CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404210115201599106

---  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
GLU 286 0.96 VAL 97 -0.45 SER 215
GLU 285 0.83 PRO 98 -0.50 SER 215
ASN 210 1.03 SER 99 -0.71 SER 166
ASN 210 0.85 GLN 100 -0.77 SER 166
ASN 210 0.94 LYS 101 -0.90 SER 166
ASN 210 0.86 THR 102 -0.68 SER 166
ASN 210 0.92 TYR 103 -0.64 SER 166
ASN 210 0.82 GLN 104 -0.55 ALA 129
ASN 210 0.87 GLY 105 -0.53 SER 166
ASN 210 0.80 SER 106 -0.48 ALA 129
ASN 210 0.80 SER 106 -0.48 ALA 129
ASN 210 0.72 TYR 107 -0.57 ALA 129
ASN 210 0.71 GLY 108 -0.68 ALA 129
ASN 210 0.71 PHE 109 -0.67 ALA 129
ASN 210 0.65 ARG 110 -0.79 ALA 129
ASN 210 0.55 LEU 111 -0.82 SER 127
ASN 210 0.46 GLY 112 -1.00 SER 127
LYS 132 0.78 PHE 113 -0.63 SER 127
LYS 132 0.50 LEU 114 -0.55 ARG 283
LYS 132 0.40 HIS 115 -0.58 ARG 283
GLY 226 0.46 SER 116 -0.55 ARG 283
GLY 226 0.39 VAL 122 -0.57 THR 123
GLY 226 0.59 THR 123 -0.57 VAL 122
GLY 226 0.46 CYS 124 -0.32 GLY 279
PRO 250 0.33 THR 125 -0.44 ASP 228
PRO 250 0.34 THR 125 -0.44 ASP 228
LYS 132 0.33 TYR 126 -0.50 ASP 228
GLY 279 0.67 SER 127 -1.00 GLY 112
ASN 210 0.44 PRO 128 -0.73 ASP 228
GLY 279 0.67 ALA 129 -0.90 ASP 228
ASN 210 0.65 LEU 130 -0.99 ASP 281
ASN 210 0.53 ASN 131 -0.50 ASP 281
ASN 210 0.54 ASN 131 -0.50 ASP 281
PHE 113 0.78 LYS 132 -0.56 ASP 281
LYS 132 0.37 MET 133 -0.34 ASP 228
PRO 250 0.43 PHE 134 -0.30 ASP 228
GLY 226 0.49 CYS 135 -0.21 LEU 130
GLY 226 0.62 GLN 136 -0.22 GLY 279
GLY 226 0.67 LEU 137 -0.25 VAL 122
GLY 226 0.79 ALA 138 -0.32 VAL 122
GLY 226 0.83 LYS 139 -0.41 VAL 122
GLY 226 0.83 LYS 139 -0.41 VAL 122
GLY 226 0.84 THR 140 -0.44 VAL 122
GLY 226 0.61 CYS 141 -0.25 SER 127
GLY 226 0.61 CYS 141 -0.25 SER 127
GLY 226 0.52 PRO 142 -0.35 ARG 283
LYS 132 0.51 VAL 143 -0.47 SER 127
ASN 210 0.35 GLN 144 -0.64 SER 127
ASN 210 0.50 LEU 145 -0.66 SER 127
ASN 210 0.52 TRP 146 -0.75 SER 127
ASN 210 0.60 VAL 147 -0.71 ALA 129
ASN 210 0.60 ASP 148 -0.73 ALA 129
ASN 210 0.61 SER 149 -0.61 ALA 129
ASN 210 0.58 THR 150 -0.54 ALA 129
ASN 210 0.64 PRO 151 -0.48 ALA 129
ASN 210 0.60 PRO 152 -0.41 ALA 129
ASN 210 0.59 PRO 152 -0.41 SER 127
ASN 210 0.55 PRO 153 -0.37 SER 127
ASN 210 0.52 PRO 153 -0.39 SER 127
ARG 209 0.58 GLY 154 -0.33 SER 127
ARG 209 0.56 GLY 154 -0.34 SER 127
ASN 210 0.64 THR 155 -0.38 SER 127
ASN 210 0.60 ARG 156 -0.38 GLN 144
ASN 210 0.58 VAL 157 -0.43 GLN 144
ASN 210 0.56 ARG 158 -0.37 PRO 98
