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CA distance fluctuations for 2402161052242961240

---  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
ARG 181 0.41 SER 96 -1.14 ALA 129
SER 166 0.20 VAL 97 -1.28 GLY 187
GLN 167 0.72 PRO 98 -1.70 PRO 219
TYR 103 0.16 SER 99 -1.71 ARG 213
THR 256 0.29 GLN 100 -1.15 ARG 213
ALA 129 0.23 LYS 101 -1.24 ARG 213
ALA 129 0.20 THR 102 -1.35 ASP 208
ALA 129 0.17 TYR 103 -1.55 ASP 208
ASN 200 0.17 GLN 104 -1.56 ASP 208
SER 99 0.14 GLY 105 -1.63 ASP 208
LEU 201 0.16 SER 106 -1.51 ASP 208
LEU 201 0.22 TYR 107 -1.35 ASP 208
LEU 201 0.23 GLY 108 -1.40 ASP 208
LEU 201 0.25 PHE 109 -1.28 ASP 208
ASN 200 0.27 ARG 110 -1.15 ASP 208
ASN 200 0.28 LEU 111 -0.95 ASP 208
ASN 200 0.28 GLY 112 -0.82 ASP 208
ASN 200 0.28 PHE 113 -0.75 SER 96
ASN 200 0.28 LEU 114 -0.73 SER 96
ASP 207 0.30 VAL 122 -0.54 SER 96
ASP 207 0.37 THR 123 -0.60 VAL 97
TYR 205 0.31 CYS 124 -0.53 PRO 98
TYR 205 0.26 THR 125 -0.67 SER 96
ASN 200 0.23 TYR 126 -0.78 SER 96
ASN 200 0.22 SER 127 -0.92 SER 96
ASN 200 0.24 PRO 128 -1.05 SER 96
LYS 101 0.23 ALA 129 -1.14 SER 96
LYS 101 0.21 LEU 130 -1.02 SER 96
LEU 111 0.24 ASN 131 -0.95 SER 96
ASN 200 0.22 LYS 132 -0.79 SER 96
TYR 205 0.25 MET 133 -0.67 SER 96
TYR 205 0.25 MET 133 -0.67 SER 96
TYR 205 0.26 PHE 134 -0.59 SER 96
TYR 205 0.31 CYS 135 -0.51 VAL 97
ASP 207 0.48 GLN 136 -0.60 VAL 97
ASP 207 0.63 LEU 137 -0.68 VAL 97
ASP 207 0.71 ALA 138 -0.80 VAL 97
ASP 207 0.56 LYS 139 -0.76 VAL 97
TYR 205 0.51 THR 140 -0.79 PRO 98
TYR 205 0.41 CYS 141 -0.75 PRO 98
TYR 205 0.41 CYS 141 -0.75 PRO 98
TYR 205 0.35 PRO 142 -0.86 PRO 98
ASN 200 0.35 VAL 143 -0.85 PRO 98
ASN 200 0.38 GLN 144 -0.89 PRO 98
ASN 200 0.36 LEU 145 -0.94 PRO 98
LEU 201 0.34 TRP 146 -1.00 ASP 208
LEU 201 0.30 VAL 147 -1.13 ASP 208
LEU 201 0.26 ASP 148 -1.19 ASP 208
LEU 201 0.24 SER 149 -1.13 ASP 208
LEU 201 0.26 THR 150 -1.07 PRO 98
PRO 222 0.34 PRO 151 -1.05 ASP 208
LEU 201 0.20 PRO 152 -1.10 PRO 98
LEU 201 0.17 PRO 153 -1.30 PRO 98
GLN 100 0.13 GLY 154 -1.44 PRO 98
GLN 100 0.16 THR 155 -1.33 PRO 98
GLN 100 0.15 ARG 156 -1.36 PRO 98
GLN 100 0.17 VAL 157 -1.19 PRO 98
GLN 100 0.16 ARG 158 -0.98 PRO 98
HIS 214 0.38 ALA 159 -0.76 PRO 98
HIS 214 0.28 MET 160 -0.56 SER 99
THR 170 0.21 ALA 161 -0.70 SER 99
