CNRS Nantes University US2B US2B
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CA distance fluctuations for 240415002639235721

---  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
GLU 285 0.88 VAL 97 -0.12 ASN 263
GLU 285 0.76 PRO 98 -0.14 PRO 128
GLU 285 0.60 SER 99 -0.16 PRO 128
GLU 285 0.53 GLN 100 -0.18 PRO 128
GLU 286 0.36 LYS 101 -0.26 PRO 128
PHE 113 0.25 THR 102 -0.48 PRO 128
LEU 289 0.20 TYR 103 -0.53 PRO 128
PHE 113 0.07 GLN 104 -0.71 ALA 129
LEU 289 0.12 GLY 105 -0.59 ALA 129
GLY 199 0.06 SER 106 -0.61 ALA 129
GLY 199 0.07 TYR 107 -0.68 ALA 129
GLY 199 0.07 GLY 108 -0.81 ALA 129
LYS 132 0.08 PHE 109 -0.78 PRO 128
LEU 111 0.11 ARG 110 -1.00 PRO 128
LYS 132 0.15 LEU 111 -1.04 PRO 128
LYS 132 0.22 GLY 112 -1.06 PRO 128
LYS 132 0.73 PHE 113 -0.46 ARG 283
LYS 132 0.39 LEU 114 -0.72 ARG 283
LYS 132 0.31 HIS 115 -0.87 ARG 283
LYS 132 0.23 SER 116 -0.80 ARG 283
PRO 128 0.39 SER 121 -0.43 LYS 139
PRO 128 0.30 VAL 122 -0.56 ARG 283
GLU 285 0.17 THR 123 -0.45 ARG 283
ASN 247 0.18 CYS 124 -0.43 ARG 283
SER 121 0.28 THR 125 -0.48 ARG 283
LYS 132 0.31 TYR 126 -0.40 ASP 281
GLY 279 0.65 SER 127 -0.78 GLY 112
GLY 279 0.58 PRO 128 -1.06 GLY 112
ASN 247 0.96 ALA 129 -0.90 ARG 110
LYS 164 0.78 LEU 130 -0.73 ASP 281
PHE 113 0.54 ASN 131 -0.46 ASP 281
PHE 113 0.73 LYS 132 -0.62 ASP 281
LYS 132 0.40 MET 133 -0.26 ASP 281
GLU 285 0.32 PHE 134 -0.18 LEU 111
GLU 285 0.40 CYS 135 -0.14 THR 253
GLU 285 0.48 GLN 136 -0.32 SER 121
GLU 285 0.68 LEU 137 -0.40 SER 121
GLU 285 0.64 ALA 138 -0.41 SER 121
GLU 285 0.44 LYS 139 -0.43 SER 121
GLU 285 0.34 THR 140 -0.37 ARG 283
GLU 285 0.32 CYS 141 -0.33 ARG 283
LYS 132 0.37 PRO 142 -0.44 ARG 283
LYS 132 0.35 VAL 143 -0.52 PRO 128
LYS 132 0.24 GLN 144 -0.69 PRO 128
LYS 132 0.18 LEU 145 -0.75 PRO 128
LYS 132 0.10 TRP 146 -0.85 PRO 128
GLY 199 0.08 VAL 147 -0.81 ALA 129
GLY 199 0.07 ASP 148 -0.83 ALA 129
GLY 199 0.08 SER 149 -0.70 ALA 129
GLY 199 0.09 THR 150 -0.62 ALA 129
GLU 285 0.11 PRO 151 -0.55 ALA 129
GLU 285 0.16 PRO 152 -0.47 ALA 129
GLU 285 0.21 PRO 153 -0.42 ALA 129
GLU 285 0.31 GLY 154 -0.39 PRO 128
GLU 285 0.30 THR 155 -0.44 PRO 128
GLU 285 0.39 ARG 156 -0.43 PRO 128
GLU 285 0.41 VAL 157 -0.47 PRO 128
GLU 285 0.56 ARG 158 -0.40 PRO 128
GLU 285 0.64 ALA 159 -0.35 PRO 128
GLU 285 0.81 MET 160 -0.24 PRO 128
