CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402180110433256074

---  normal mode 9  ---

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
SER 215 0.45 VAL 97 -0.95 GLU 286
SER 215 0.50 PRO 98 -0.83 GLU 285
SER 166 0.71 SER 99 -1.03 ASN 210
SER 166 0.77 GLN 100 -0.85 ASN 210
SER 166 0.89 LYS 101 -0.93 ASN 210
SER 166 0.68 THR 102 -0.86 ASN 210
SER 166 0.64 TYR 103 -0.92 ASN 210
ALA 129 0.55 GLN 104 -0.82 ASN 210
SER 166 0.53 GLY 105 -0.87 ASN 210
ALA 129 0.48 SER 106 -0.80 ASN 210
ALA 129 0.48 SER 106 -0.80 ASN 210
ALA 129 0.56 TYR 107 -0.72 ASN 210
ALA 129 0.68 GLY 108 -0.71 ASN 210
ALA 129 0.67 PHE 109 -0.71 ASN 210
ALA 129 0.79 ARG 110 -0.65 ASN 210
SER 127 0.82 LEU 111 -0.55 ASN 210
SER 127 1.00 GLY 112 -0.46 ASN 210
SER 127 0.63 PHE 113 -0.78 LYS 132
ARG 283 0.55 LEU 114 -0.50 LYS 132
ARG 283 0.58 HIS 115 -0.40 LYS 132
ARG 283 0.55 SER 116 -0.47 GLY 226
THR 123 0.57 VAL 122 -0.40 GLY 226
VAL 122 0.57 THR 123 -0.60 GLY 226
GLY 279 0.32 CYS 124 -0.47 GLY 226
ASP 228 0.44 THR 125 -0.33 PRO 250
ASP 228 0.44 THR 125 -0.34 PRO 250
ASP 228 0.50 TYR 126 -0.33 LYS 132
GLY 112 1.00 SER 127 -0.67 GLY 279
ASP 228 0.73 PRO 128 -0.44 ASN 210
ASP 228 0.91 ALA 129 -0.67 GLY 279
ASP 281 0.99 LEU 130 -0.65 ASN 210
ASP 281 0.50 ASN 131 -0.53 ASN 210
ASP 281 0.50 ASN 131 -0.54 ASN 210
ASP 281 0.56 LYS 132 -0.78 PHE 113
ASP 228 0.34 MET 133 -0.37 LYS 132
ASP 228 0.30 PHE 134 -0.43 PRO 250
LEU 130 0.20 CYS 135 -0.50 GLY 226
GLY 279 0.22 GLN 136 -0.63 GLY 226
VAL 122 0.24 LEU 137 -0.69 GLY 226
VAL 122 0.32 ALA 138 -0.81 GLY 226
VAL 122 0.41 LYS 139 -0.84 GLY 226
VAL 122 0.41 LYS 139 -0.84 GLY 226
VAL 122 0.44 THR 140 -0.85 GLY 226
SER 127 0.25 CYS 141 -0.61 GLY 226
SER 127 0.25 CYS 141 -0.62 GLY 226
ARG 283 0.35 PRO 142 -0.53 GLY 226
SER 127 0.47 VAL 143 -0.52 LYS 132
SER 127 0.64 GLN 144 -0.35 ASN 210
SER 127 0.66 LEU 145 -0.50 ASN 210
SER 127 0.75 TRP 146 -0.51 ASN 210
ALA 129 0.71 VAL 147 -0.60 ASN 210
ALA 129 0.73 ASP 148 -0.60 ASN 210
ALA 129 0.61 SER 149 -0.61 ASN 210
ALA 129 0.54 THR 150 -0.58 ASN 210
ALA 129 0.48 PRO 151 -0.64 ASN 210
ALA 129 0.41 PRO 152 -0.60 ASN 210
SER 127 0.41 PRO 152 -0.59 ASN 210
SER 127 0.37 PRO 153 -0.55 ASN 210
SER 127 0.39 PRO 153 -0.52 ASN 210
SER 127 0.33 GLY 154 -0.58 ARG 209
SER 127 0.34 GLY 154 -0.56 ARG 209
SER 127 0.38 THR 155 -0.64 ASN 210
GLN 144 0.39 ARG 156 -0.61 ASN 210
GLN 144 0.43 VAL 157 -0.58 ASN 210
