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CA distance fluctuations for 2404250151202365723

---  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
ASN 263 0.65 SER 96 -0.84 ASN 288
ASN 263 0.72 VAL 97 -0.94 GLU 285
GLY 105 0.65 PRO 98 -1.52 ILE 162
SER 166 0.84 SER 99 -1.61 ALA 159
PHE 113 0.55 GLN 100 -1.26 GLU 285
PHE 113 0.64 LYS 101 -1.23 GLU 285
PHE 113 0.45 THR 102 -1.62 GLU 285
PRO 98 0.63 TYR 103 -1.53 LEU 130
PRO 98 0.45 GLN 104 -1.79 LEU 130
PRO 98 0.65 GLY 105 -1.77 LEU 130
PRO 98 0.58 SER 106 -1.68 LEU 289
ARG 213 0.45 TYR 107 -1.78 ALA 129
PRO 98 0.35 GLY 108 -1.70 ALA 129
ARG 213 0.29 PHE 109 -1.51 ASN 131
PRO 223 0.42 ARG 110 -1.64 ASN 131
CYS 229 0.56 LEU 111 -1.32 ASN 131
CYS 229 0.69 GLY 112 -1.21 SER 127
PHE 270 1.37 PHE 113 -0.64 PRO 128
PHE 270 0.88 LEU 114 -0.46 SER 183
ASP 228 0.95 HIS 115 -0.50 ASP 148
SER 227 1.03 SER 116 -0.42 SER 183
GLY 226 0.93 GLY 117 -0.57 ARG 110
GLY 226 0.80 THR 118 -0.61 PRO 98
GLY 226 0.93 ALA 119 -0.55 PRO 98
GLY 226 0.84 LYS 120 -0.56 PRO 98
GLY 226 0.97 SER 121 -0.56 ALA 276
GLY 226 0.91 VAL 122 -0.48 PRO 98
GLY 226 0.78 THR 123 -0.51 PRO 98
SER 227 0.72 CYS 124 -0.53 PRO 98
GLY 226 0.63 THR 125 -0.67 LEU 111
GLY 226 0.41 TYR 126 -1.18 LEU 111
ARG 248 0.49 SER 127 -1.52 ARG 110
ARG 248 0.49 PRO 128 -1.74 TRP 146
ARG 248 0.67 ALA 129 -1.78 TYR 107
ARG 248 0.84 LEU 130 -1.79 GLN 104
ARG 248 0.64 ASN 131 -1.64 ARG 110
PRO 250 0.52 LYS 132 -0.96 ARG 110
SER 227 0.45 MET 133 -0.84 LEU 111
SER 227 0.45 MET 133 -0.84 LEU 111
GLY 226 0.45 PHE 134 -0.85 PRO 98
GLY 262 0.54 CYS 135 -0.73 PRO 98
GLY 262 0.71 GLN 136 -0.64 PRO 98
GLY 262 0.82 LEU 137 -0.66 PRO 98
GLY 262 0.92 ALA 138 -0.70 SER 183
ARG 158 0.81 LYS 139 -0.73 SER 183
ARG 158 0.98 THR 140 -0.78 SER 183
ARG 158 0.95 CYS 141 -0.67 ASP 184
ARG 158 0.95 CYS 141 -0.67 ASP 184
ARG 158 0.98 PRO 142 -0.67 ASP 184
ILE 255 1.28 VAL 143 -0.87 TYR 126
ILE 255 0.95 GLN 144 -1.12 PRO 128
ILE 255 0.66 LEU 145 -1.45 PRO 128
PRO 223 0.51 TRP 146 -1.74 PRO 128
PRO 222 0.58 VAL 147 -1.68 ALA 129
PRO 222 0.50 ASP 148 -1.71 ALA 129
TYR 220 0.39 SER 149 -1.72 ALA 129
TYR 220 0.36 THR 150 -1.61 ALA 129
GLU 204 0.54 PRO 151 -1.45 ALA 129
GLU 204 0.51 PRO 152 -1.29 ALA 129
GLU 204 0.49 PRO 153 -1.30 ASP 228
GLU 204 0.85 GLY 154 -1.13 LEU 289
GLU 204 0.78 THR 155 -1.19 LEU 289
ILE 232 0.78 ARG 156 -0.94 LEU 289