GLU 285 0.94 ALA 161 -0.22 TYR 236
GLU 285 1.02 ILE 162 -0.14 TYR 236
GLU 285 1.09 TYR 163 -0.11 GLN 100
GLU 286 0.92 LYS 164 -0.09 LYS 101
GLU 286 1.15 GLN 165 -0.09 LYS 101
GLU 286 1.16 SER 166 -0.08 ASN 263
GLU 286 1.39 GLN 167 -0.12 ASN 247
GLU 286 1.35 HIS 168 -0.15 ASN 247
GLU 286 1.12 MET 169 -0.10 ASN 247
GLU 285 1.13 THR 170 -0.10 ASN 247
GLU 285 1.33 GLU 171 -0.12 MET 246
GLU 285 1.34 VAL 172 -0.10 GLY 245
GLU 285 1.36 VAL 173 -0.10 GLY 245
GLU 285 1.42 ARG 174 -0.14 SER 121
GLU 285 1.41 ARG 175 -0.21 SER 121
GLU 285 1.56 CYS 176 -0.21 SER 121
GLU 285 1.44 PRO 177 -0.24 SER 121
GLU 285 1.28 HIS 178 -0.31 SER 121
GLU 285 1.20 HIS 179 -0.34 SER 121
GLU 285 1.21 GLU 180 -0.30 SER 121
GLU 285 1.08 ARG 181 -0.36 SER 121
GLU 285 0.71 ASP 186 -0.28 SER 121
GLU 285 0.75 GLY 187 -0.24 SER 121
GLU 285 0.74 LEU 188 -0.23 SER 121
GLU 285 0.85 ALA 189 -0.24 SER 121
GLU 285 0.97 PRO 190 -0.23 SER 121
GLU 285 1.07 PRO 191 -0.27 SER 121
GLU 285 1.22 GLN 192 -0.22 SER 121
GLU 285 1.11 HIS 193 -0.21 SER 121
GLU 285 1.10 LEU 194 -0.19 SER 121
GLU 285 0.88 ILE 195 -0.19 SER 121
GLU 285 0.75 ARG 196 -0.23 SER 121
GLU 285 0.58 VAL 197 -0.25 PRO 128
GLU 285 0.48 GLU 198 -0.25 SER 121
GLU 285 0.38 GLY 199 -0.31 ARG 283
GLU 285 0.41 ASN 200 -0.29 PRO 128
GLU 285 0.43 LEU 201 -0.27 PRO 128
GLU 285 0.47 ARG 202 -0.30 PRO 128
GLU 285 0.57 VAL 203 -0.28 PRO 128
GLU 285 0.66 GLU 204 -0.25 PRO 128
GLU 285 0.80 TYR 205 -0.20 PRO 128
GLU 285 0.85 LEU 206 -0.19 PRO 128
GLU 285 0.97 ASP 207 -0.14 SER 121
GLU 285 0.93 ASP 208 -0.11 PRO 128
LEU 289 0.97 ARG 209 -0.10 SER 121
LEU 289 1.04 ASN 210 -0.07 SER 121
LEU 289 1.03 THR 211 -0.07 SER 121
GLU 285 1.10 PHE 212 -0.11 SER 121
GLU 285 1.09 ARG 213 -0.10 SER 121
GLU 285 1.03 HIS 214 -0.13 SER 121
GLU 285 0.86 SER 215 -0.21 PRO 128
GLU 285 0.73 VAL 216 -0.26 PRO 128
GLU 285 0.59 VAL 217 -0.34 PRO 128
GLU 285 0.47 VAL 218 -0.37 PRO 128
GLU 285 0.37 PRO 219 -0.41 PRO 128
GLU 285 0.27 TYR 220 -0.47 PRO 128
GLU 285 0.19 GLU 221 -0.46 PRO 128
GLY 199 0.15 PRO 222 -0.53 ALA 129
GLY 199 0.17 PRO 223 -0.58 ALA 129
GLY 199 0.24 GLU 224 -0.51 ARG 283
GLY 199 0.20 VAL 225 -0.59 GLU 286
GLY 199 0.13 GLY 226 -0.72 GLU 286
GLY 199 0.13 SER 227 -0.68 ARG 283
GLY 199 0.11 ASP 228 -0.77 ALA 129
LYS 132 0.11 CYS 229 -0.72 ALA 129