PRO 98 0.37 ARG 158 -0.56 ASN 210
PRO 98 0.29 ALA 159 -0.55 GLU 285
TYR 236 0.24 MET 160 -0.70 GLU 285
TYR 236 0.30 ALA 161 -0.75 GLU 285
GLN 100 0.27 ILE 162 -0.84 GLU 285
LYS 101 0.42 TYR 163 -0.90 THR 284
LYS 101 0.42 LYS 164 -0.82 ARG 283
LYS 101 0.52 GLN 165 -1.11 ARG 283
LYS 101 0.89 SER 166 -1.32 ARG 283
LYS 101 0.65 GLN 167 -1.37 THR 284
LYS 101 0.65 GLN 167 -1.37 THR 284
LYS 101 0.51 HIS 168 -1.26 THR 284
GLN 100 0.65 MET 169 -1.12 THR 284
SER 99 0.41 THR 170 -1.18 GLU 285
LYS 101 0.29 GLU 171 -1.25 GLU 285
GLN 100 0.19 VAL 172 -1.17 GLU 285
GLN 100 0.22 VAL 173 -1.04 GLU 285
PHE 212 0.34 ARG 174 -1.05 GLU 285
PHE 212 0.36 ARG 175 -0.99 GLU 285
PHE 212 0.36 ARG 175 -0.99 GLU 285
ARG 209 0.39 CYS 176 -1.07 GLU 285
ASN 210 0.54 PRO 177 -1.13 GLU 285
ASN 210 0.46 HIS 178 -0.97 GLU 285
ARG 209 0.40 HIS 179 -0.88 GLU 285
ARG 209 0.52 GLU 180 -0.97 GLU 285
ARG 209 0.57 ARG 181 -0.94 GLU 285
ARG 209 0.45 CYS 182 -0.79 GLU 285
ARG 209 0.45 CYS 182 -0.79 GLU 285
ARG 209 0.59 GLY 187 -0.76 GLY 226
ARG 209 0.46 LEU 188 -0.71 GLY 226
ARG 209 0.42 ALA 189 -0.74 GLU 285
ARG 209 0.56 PRO 190 -0.87 GLU 285
ARG 209 0.51 PRO 191 -0.92 GLU 285
PHE 212 0.55 GLN 192 -1.02 GLU 285
PHE 212 0.41 HIS 193 -0.90 GLU 285
PHE 212 0.30 LEU 194 -0.80 GLU 285
PHE 212 0.18 ILE 195 -0.66 GLU 285
VAL 122 0.23 ARG 196 -0.66 GLY 226
VAL 122 0.25 VAL 197 -0.71 GLY 226
VAL 122 0.30 GLU 198 -0.93 GLY 226
ARG 283 0.35 GLY 199 -1.07 VAL 225
ARG 283 0.30 ASN 200 -0.96 GLU 224
ARG 283 0.26 LEU 201 -0.88 VAL 225
PRO 98 0.28 ARG 202 -0.65 GLU 224
PRO 98 0.29 VAL 203 -0.59 VAL 225
PRO 98 0.37 GLU 204 -0.64 GLU 285
PRO 98 0.35 TYR 205 -0.76 GLU 285
PRO 98 0.42 LEU 206 -0.85 GLU 285
LEU 188 0.37 ASP 207 -0.98 GLU 285
GLY 187 0.36 ASP 208 -0.94 GLU 285
GLY 187 0.59 ARG 209 -1.09 ASN 263
ARG 181 0.55 ASN 210 -1.10 LEU 264
ASP 208 0.26 THR 211 -1.09 GLU 285
GLN 192 0.55 PHE 212 -1.09 GLU 285
VAL 97 0.38 ARG 213 -1.04 GLU 285
VAL 97 0.40 HIS 214 -0.94 GLU 285
PRO 98 0.49 SER 215 -0.78 GLU 285
PRO 98 0.50 SER 215 -0.78 GLU 285
PRO 98 0.38 VAL 216 -0.66 GLU 285
PRO 98 0.37 VAL 217 -0.56 GLU 285
SER 127 0.31 VAL 218 -0.45 GLU 224
SER 127 0.38 PRO 219 -0.44 ASN 210
SER 127 0.44 TYR 220 -0.52 ASN 210
SER 127 0.45 GLU 221 -0.47 ASN 210
SER 127 0.52 PRO 222 -0.48 ASN 200
ARG 283 0.63 PRO 223 -0.62 GLY 199
ARG 283 0.72 GLU 224 -0.97 GLY 199
ARG 283 0.63 VAL 225 -1.07 GLY 199