ILE 232 1.24 VAL 157 -1.23 SER 99
HIS 233 1.33 ARG 158 -1.32 SER 99
TYR 234 1.21 ALA 159 -1.61 SER 99
GLY 262 0.74 MET 160 -1.14 SER 99
GLY 262 0.70 ALA 161 -1.51 PRO 98
PHE 113 0.63 ILE 162 -1.52 PRO 98
PHE 113 0.60 TYR 163 -1.24 PRO 98
PHE 113 0.72 LYS 164 -1.02 PRO 98
PHE 113 0.63 GLN 165 -0.69 THR 284
SER 99 0.84 SER 166 -0.67 THR 284
SER 99 0.76 GLN 167 -0.54 THR 284
GLY 262 0.51 HIS 168 -0.58 PRO 98
PHE 113 0.56 MET 169 -0.59 THR 284
ASN 263 0.57 THR 170 -0.77 THR 211
ASN 263 0.69 GLU 171 -0.56 PRO 98
ASN 263 0.87 VAL 172 -0.62 PRO 98
GLY 262 0.90 VAL 173 -0.99 PRO 98
GLY 262 1.05 ARG 174 -0.78 PRO 98
GLY 262 1.04 ARG 175 -0.71 PRO 98
GLY 262 0.94 CYS 176 -0.58 PRO 98
GLY 262 0.95 PRO 177 -0.44 PRO 98
GLY 262 0.89 HIS 178 -0.47 PRO 98
GLY 262 0.98 HIS 179 -0.57 PRO 98
GLY 262 1.06 GLU 180 -0.52 PRO 98
SER 261 1.02 ARG 181 -0.41 PRO 98
SER 261 0.92 CYS 182 -0.66 ALA 138
SER 261 0.97 SER 183 -0.78 THR 140
SER 261 0.71 ASP 184 -1.13 GLU 198
GLY 262 0.97 SER 185 -0.48 PRO 223
GLY 262 0.89 ASP 186 -0.57 PRO 223
SER 261 0.93 GLY 187 -0.54 SER 99
GLY 262 1.04 LEU 188 -0.66 SER 99
GLY 262 1.32 ALA 189 -0.67 SER 99
GLY 262 1.46 PRO 190 -0.57 SER 99
GLY 262 1.27 PRO 191 -0.52 PRO 98
GLY 262 1.27 GLN 192 -0.57 PRO 98
GLY 262 1.32 HIS 193 -0.74 PRO 98
GLY 262 1.10 LEU 194 -0.92 PRO 98
GLY 262 1.09 ILE 195 -0.91 PRO 98
GLY 262 1.08 ARG 196 -0.82 ASP 184
VAL 217 1.14 VAL 197 -0.95 ASP 184
VAL 217 0.92 GLU 198 -1.13 ASP 184
SER 121 0.70 GLY 199 -0.83 ASP 184
GLY 262 0.54 ASN 200 -0.92 PRO 223
GLY 262 0.63 LEU 201 -0.95 PRO 223
SER 260 0.65 ARG 202 -0.83 GLU 221
GLY 262 0.85 VAL 203 -0.93 SER 99
SER 260 1.16 GLU 204 -0.83 SER 99
GLY 262 1.47 TYR 205 -0.81 SER 99
GLY 262 1.64 LEU 206 -0.82 SER 99
GLY 262 1.55 ASP 207 -0.66 SER 99
ASN 263 1.52 ASP 208 -0.83 SER 99
SER 261 1.30 ARG 209 -0.70 SER 99
ASN 263 1.08 ASN 210 -0.76 ASN 288
ASN 263 1.19 THR 211 -0.77 THR 170
ASN 263 1.18 PHE 212 -0.50 ASN 288
ASN 263 1.15 ARG 213 -0.51 GLU 285
GLY 262 1.21 HIS 214 -0.58 PRO 98
GLY 262 1.11 SER 215 -0.91 SER 99
GLY 262 1.12 VAL 216 -1.06 SER 99
VAL 197 1.14 VAL 217 -1.13 SER 99
GLU 198 0.82 VAL 218 -1.06 SER 99
HIS 233 0.68 PRO 219 -0.92 SER 99
PRO 151 0.51 TYR 220 -1.10 PRO 128
VAL 147 0.55 GLU 221 -0.88 PRO 128
VAL 147 0.58 PRO 222 -0.97 PRO 128
TRP 146 0.51 PRO 223 -0.95 LEU 201
SER 121 0.49 GLU 224 -0.77 LEU 201
SER 121 0.63 VAL 225 -0.91 PRO 153