GLU 285 0.55 ALA 159 -0.30 PRO 98
GLU 285 0.70 MET 160 -0.25 MET 169
GLU 285 0.75 ALA 161 -0.30 TYR 236
GLU 285 0.84 ILE 162 -0.27 GLN 100
THR 284 0.90 TYR 163 -0.43 LYS 101
ARG 283 0.82 LYS 164 -0.42 LYS 101
ARG 283 1.12 GLN 165 -0.53 LYS 101
ARG 283 1.32 SER 166 -0.90 LYS 101
THR 284 1.37 GLN 167 -0.66 LYS 101
THR 284 1.37 GLN 167 -0.66 LYS 101
THR 284 1.26 HIS 168 -0.51 LYS 101
THR 284 1.12 MET 169 -0.66 GLN 100
GLU 285 1.18 THR 170 -0.41 SER 99
GLU 285 1.25 GLU 171 -0.29 LYS 101
GLU 285 1.17 VAL 172 -0.19 GLN 100
GLU 285 1.04 VAL 173 -0.22 GLN 100
GLU 285 1.05 ARG 174 -0.34 PHE 212
GLU 285 0.99 ARG 175 -0.36 PHE 212
GLU 285 0.99 ARG 175 -0.36 PHE 212
GLU 285 1.07 CYS 176 -0.39 ARG 209
GLU 285 1.13 PRO 177 -0.53 ASN 210
GLU 285 0.97 HIS 178 -0.45 ASN 210
GLU 285 0.87 HIS 179 -0.40 ARG 209
GLU 285 0.97 GLU 180 -0.52 ARG 209
GLU 285 0.94 ARG 181 -0.56 ARG 209
GLU 285 0.79 CYS 182 -0.44 ARG 209
GLU 285 0.79 CYS 182 -0.44 ARG 209
GLY 226 0.75 GLY 187 -0.60 ARG 209
GLY 226 0.70 LEU 188 -0.46 ARG 209
GLU 285 0.74 ALA 189 -0.42 ARG 209
GLU 285 0.87 PRO 190 -0.56 ARG 209
GLU 285 0.92 PRO 191 -0.51 ARG 209
GLU 285 1.02 GLN 192 -0.55 PHE 212
GLU 285 0.90 HIS 193 -0.40 PHE 212
GLU 285 0.80 LEU 194 -0.30 PHE 212
GLU 285 0.66 ILE 195 -0.18 PHE 212
GLY 226 0.65 ARG 196 -0.23 VAL 122
GLY 226 0.71 VAL 197 -0.25 VAL 122
GLY 226 0.93 GLU 198 -0.30 VAL 122
VAL 225 1.06 GLY 199 -0.35 ARG 283
GLU 224 0.95 ASN 200 -0.30 ARG 283
VAL 225 0.87 LEU 201 -0.26 ARG 283
GLU 224 0.64 ARG 202 -0.28 PRO 98
VAL 225 0.59 VAL 203 -0.30 PRO 98
GLU 285 0.64 GLU 204 -0.37 PRO 98
GLU 285 0.76 TYR 205 -0.36 PRO 98
GLU 285 0.85 LEU 206 -0.42 PRO 98
GLU 285 0.98 ASP 207 -0.37 LEU 188
GLU 285 0.94 ASP 208 -0.36 GLY 187
ASN 263 1.09 ARG 209 -0.60 GLY 187
LEU 264 1.10 ASN 210 -0.54 ARG 181
GLU 285 1.09 THR 211 -0.26 ASP 208
GLU 285 1.09 PHE 212 -0.55 GLN 192
GLU 285 1.04 ARG 213 -0.38 VAL 97
GLU 285 0.94 HIS 214 -0.40 VAL 97
GLU 285 0.78 SER 215 -0.49 PRO 98
GLU 285 0.78 SER 215 -0.50 PRO 98
GLU 285 0.66 VAL 216 -0.38 PRO 98
GLU 285 0.56 VAL 217 -0.38 PRO 98
GLU 224 0.44 VAL 218 -0.31 SER 127
ASN 210 0.43 PRO 219 -0.38 SER 127
ASN 210 0.51 TYR 220 -0.44 SER 127
ASN 210 0.47 GLU 221 -0.45 SER 127
ASN 200 0.48 PRO 222 -0.52 SER 127
GLY 199 0.61 PRO 223 -0.63 ARG 283
GLY 199 0.97 GLU 224 -0.71 ARG 283
GLY 199 1.06 VAL 225 -0.63 ARG 283
GLY 199 1.05 GLY 226 -0.62 GLU 286
