 167
SER 96 0.81 ARG 282 -0.16 GLN 167
SER 96 0.84 ARG 283 -0.17 GLN 167
SER 96 0.75 THR 284 -0.22 GLN 167
SER 96 0.78 GLU 285 -0.23 GLN 167
SER 96 0.92 GLU 286 -0.18 GLN 167
SER 96 0.89 GLU 287 -0.21 GLN 167

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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.