LYS 132 0.17 THR 230 -0.58 PRO 128
LYS 132 0.24 THR 231 -0.49 PRO 128
GLU 285 0.29 ILE 232 -0.41 PRO 128
GLU 285 0.35 HIS 233 -0.33 ARG 283
GLU 285 0.52 TYR 234 -0.25 PRO 128
GLU 285 0.62 ASN 235 -0.27 SER 121
GLU 285 0.79 TYR 236 -0.24 SER 121
GLU 285 0.94 MET 237 -0.31 SER 121
GLU 285 1.12 CYS 238 -0.26 SER 121
GLU 285 1.12 CYS 238 -0.26 SER 121
GLU 285 1.07 ASN 239 -0.19 SER 121
GLU 285 1.11 SER 240 -0.12 LEU 252
THR 284 1.25 SER 241 -0.09 LEU 252
GLU 285 1.44 CYS 242 -0.15 SER 121
GLU 285 1.56 MET 243 -0.10 CYS 238
THR 284 1.45 GLY 244 -0.08 CYS 238
THR 284 1.82 GLY 245 -0.11 GLU 171
THR 284 1.66 MET 246 -0.12 HIS 168
ARG 283 1.69 ASN 247 -0.15 HIS 168
THR 284 1.34 ARG 248 -0.05 LYS 101
THR 284 1.23 ARG 249 -0.08 LYS 101
GLU 285 0.93 PRO 250 -0.08 LYS 101
GLU 285 0.97 ILE 251 -0.13 LEU 252
GLU 285 0.73 LEU 252 -0.15 TYR 236
GLU 285 0.66 THR 253 -0.26 PRO 128
GLU 285 0.58 ILE 254 -0.36 PRO 128
GLU 285 0.45 ILE 255 -0.50 PRO 128
GLU 285 0.43 THR 256 -0.49 PRO 128
GLU 285 0.33 LEU 257 -0.52 PRO 128
GLU 285 0.39 GLU 258 -0.43 PRO 128
GLU 285 0.35 ASP 259 -0.40 PRO 128
GLU 285 0.40 SER 260 -0.35 PRO 128
ASN 288 0.47 SER 261 -0.31 PRO 128
GLU 285 0.50 GLY 262 -0.33 PRO 128
LEU 289 0.44 ASN 263 -0.35 PRO 128
GLU 285 0.39 LEU 264 -0.40 PRO 128
GLU 285 0.27 LEU 265 -0.48 PRO 128
GLU 285 0.24 GLY 266 -0.56 PRO 128
GLU 285 0.30 ARG 267 -0.56 PRO 128
GLU 285 0.25 ASN 268 -0.66 PRO 128
PHE 113 0.37 SER 269 -0.48 PRO 128
PHE 113 0.62 PHE 270 -0.28 PRO 128
LEU 130 0.56 GLU 271 -0.21 ASP 281
GLU 285 0.58 VAL 272 -0.15 ASN 131
GLU 285 0.66 ARG 273 -0.25 CYS 275
GLU 285 0.75 VAL 274 -0.13 SER 121
GLU 285 0.63 CYS 275 -0.25 ARG 273
ASP 281 0.52 ALA 276 -0.22 SER 121
ASP 281 0.43 CYS 277 -0.31 ARG 280
ALA 129 0.35 PRO 278 -0.14 CYS 277
SER 127 0.65 GLY 279 -0.44 VAL 122
ALA 129 0.67 ARG 280 -0.31 CYS 277
SER 241 0.80 ASP 281 -0.73 LEU 130
ARG 248 0.87 ARG 282 -0.68 ASP 281
ASN 247 1.69 ARG 283 -0.87 HIS 115
GLY 245 1.82 THR 284 -0.43 GLY 226
CYS 176 1.56 GLU 285 -0.25 ASP 228
GLN 167 1.39 GLU 286 -0.72 GLY 226
GLN 167 1.10 GLU 287 -0.68 GLY 226
GLU 171 1.00 ASN 288 -0.34 GLY 226
GLU 171 1.07 LEU 289 -0.41 GLY 226
THR 170 0.71 ARG 290 -0.53 GLY 226

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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.