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CA distance fluctuations for 24041412001571065

---  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
GLY 262 1.29 SER 96 -0.32 PRO 177
GLY 262 1.08 VAL 97 -0.41 GLY 112
GLU 258 1.10 PRO 98 -0.49 LEU 206
LEU 264 0.99 SER 99 -0.67 LEU 206
GLU 285 0.86 GLN 100 -0.62 GLY 112
LEU 130 1.34 LYS 101 -0.48 LEU 206
LEU 130 1.73 THR 102 -0.37 LEU 206
ALA 129 1.55 TYR 103 -0.45 LEU 206
ALA 129 1.56 GLN 104 -0.28 LEU 206
ALA 129 1.32 GLY 105 -0.31 LEU 206
ALA 129 1.14 SER 106 -0.26 GLU 204
ALA 129 1.00 TYR 107 -0.20 GLU 258
ALA 129 1.19 GLY 108 -0.19 SER 166
ALA 129 1.06 PHE 109 -0.20 SER 166
PRO 128 1.07 ARG 110 -0.39 SER 166
PRO 128 0.75 LEU 111 -0.48 SER 166
ASN 200 0.53 GLY 112 -1.41 PHE 270
ASN 200 0.44 PHE 113 -0.99 PHE 270
LEU 289 0.27 LEU 114 -1.16 THR 231
THR 102 0.42 HIS 115 -1.23 SER 227
THR 102 0.47 SER 116 -1.14 SER 227
THR 102 0.66 GLY 117 -1.20 SER 227
THR 102 0.73 THR 118 -1.18 GLY 226
THR 102 0.57 ALA 119 -1.22 GLY 226
THR 102 0.53 LYS 120 -1.09 GLY 226
THR 102 0.41 SER 121 -1.02 GLY 226
THR 102 0.44 VAL 122 -0.97 GLY 226
THR 102 0.43 THR 123 -0.80 PRO 219
THR 102 0.49 CYS 124 -0.75 GLY 226
THR 102 0.68 THR 125 -0.89 SER 227
THR 102 0.89 TYR 126 -0.86 SER 227
THR 102 1.25 SER 127 -0.81 SER 227
GLN 104 1.34 PRO 128 -0.72 SER 227
GLN 104 1.56 ALA 129 -0.82 ARG 248
THR 102 1.73 LEU 130 -1.00 ARG 248
THR 102 1.44 ASN 131 -0.69 SER 227
THR 102 0.99 LYS 132 -0.75 SER 227
ASN 268 0.85 MET 133 -0.67 SER 227
ASN 268 0.85 MET 133 -0.67 SER 227
THR 102 0.75 PHE 134 -0.70 SER 227
THR 102 0.53 CYS 135 -0.63 GLY 226
THR 102 0.41 GLN 136 -0.60 GLY 226
THR 102 0.30 LEU 137 -0.47 GLY 226
LEU 111 0.28 ALA 138 -0.52 PRO 219
LEU 111 0.32 LYS 139 -0.71 PRO 219
LEU 111 0.37 THR 140 -0.86 PRO 219
LEU 111 0.42 CYS 141 -0.72 PRO 219
LEU 111 0.42 CYS 141 -0.72 PRO 219
LEU 111 0.46 PRO 142 -0.75 PRO 219
LEU 111 0.67 VAL 143 -0.87 THR 253
ASN 200 0.61 GLN 144 -1.01 PHE 270
ASN 200 0.91 LEU 145 -0.56 LEU 114
ASN 200 0.79 TRP 146 -0.48 PHE 270
ASN 210 0.80 VAL 147 -0.28 LEU 114
ASN 210 0.79 ASP 148 -0.24 SER 166
ASN 210 1.01 SER 149 -0.30 LEU 114
ASN 210 1.23 THR 150 -0.47 LEU 114
ASN 210 1.39 PRO 151 -0.42 LEU 114
ASN 210 1.70 PRO 152 -0.45 SER 121
ASN 210 1.90 PRO 153 -0.62 SER 121
ASN 210 1.75 GLY 154 -0.64 GLY 199
ASN 210 1.59 THR 155 -0.62 HIS 233
THR 211 1.37 ARG 156 -0.83 HIS 233
THR 211 1.00 VAL 157 -0.86 HIS 233