THR 170 0.27 ILE 162 -0.91 SER 99
THR 170 0.19 TYR 163 -0.71 SER 99
PRO 98 0.23 LYS 164 -0.76 ARG 213
PRO 98 0.45 GLN 165 -0.70 ARG 213
PRO 98 0.63 SER 166 -0.81 ARG 213
PRO 98 0.63 SER 166 -0.81 ARG 213
PRO 98 0.72 GLN 167 -0.62 ARG 213
PRO 98 0.52 HIS 168 -0.59 ARG 213
PRO 98 0.43 MET 169 -0.88 ARG 213
PRO 98 0.51 THR 170 -0.52 ARG 213
PRO 98 0.35 GLU 171 -0.49 SER 99
ALA 161 0.20 VAL 172 -0.57 SER 99
PHE 212 0.17 VAL 173 -0.64 SER 99
PHE 212 0.45 ARG 174 -0.54 VAL 97
ASP 207 0.72 ARG 175 -0.64 VAL 97
PHE 212 0.82 CYS 176 -0.60 VAL 97
PHE 212 1.06 PRO 177 -0.69 VAL 97
PHE 212 1.12 HIS 178 -0.77 VAL 97
PHE 212 1.05 HIS 179 -0.82 VAL 97
PHE 212 1.15 GLU 180 -0.87 VAL 97
PHE 212 1.44 ARG 181 -0.97 VAL 97
ASP 207 1.33 SER 185 -1.17 VAL 97
ASP 207 1.00 ASP 186 -1.53 LEU 201
ASP 207 1.13 GLY 187 -1.48 LEU 201
ASP 207 0.87 LEU 188 -1.27 VAL 203
ASP 207 0.96 ALA 189 -1.21 VAL 203
ASP 207 1.22 PRO 190 -0.98 VAL 97
ASP 207 1.38 PRO 191 -0.97 VAL 97
ARG 213 0.99 GLN 192 -0.80 VAL 97
ASP 207 0.73 HIS 193 -0.75 VAL 97
HIS 214 0.58 LEU 194 -0.67 VAL 97
HIS 214 0.68 ILE 195 -0.70 VAL 97
TYR 205 0.92 ARG 196 -0.89 PRO 98
TYR 205 0.86 VAL 197 -1.11 PRO 98
TYR 205 0.81 GLU 198 -1.13 PRO 98
TYR 205 0.56 GLY 199 -1.28 PRO 98
ILE 232 0.59 ASN 200 -1.41 PRO 98
GLU 224 0.67 LEU 201 -1.53 ASP 186
GLU 221 0.37 ARG 202 -1.51 PRO 98
GLU 221 0.35 VAL 203 -1.30 PRO 98
VAL 197 0.46 GLU 204 -1.23 PRO 98
ARG 196 0.92 TYR 205 -0.96 PRO 98
PRO 190 0.80 LEU 206 -1.35 GLY 262
PRO 191 1.38 ASP 207 -1.35 ASN 263
ARG 181 0.83 ASP 208 -1.63 GLY 105
ARG 181 0.73 ARG 209 -1.09 SER 106
ARG 181 0.60 ASN 210 -1.02 SER 106
ARG 181 0.75 THR 211 -1.30 GLN 104
ARG 181 1.44 PHE 212 -1.11 GLY 105
GLN 192 0.99 ARG 213 -1.71 SER 99
ILE 195 0.68 HIS 214 -0.86 SER 99
HIS 214 0.51 SER 215 -0.78 SER 99
HIS 214 0.27 VAL 216 -0.96 PRO 98
HIS 214 0.18 VAL 217 -1.20 PRO 98
VAL 203 0.17 VAL 218 -1.48 PRO 98
PRO 151 0.19 PRO 219 -1.70 PRO 98
PRO 151 0.33 TYR 220 -1.51 PRO 98
LEU 201 0.57 GLU 221 -1.48 PRO 98
LEU 201 0.54 PRO 222 -1.28 PRO 98
LEU 201 0.59 PRO 223 -1.16 PRO 98
LEU 201 0.67 GLU 224 -1.17 PRO 98
LEU 201 0.56 VAL 225 -1.07 PRO 98
LEU 201 0.49 GLY 226 -0.96 PRO 98
LEU 201 0.49 SER 227 -0.97 PRO 98
LEU 201 0.43 ASP 228 -0.91 PRO 98
LEU 201 0.45 CYS 229 -0.98 PRO 98