GLY 199 0.59 SER 227 -0.85 ARG 283
GLY 199 0.43 ASP 228 -0.90 ALA 129
ASN 210 0.44 CYS 229 -0.78 SER 127
GLY 199 0.49 THR 230 -0.60 SER 127
GLY 226 0.44 THR 231 -0.49 SER 127
GLY 226 0.48 ILE 232 -0.36 SER 127
GLY 226 0.72 HIS 233 -0.29 ARG 283
GLY 226 0.62 TYR 234 -0.22 VAL 122
GLY 226 0.71 ASN 235 -0.27 VAL 122
GLY 226 0.61 TYR 236 -0.34 THR 253
GLU 285 0.65 MET 237 -0.27 PHE 212
GLU 285 0.73 CYS 238 -0.24 LEU 252
GLU 285 0.73 CYS 238 -0.24 LEU 252
ASP 281 0.76 ASN 239 -0.27 LEU 252
ASP 281 0.91 SER 240 -0.22 LEU 252
ASP 281 1.14 SER 241 -0.21 LYS 132
GLU 285 0.88 CYS 242 -0.22 ARG 209
THR 284 1.05 MET 243 -0.28 ASN 210
GLU 285 1.21 GLY 244 -0.38 ASN 210
GLU 285 1.10 GLY 245 -0.26 ASN 210
GLU 285 0.97 MET 246 -0.23 LYS 101
THR 284 1.03 ASN 247 -0.22 LYS 101
ASP 281 1.07 ARG 248 -0.23 LYS 101
ARG 282 1.00 ARG 249 -0.29 LYS 101
ARG 282 1.04 PRO 250 -0.27 LYS 101
ARG 282 0.69 ILE 251 -0.23 LYS 101
GLU 285 0.56 LEU 252 -0.31 TYR 236
GLU 285 0.56 LEU 252 -0.31 TYR 236
GLU 285 0.52 THR 253 -0.34 TYR 236
ASN 210 0.68 ILE 254 -0.35 SER 166
ASN 210 0.68 ILE 254 -0.35 SER 166
ASN 210 0.65 ILE 255 -0.35 SER 166
ASN 210 0.82 THR 256 -0.77 THR 256
ASN 210 0.82 THR 256 -0.77 THR 256
ASN 210 0.78 LEU 257 -0.38 SER 166
ASN 210 0.84 GLU 258 -0.39 PRO 98
ASN 210 0.84 GLU 258 -0.39 PRO 98
ARG 209 0.80 ASP 259 -0.35 PRO 98
ARG 209 0.74 SER 260 -0.33 PRO 98
ARG 209 0.93 SER 261 -0.36 PRO 98
ARG 209 1.06 GLY 262 -0.47 PRO 98
ARG 209 1.09 ASN 263 -0.47 PRO 98
ASN 210 1.10 LEU 264 -0.50 SER 166
ASN 210 0.94 LEU 265 -0.47 SER 166
ASN 210 0.90 GLY 266 -0.50 SER 166
ASN 210 0.90 ARG 267 -0.53 SER 166
ASN 210 0.75 ASN 268 -0.48 SER 166
ASN 210 0.67 SER 269 -0.40 SER 166
LYS 132 0.64 PHE 270 -0.25 SER 166
ASN 210 0.46 GLU 271 -0.22 ASP 228
ASN 210 0.46 GLU 271 -0.22 ASP 228
ARG 282 0.40 VAL 272 -0.23 CYS 275
ILE 195 0.44 ARG 273 -0.46 LYS 132
ASP 281 0.50 VAL 274 -0.26 LYS 132
ASP 281 0.66 CYS 275 -0.41 LYS 132
GLY 226 0.53 ALA 276 -0.34 LEU 130
GLY 226 0.42 CYS 277 -0.34 LEU 130
GLN 167 0.39 PRO 278 -0.33 LEU 130
SER 127 0.67 GLY 279 -0.51 THR 123
GLN 167 0.72 ARG 280 -0.40 ASP 228
SER 241 1.14 ASP 281 -0.99 LEU 130
PRO 250 1.04 ARG 282 -0.59 ASP 228
GLN 167 1.36 ARG 283 -0.85 SER 227
GLN 167 1.37 THR 284 -0.54 ASP 228
GLU 171 1.25 GLU 285 -0.38 ASP 228
GLN 167 1.21 GLU 286 -0.68 SER 227

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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.