THR 211 0.90 ARG 158 -0.72 HIS 233
ILE 232 0.45 ALA 159 -0.55 GLN 144
ARG 158 0.36 MET 160 -0.56 GLN 144
ASP 281 0.34 ALA 161 -0.66 GLY 112
GLY 262 0.51 ILE 162 -0.73 GLY 112
GLY 262 0.52 TYR 163 -0.79 GLY 112
GLY 262 0.56 LYS 164 -0.96 GLY 112
GLY 262 0.59 GLN 165 -0.89 GLY 112
GLY 262 0.67 SER 166 -0.87 GLY 112
GLY 262 0.63 GLN 167 -0.73 GLY 112
GLY 262 0.62 HIS 168 -0.69 LEU 289
GLY 262 0.71 MET 169 -0.71 GLY 112
GLY 262 0.84 THR 170 -0.53 GLY 112
GLY 262 0.66 GLU 171 -0.61 LEU 289
ARG 156 0.56 VAL 172 -0.49 LEU 289
GLY 262 0.36 VAL 173 -0.54 GLY 112
PRO 222 0.28 ARG 174 -0.61 PHE 212
PRO 222 0.23 ARG 175 -0.63 PHE 212
PRO 222 0.19 CYS 176 -0.65 LEU 289
PRO 222 0.23 PRO 177 -0.76 PHE 212
ILE 232 0.19 HIS 178 -0.62 PHE 212
ILE 232 0.22 HIS 179 -0.61 PHE 212
PRO 223 0.27 GLU 180 -0.79 PHE 212
PRO 223 0.29 ARG 181 -0.72 PHE 212
PRO 223 0.26 CYS 182 -0.59 PHE 212
THR 231 0.32 SER 183 -0.54 PHE 212
THR 231 0.34 ASP 184 -0.48 PHE 212
THR 231 0.45 SER 185 -0.48 PHE 212
THR 231 0.50 ASP 186 -0.49 SER 261
PRO 223 0.58 GLY 187 -0.52 GLY 262
PRO 223 0.67 LEU 188 -0.54 GLY 262
PRO 223 0.51 ALA 189 -0.41 GLY 262
PRO 223 0.49 PRO 190 -0.60 PHE 212
PRO 223 0.40 PRO 191 -0.77 PHE 212
PRO 222 0.36 GLN 192 -0.91 PHE 212
PRO 222 0.35 HIS 193 -0.55 PHE 212
ILE 232 0.31 LEU 194 -0.43 PHE 212
ILE 232 0.41 ILE 195 -0.27 GLN 144
ILE 232 0.48 ARG 196 -0.32 GLY 262
ILE 232 0.68 VAL 197 -0.47 PRO 219
THR 231 0.56 GLU 198 -0.78 PRO 219
THR 231 0.91 GLY 199 -0.86 PRO 219
THR 230 1.43 ASN 200 -0.59 SER 261
THR 230 1.24 LEU 201 -0.71 SER 261
THR 230 1.15 ARG 202 -0.88 GLY 262
THR 230 0.94 VAL 203 -0.72 GLY 262
PRO 223 0.70 GLU 204 -0.71 GLY 262
PRO 222 0.60 TYR 205 -0.49 LEU 264
PRO 222 0.64 LEU 206 -0.67 SER 99
PRO 219 0.61 ASP 207 -0.55 SER 99
PRO 219 1.21 ASP 208 -0.39 SER 99
GLY 154 1.41 ARG 209 -0.69 ARG 181
PRO 153 1.90 ASN 210 -0.66 PRO 177
ARG 156 1.37 THR 211 -0.54 PRO 177
ARG 156 0.98 PHE 212 -0.91 GLN 192
ARG 156 0.81 ARG 213 -0.43 GLN 192
PRO 222 0.48 HIS 214 -0.54 SER 99
PRO 222 0.50 SER 215 -0.50 SER 99
PRO 222 0.52 VAL 216 -0.35 LEU 264
ASP 208 0.88 VAL 217 -0.45 HIS 233
ASP 208 0.92 VAL 218 -0.70 HIS 233
ARG 209 1.39 PRO 219 -1.06 ILE 232
ASN 210 1.26 TYR 220 -0.86 ILE 232
ASN 210 1.23 GLU 221 -0.85 SER 116
ASN 210 1.21 PRO 222 -0.77 SER 116
ARG 202 1.14 PRO 223 -0.93 SER 116
ASN 210 0.92 GLU 224 -1.12 SER 116
ASN 210 1.05 VAL 225 -1.01 ALA 119
