CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404111648063733338

---  normal mode 14  ---

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
ARG 213 1.14 VAL 97 -1.31 ASN 288
THR 150 0.37 PRO 98 -1.23 GLU 285
GLN 167 1.49 SER 99 -1.76 LEU 257
ILE 162 0.57 GLN 100 -1.56 GLU 285
SER 166 0.45 LYS 101 -1.79 GLU 285
SER 166 0.34 THR 102 -1.82 GLU 285
LEU 206 0.37 TYR 103 -1.65 GLU 285
LEU 206 0.31 GLN 104 -1.74 LEU 130
LEU 206 0.43 GLY 105 -1.72 LEU 130
PRO 151 0.47 SER 106 -1.57 LEU 130
LEU 206 0.37 TYR 107 -1.64 ALA 129
LEU 206 0.27 GLY 108 -1.72 ALA 129
THR 256 0.21 PHE 109 -1.57 ASN 131
SER 166 0.20 ARG 110 -1.78 ASN 131
CYS 229 0.31 LEU 111 -1.38 ASN 131
ILE 255 0.55 GLY 112 -1.27 PRO 151
PHE 270 1.20 PHE 113 -1.29 PRO 151
PHE 270 0.79 LEU 114 -1.10 PRO 151
GLY 226 0.66 HIS 115 -0.94 PRO 151
GLY 226 0.73 SER 116 -0.82 PRO 151
GLY 226 0.90 SER 121 -0.88 ALA 276
GLY 226 0.65 VAL 122 -0.72 PRO 151
GLY 226 0.58 THR 123 -0.68 PRO 151
GLY 226 0.49 CYS 124 -0.82 PRO 151
GLY 226 0.41 THR 125 -1.01 PRO 151
GLY 226 0.30 TYR 126 -1.11 PRO 151
ARG 248 0.39 SER 127 -1.31 ARG 110
ASN 247 0.59 PRO 128 -1.87 TRP 146
ASN 247 0.77 ALA 129 -1.81 ASP 148
SER 241 0.80 LEU 130 -1.74 GLN 104
ASN 247 0.74 ASN 131 -1.78 ARG 110
PRO 250 0.40 LYS 132 -1.06 ARG 282
LEU 114 0.39 MET 133 -0.90 PRO 151
LEU 130 0.46 PHE 134 -0.88 PRO 151
GLY 262 0.38 CYS 135 -0.73 PRO 151
GLY 262 0.50 GLN 136 -0.61 PRO 151
GLY 262 0.59 LEU 137 -0.52 PRO 151
GLY 262 0.71 ALA 138 -0.50 PRO 151
GLY 262 0.64 LYS 139 -0.60 PRO 151
ARG 158 0.68 THR 140 -0.68 PRO 151
ARG 158 0.68 CYS 141 -0.80 PRO 151
ILE 255 0.80 PRO 142 -0.94 PRO 151
ILE 255 1.08 VAL 143 -1.03 PRO 151
ILE 255 0.79 GLN 144 -1.28 PRO 151
THR 256 0.62 LEU 145 -1.45 PRO 128
THR 256 0.39 TRP 146 -1.87 PRO 128
LEU 257 0.57 VAL 147 -1.67 ALA 129
ARG 156 0.48 ASP 148 -1.81 ALA 129
THR 155 0.64 SER 149 -1.61 ALA 129
GLU 258 1.12 THR 150 -1.31 ALA 129
SER 106 0.47 PRO 151 -1.71 PRO 128
LEU 206 0.28 PRO 152 -1.55 ALA 129
ASP 186 0.58 PRO 153 -1.40 LEU 289
GLU 204 0.73 GLY 154 -1.35 LEU 289
THR 150 1.07 THR 155 -1.38 LEU 289
THR 150 0.87 ARG 156 -1.24 SER 99
ILE 232 1.09 VAL 157 -1.37 SER 99
ILE 232 1.00 ARG 158 -1.14 SER 99
TYR 234 0.89 ALA 159 -0.99 GLU 285
GLY 262 0.58 MET 160 -0.93 GLU 285