GLU 286 0.61 GLY 226 -1.05 GLY 199
ARG 283 0.85 SER 227 -0.60 GLY 199
ALA 129 0.91 ASP 228 -0.43 GLY 199
SER 127 0.78 CYS 229 -0.44 ASN 210
SER 127 0.60 THR 230 -0.49 GLY 199
SER 127 0.49 THR 231 -0.44 GLY 226
SER 127 0.35 ILE 232 -0.48 GLY 226
ARG 283 0.29 HIS 233 -0.72 GLY 226
VAL 122 0.22 TYR 234 -0.63 GLY 226
VAL 122 0.27 ASN 235 -0.72 GLY 226
THR 253 0.35 TYR 236 -0.62 GLY 226
PHE 212 0.27 MET 237 -0.65 GLU 285
PHE 212 0.23 CYS 238 -0.73 GLU 285
LEU 252 0.24 CYS 238 -0.73 GLU 285
LEU 252 0.27 ASN 239 -0.76 ASP 281
LEU 252 0.22 SER 240 -0.91 ASP 281
LYS 132 0.21 SER 241 -1.14 ASP 281
ARG 209 0.22 CYS 242 -0.88 GLU 285
ASN 210 0.28 MET 243 -1.05 THR 284
ASN 210 0.38 GLY 244 -1.21 GLU 285
ASN 210 0.26 GLY 245 -1.10 GLU 285
LYS 101 0.23 MET 246 -0.97 GLU 285
LYS 101 0.22 ASN 247 -1.03 THR 284
LYS 101 0.22 ARG 248 -1.07 ASP 281
LYS 101 0.29 ARG 249 -1.00 ARG 282
LYS 101 0.26 PRO 250 -1.04 ARG 282
LYS 101 0.23 ILE 251 -0.69 ARG 282
TYR 236 0.31 LEU 252 -0.56 GLU 285
TYR 236 0.31 LEU 252 -0.56 GLU 285
TYR 236 0.35 THR 253 -0.52 GLU 285
SER 166 0.35 ILE 254 -0.68 ASN 210
SER 166 0.35 ILE 254 -0.68 ASN 210
SER 166 0.35 ILE 255 -0.65 ASN 210
THR 256 0.77 THR 256 -0.82 ASN 210
THR 256 0.77 THR 256 -0.82 ASN 210
SER 166 0.38 LEU 257 -0.78 ASN 210
PRO 98 0.38 GLU 258 -0.84 ASN 210
PRO 98 0.38 GLU 258 -0.85 ASN 210
PRO 98 0.35 ASP 259 -0.80 ARG 209
PRO 98 0.32 SER 260 -0.75 ARG 209
PRO 98 0.36 SER 261 -0.94 ARG 209
PRO 98 0.46 GLY 262 -1.06 ARG 209
PRO 98 0.46 ASN 263 -1.09 ARG 209
SER 166 0.49 LEU 264 -1.10 ASN 210
SER 166 0.46 LEU 265 -0.94 ASN 210
SER 166 0.50 GLY 266 -0.90 ASN 210
SER 166 0.52 ARG 267 -0.90 ASN 210
SER 166 0.48 ASN 268 -0.75 ASN 210
SER 166 0.40 SER 269 -0.66 ASN 210
SER 166 0.25 PHE 270 -0.64 LYS 132
ASP 228 0.22 GLU 271 -0.46 ASN 210
ASP 228 0.22 GLU 271 -0.46 ASN 210
CYS 275 0.23 VAL 272 -0.40 ARG 282
LYS 132 0.46 ARG 273 -0.44 ILE 195
LYS 132 0.27 VAL 274 -0.50 ASP 281
LYS 132 0.41 CYS 275 -0.66 ASP 281
LEU 130 0.34 ALA 276 -0.55 GLY 226
LEU 130 0.34 CYS 277 -0.43 GLY 226
LEU 130 0.33 PRO 278 -0.39 GLN 167
THR 123 0.51 GLY 279 -0.67 SER 127
ASP 228 0.40 ARG 280 -0.72 GLN 167
LEU 130 0.99 ASP 281 -1.14 SER 241
ASP 228 0.59 ARG 282 -1.04 PRO 250
SER 227 0.85 ARG 283 -1.36 GLN 167
ASP 228 0.54 THR 284 -1.37 GLN 167
ASP 228 0.39 GLU 285 -1.25 GLU 171
SER 227 0.68 GLU 286 -1.21 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.