SER 116 0.99 GLY 226 -0.98 PRO 153
SER 116 1.03 SER 227 -1.04 PRO 153
HIS 115 0.95 ASP 228 -1.30 PRO 153
GLY 112 0.69 CYS 229 -1.14 PRO 128
SER 121 0.43 THR 230 -1.10 PRO 128
ARG 158 0.82 THR 231 -0.95 PRO 128
ARG 158 1.28 ILE 232 -0.83 PRO 128
ARG 158 1.33 HIS 233 -0.89 ASP 184
ARG 158 1.28 TYR 234 -0.91 ASP 184
GLY 262 0.90 ASN 235 -0.97 ASP 184
GLY 262 0.90 TYR 236 -0.75 PRO 98
GLY 262 0.97 MET 237 -0.77 PRO 98
GLY 262 0.88 CYS 238 -0.82 PRO 98
GLY 262 0.74 ASN 239 -0.84 PRO 98
GLY 262 0.67 SER 240 -0.90 PRO 98
LEU 130 0.80 SER 241 -0.74 PRO 98
GLY 262 0.76 CYS 242 -0.68 PRO 98
GLY 262 0.73 MET 243 -0.57 PRO 98
GLY 262 0.79 GLY 244 -0.50 PRO 98
GLY 262 0.84 GLY 245 -0.66 PRO 98
GLY 262 0.76 MET 246 -0.83 PRO 98
LEU 130 0.72 ASN 247 -0.70 PRO 98
LEU 130 0.84 ARG 248 -0.78 PRO 98
LEU 130 0.64 ARG 249 -0.90 PRO 98
PHE 113 0.60 PRO 250 -1.06 PRO 98
PHE 113 0.66 ILE 251 -1.38 PRO 98
PHE 113 0.87 LEU 252 -1.39 PRO 98
PHE 113 0.88 THR 253 -1.26 PRO 98
VAL 143 1.08 ILE 254 -1.29 SER 99
VAL 143 1.28 ILE 255 -1.60 SER 99
ILE 232 0.87 THR 256 -1.14 SER 99
ILE 232 0.55 LEU 257 -1.14 LEU 289
SER 215 0.87 GLU 258 -1.21 LEU 289
LEU 206 0.99 ASP 259 -1.34 LEU 289
LEU 206 1.17 SER 260 -1.15 LEU 289
PRO 190 1.32 SER 261 -1.07 LEU 289
LEU 206 1.64 GLY 262 -1.04 LEU 289
ASP 208 1.52 ASN 263 -1.35 LEU 289
ARG 213 1.08 LEU 264 -1.43 LEU 289
ARG 213 0.73 LEU 265 -1.50 LEU 289
ARG 213 0.59 GLY 266 -1.42 LEU 130
VAL 143 0.50 ARG 267 -1.27 GLU 285
VAL 143 0.62 ASN 268 -1.28 GLU 285
PHE 113 0.99 SER 269 -1.10 GLU 285
PHE 113 1.37 PHE 270 -0.99 PRO 98
PHE 113 0.95 GLU 271 -0.99 PRO 98
PHE 113 0.66 VAL 272 -1.05 PRO 98
GLY 262 0.50 ARG 273 -0.95 PRO 98
GLY 262 0.62 VAL 274 -0.91 PRO 98
GLY 262 0.57 CYS 275 -0.83 PRO 98
ASP 186 0.68 ALA 276 -0.68 PRO 98
ASP 186 0.63 CYS 277 -0.75 PRO 98
ASP 186 0.63 CYS 277 -0.75 PRO 98
GLY 226 0.60 PRO 278 -0.78 PRO 98
GLY 226 0.70 GLY 279 -0.72 PRO 98
GLY 226 0.60 ARG 280 -0.79 PRO 98
GLY 226 0.47 ASP 281 -0.94 PRO 98
LEU 130 0.45 ARG 282 -0.96 ARG 110
GLY 226 0.48 ARG 283 -0.90 GLN 104
GLY 226 0.31 THR 284 -1.13 THR 102
GLU 286 0.21 GLU 285 -1.62 THR 102
SER 241 0.26 GLU 286 -1.64 GLN 104
ALA 276 0.16 GLU 287 -1.34 TYR 103
MET 243 0.14 ASN 288 -1.41 GLY 105
MET 243 0.18 LEU 289 -1.68 SER 106

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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.