PHE 113 0.57 ALA 161 -0.85 GLU 285
PHE 113 0.57 ILE 162 -0.84 GLU 285
SER 99 0.73 TYR 163 -0.81 THR 284
SER 99 0.71 LYS 164 -1.01 THR 284
SER 99 1.08 GLN 165 -0.94 THR 284
SER 99 1.46 SER 166 -0.96 THR 284
SER 99 1.49 GLN 167 -0.77 THR 284
SER 99 1.24 HIS 168 -0.71 THR 284
SER 99 1.20 MET 169 -0.84 THR 284
SER 99 0.86 THR 170 -0.84 ASN 288
SER 99 0.76 GLU 171 -0.64 ASN 288
VAL 97 0.77 VAL 172 -0.62 ASN 288
GLY 262 0.56 VAL 173 -0.58 GLU 285
GLY 262 0.67 ARG 174 -0.48 GLU 285
GLY 262 0.67 ARG 175 -0.34 GLU 285
GLY 262 0.59 CYS 176 -0.27 SER 121
SER 261 0.61 PRO 177 -0.24 SER 121
SER 261 0.60 HIS 178 -0.27 SER 121
SER 261 0.65 HIS 179 -0.30 PRO 151
SER 261 0.73 GLU 180 -0.29 ASP 186
SER 261 0.71 ARG 181 -0.36 ASP 186
LEU 201 1.09 ASP 186 -0.38 LEU 289
SER 261 0.95 GLY 187 -0.43 LEU 289
SER 261 1.13 LEU 188 -0.55 LEU 289
GLY 262 1.06 ALA 189 -0.53 LEU 289
SER 261 1.01 PRO 190 -0.50 LEU 289
SER 261 0.87 PRO 191 -0.39 LEU 289
GLY 262 0.82 GLN 192 -0.42 GLU 285
GLY 262 0.90 HIS 193 -0.54 GLU 285
GLY 262 0.76 LEU 194 -0.55 GLU 285
GLY 262 0.81 ILE 195 -0.68 GLU 285
GLY 262 0.89 ARG 196 -0.60 GLU 285
GLY 262 0.87 VAL 197 -0.61 GLU 285
GLY 262 0.77 GLU 198 -0.54 PRO 151
PRO 219 0.76 GLY 199 -0.59 PRO 128
SER 261 0.64 ASN 200 -0.91 PRO 128
ASP 186 1.09 LEU 201 -1.06 GLU 224
SER 261 0.86 ARG 202 -0.85 LEU 289
GLY 262 1.04 VAL 203 -0.82 LEU 289
GLY 262 1.54 GLU 204 -0.79 LEU 289
GLY 262 1.45 TYR 205 -0.71 LEU 289
GLY 262 1.38 LEU 206 -0.74 LEU 289
GLY 262 0.92 ASP 207 -0.75 LEU 289
VAL 97 0.75 ASP 208 -0.95 LEU 289
PRO 191 0.56 ARG 209 -1.01 LEU 289
PRO 177 0.46 ASN 210 -1.15 ASN 288
VAL 97 0.69 THR 211 -1.02 ASN 288
VAL 97 0.80 PHE 212 -0.80 ASN 288
VAL 97 1.14 ARG 213 -0.74 ASN 288
GLY 262 0.90 HIS 214 -0.69 GLU 285
GLY 262 0.99 SER 215 -0.80 GLU 285
GLY 262 1.16 VAL 216 -0.81 GLU 285
GLY 262 0.89 VAL 217 -0.93 LEU 289
GLU 198 0.72 VAL 218 -1.00 SER 99
GLY 199 0.76 PRO 219 -1.05 LEU 289
THR 150 0.56 TYR 220 -1.19 SER 99
SER 121 0.42 GLU 221 -1.05 LEU 289
SER 121 0.40 PRO 222 -1.09 PRO 128
SER 121 0.47 PRO 223 -1.03 PRO 128
SER 121 0.67 GLU 224 -1.06 LEU 201
SER 121 0.81 VAL 225 -0.80 LEU 201
SER 121 0.90 GLY 226 -0.78 PRO 151
SER 121 0.66 SER 227 -0.97 PRO 151
SER 121 0.41 ASP 228 -1.20 PRO 151
ILE 255 0.40 CYS 229 -1.33 PRO 151