ASN 210 0.80 GLY 226 -1.22 ALA 119
ASN 210 0.70 SER 227 -1.23 HIS 115
LEU 201 0.88 ASP 228 -1.00 HIS 115
ASN 200 1.04 CYS 229 -1.05 LEU 114
ASN 200 1.43 THR 230 -1.07 LEU 114
ASN 200 1.42 THR 231 -1.16 LEU 114
VAL 197 0.68 ILE 232 -1.06 PRO 219
LEU 111 0.44 HIS 233 -0.97 PRO 219
LEU 111 0.40 TYR 234 -0.65 PRO 219
LEU 111 0.31 ASN 235 -0.53 PRO 219
SER 269 0.31 TYR 236 -0.31 PRO 219
ILE 232 0.21 MET 237 -0.39 PHE 212
SER 269 0.19 CYS 238 -0.46 LEU 289
THR 102 0.28 ASN 239 -0.54 LEU 289
THR 102 0.30 SER 240 -0.74 LEU 130
THR 102 0.25 SER 241 -0.84 LEU 289
THR 102 0.17 CYS 242 -0.79 LEU 289
GLY 262 0.19 MET 243 -0.92 LEU 289
GLY 262 0.21 GLY 244 -0.86 LEU 289
GLY 262 0.22 GLY 245 -0.74 LEU 289
GLY 262 0.30 MET 246 -0.74 LEU 289
GLY 262 0.29 ASN 247 -0.95 LEU 289
ASN 263 0.31 ARG 248 -1.00 LEU 130
GLY 262 0.38 ARG 249 -0.97 LEU 130
ASP 281 0.44 PRO 250 -0.89 LEU 130
ASP 281 0.45 ILE 251 -0.80 GLY 112
ASP 281 0.54 LEU 252 -0.99 GLY 112
ASP 281 0.44 THR 253 -0.95 GLN 144
ASN 288 0.50 ILE 254 -0.80 GLN 144
PRO 128 0.64 ILE 255 -0.64 GLN 144
ALA 129 0.74 THR 256 -0.44 GLN 144
ASN 210 0.92 LEU 257 -0.46 GLN 144
PRO 98 1.10 GLU 258 -0.49 HIS 233
ASN 210 1.33 ASP 259 -0.53 ARG 202
ASN 210 1.40 SER 260 -0.69 ARG 202
SER 96 1.08 SER 261 -0.82 ARG 202
SER 96 1.29 GLY 262 -0.88 ARG 202
SER 96 1.00 ASN 263 -0.65 GLU 204
ASN 288 1.05 LEU 264 -0.64 GLU 204
ASN 288 0.99 LEU 265 -0.45 GLU 204
ALA 129 1.11 GLY 266 -0.36 LEU 206
LEU 130 1.15 ARG 267 -0.43 LEU 206
ASN 131 1.26 ASN 268 -0.45 GLN 144
MET 133 0.81 SER 269 -1.03 GLY 112
SER 269 0.63 PHE 270 -1.41 GLY 112
ASP 281 0.75 GLU 271 -1.03 GLY 112
ASP 281 0.59 VAL 272 -0.68 GLY 112
VAL 272 0.58 ARG 273 -0.63 LEU 130
THR 102 0.46 VAL 274 -0.55 GLY 226
THR 102 0.49 CYS 275 -0.66 GLY 226
THR 102 0.48 ALA 276 -0.70 GLY 226
THR 102 0.61 CYS 277 -0.86 GLY 226
THR 102 0.61 CYS 277 -0.86 GLY 226
THR 102 0.69 PRO 278 -0.86 GLY 226
THR 102 0.74 GLY 279 -1.03 GLY 226
THR 102 0.76 ARG 280 -1.02 GLY 226
LYS 101 0.92 ASP 281 -0.87 GLY 226
THR 102 1.00 ARG 282 -0.90 GLY 226
THR 102 0.95 ARG 283 -1.04 GLY 226
LYS 101 1.08 THR 284 -0.89 GLY 226
LYS 101 1.24 GLU 285 -0.71 GLY 226
THR 102 1.26 GLU 286 -0.70 ARG 248
LYS 101 1.09 GLU 287 -0.82 GLY 226
TYR 103 1.25 ASN 288 -0.59 MET 243
TYR 103 1.00 LEU 289 -0.97 ARG 248

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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.