LEU 201 0.53 THR 230 -1.13 PRO 98
ASN 200 0.55 THR 231 -1.09 PRO 98
ASN 200 0.59 ILE 232 -1.14 PRO 98
TYR 205 0.51 HIS 233 -1.03 PRO 98
TYR 205 0.55 TYR 234 -0.90 PRO 98
TYR 205 0.62 ASN 235 -0.77 PRO 98
ASP 207 0.51 TYR 236 -0.67 VAL 97
ASP 207 0.76 MET 237 -0.75 VAL 97
ASP 207 0.69 CYS 238 -0.64 VAL 97
ASP 207 0.69 CYS 238 -0.63 VAL 97
ASP 207 0.54 ASN 239 -0.53 VAL 97
ASP 207 0.35 SER 240 -0.44 SER 99
PHE 212 0.47 SER 241 -0.38 SER 99
PHE 212 0.61 CYS 242 -0.45 VAL 97
PHE 212 0.41 MET 243 -0.45 SER 99
HIS 168 0.28 GLY 244 -0.42 SER 99
PHE 212 0.36 GLY 245 -0.35 SER 99
PRO 98 0.38 MET 246 -0.30 SER 99
PRO 98 0.39 ASN 247 -0.36 SER 96
PRO 98 0.23 ARG 248 -0.36 SER 96
PRO 98 0.25 SER 249 -0.43 SER 99
MET 169 0.16 PRO 250 -0.47 SER 99
THR 170 0.16 ILE 251 -0.60 SER 99
ILE 195 0.17 LEU 252 -0.70 ARG 213
ILE 195 0.23 THR 253 -0.61 ARG 213
THR 170 0.18 ILE 254 -0.89 ARG 213
THR 170 0.18 ILE 254 -0.89 ARG 213
VAL 216 0.15 ILE 255 -0.76 ASP 208
GLN 100 0.29 THR 256 -0.89 ASP 208
GLN 100 0.29 THR 256 -0.89 ASP 208
GLN 100 0.23 LEU 257 -0.96 ASP 208
GLN 100 0.21 GLU 258 -0.98 PRO 98
GLN 100 0.17 ASP 259 -1.06 PRO 98
GLN 100 0.14 SER 260 -1.19 PRO 98
GLN 100 0.13 SER 261 -1.06 LEU 206
GLN 100 0.16 GLY 262 -1.35 LEU 206
GLN 100 0.19 ASN 263 -1.35 ASP 207
GLN 100 0.25 LEU 264 -1.30 ASP 207
GLN 100 0.19 LEU 265 -1.25 ASP 208
GLN 100 0.19 GLY 266 -1.31 ASP 208
GLN 100 0.19 ARG 267 -1.19 ASP 208
ASN 200 0.21 ASN 268 -1.08 ASP 208
THR 170 0.19 SER 269 -0.85 ASP 208
ASN 200 0.26 PHE 270 -0.73 THR 211
ASN 200 0.21 GLU 271 -0.67 SER 96
TYR 205 0.26 VAL 272 -0.54 SER 96
TYR 205 0.26 VAL 272 -0.54 SER 96
TYR 205 0.22 ARG 273 -0.49 SER 96
ASP 207 0.37 VAL 274 -0.47 VAL 97
ASP 207 0.40 CYS 275 -0.46 VAL 97
ASP 207 0.47 ALA 276 -0.52 VAL 97
ASP 207 0.36 CYS 277 -0.47 SER 96
ASP 207 0.36 CYS 277 -0.46 SER 96
ASP 207 0.28 PRO 278 -0.55 SER 96
TYR 205 0.23 GLY 279 -0.65 SER 96
ASP 207 0.23 ARG 280 -0.63 SER 96
ASP 207 0.20 ASP 281 -0.64 SER 96
TYR 205 0.19 ARG 282 -0.76 SER 96
TYR 205 0.17 ARG 283 -0.81 SER 96
GLN 167 0.17 THR 284 -0.77 SER 96
GLN 165 0.19 GLU 285 -0.83 SER 96
GLN 165 0.17 GLU 286 -0.96 SER 96
GLN 165 0.17 GLU 287 -0.94 SER 96

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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.