VAL 157 0.48 THR 230 -1.14 PRO 128
VAL 157 0.76 THR 231 -1.04 PRO 151
VAL 157 1.09 ILE 232 -0.86 PRO 128
ARG 158 0.95 HIS 233 -0.73 PRO 151
ARG 158 0.96 TYR 234 -0.64 PRO 151
GLY 262 0.74 ASN 235 -0.55 PRO 151
GLY 262 0.67 TYR 236 -0.51 PRO 151
GLY 262 0.69 MET 237 -0.43 PRO 151
GLY 262 0.60 CYS 238 -0.39 PRO 151
GLY 262 0.60 CYS 238 -0.40 PRO 151
LEU 130 0.55 ASN 239 -0.45 PRO 151
LEU 130 0.61 SER 240 -0.42 PRO 151
LEU 130 0.80 SER 241 -0.51 SER 121
LEU 130 0.64 CYS 242 -0.41 SER 121
LEU 130 0.53 MET 243 -0.35 THR 284
LEU 130 0.62 GLY 244 -0.44 THR 284
LEU 130 0.68 GLY 245 -0.41 SER 121
LEU 130 0.78 MET 246 -0.52 SER 121
LEU 130 0.80 ASN 247 -0.57 ARG 280
LEU 130 0.79 ARG 248 -0.58 ARG 280
SER 99 0.71 ARG 249 -0.68 THR 284
ASN 131 0.53 PRO 250 -0.78 THR 284
PHE 113 0.59 ILE 251 -0.78 THR 284
PHE 113 0.80 LEU 252 -0.98 GLU 285
PHE 113 0.85 THR 253 -1.01 GLU 285
VAL 143 0.91 ILE 254 -1.21 GLU 285
VAL 143 1.08 ILE 255 -1.22 GLU 285
VAL 143 0.76 THR 256 -1.61 SER 99
THR 150 0.87 LEU 257 -1.76 SER 99
THR 150 1.12 GLU 258 -1.48 LEU 289
THR 150 1.07 ASP 259 -1.57 LEU 289
GLU 204 1.17 SER 260 -1.41 LEU 289
GLU 204 1.28 SER 261 -1.41 LEU 289
GLU 204 1.54 GLY 262 -1.44 LEU 289
LEU 206 1.27 ASN 263 -1.72 LEU 289
LEU 206 1.00 LEU 264 -1.75 LEU 289
THR 150 0.84 LEU 265 -1.64 LEU 289
THR 150 0.55 GLY 266 -1.47 LEU 289
VAL 143 0.44 ARG 267 -1.60 GLU 285
PHE 113 0.50 ASN 268 -1.55 GLU 285
PHE 113 0.86 SER 269 -1.38 GLU 285
PHE 113 1.20 PHE 270 -1.14 GLU 285
PHE 113 0.84 GLU 271 -0.98 GLU 285
PHE 113 0.61 VAL 272 -0.74 ASP 281
LEU 130 0.49 ARG 273 -0.63 PRO 151
LEU 130 0.48 VAL 274 -0.58 PRO 151
LEU 130 0.64 CYS 275 -0.60 PRO 151
LEU 130 0.61 ALA 276 -0.88 SER 121
LEU 130 0.48 CYS 277 -0.66 PRO 151
LEU 130 0.51 PRO 278 -0.76 PRO 151
GLY 226 0.49 GLY 279 -0.80 PRO 151
GLY 226 0.46 ARG 280 -0.72 PRO 151
LEU 130 0.60 ASP 281 -0.93 GLU 271
LEU 130 0.67 ARG 282 -1.06 LYS 132
GLY 226 0.38 ARG 283 -0.97 THR 102
GLY 226 0.18 THR 284 -1.36 LYS 101
GLU 286 0.25 GLU 285 -1.82 THR 102
GLU 285 0.25 GLU 286 -1.65 THR 102
SER 121 0.18 GLU 287 -1.43 LYS 101
SER 121 0.08 ASN 288 -1.42 LEU 264
MET 246 0.05 LEU 289 -1.75 LEU 264

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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.