CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402142129462809764

---  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
SER 99 0.46 SER 96 -1.68 ARG 156
THR 211 0.91 VAL 97 -1.75 LEU 265
ASN 210 1.02 PRO 98 -1.63 ARG 158
SER 166 0.69 SER 99 -1.69 ASP 148
ASP 208 0.87 GLN 100 -0.60 PHE 270
ARG 209 0.87 LYS 101 -0.75 ASN 131
ASN 210 0.62 THR 102 -0.63 VAL 97
ARG 209 0.48 TYR 103 -1.00 VAL 97
ARG 209 0.27 GLN 104 -1.03 VAL 97
THR 230 0.48 GLY 105 -1.30 VAL 97
THR 230 0.51 SER 106 -1.30 VAL 97
THR 230 0.51 TYR 107 -1.33 SER 99
ALA 129 0.54 GLY 108 -1.22 SER 99
PRO 128 0.52 PHE 109 -1.16 SER 99
ASN 131 0.69 ARG 110 -0.93 SER 99
ASN 131 0.84 LEU 111 -0.82 ASN 200
PRO 128 0.95 GLY 112 -0.82 ASN 200
TYR 220 1.07 PHE 113 -0.61 PRO 98
SER 227 1.53 LEU 114 -0.53 PRO 98
GLY 226 1.38 VAL 122 -0.33 PRO 98
TYR 220 1.34 THR 123 -0.36 PRO 98
TYR 220 1.37 CYS 124 -0.40 PRO 98
TYR 220 1.21 THR 125 -0.41 LYS 101
SER 227 1.04 TYR 126 -0.51 LYS 101
SER 227 0.95 SER 127 -0.56 LYS 101
GLY 112 0.95 PRO 128 -0.66 LYS 101
ASP 148 0.82 ALA 129 -0.63 LYS 101
SER 227 0.73 LEU 130 -0.65 LYS 101
LEU 111 0.84 ASN 131 -0.75 LYS 101
TYR 220 0.79 LYS 132 -0.57 LYS 101
TYR 220 0.97 MET 133 -0.45 LYS 101
TYR 220 0.97 MET 133 -0.45 LYS 101
TYR 220 1.02 PHE 134 -0.37 LYS 101
TYR 220 1.14 CYS 135 -0.35 PRO 98
TYR 220 1.11 GLN 136 -0.32 PRO 98
TYR 220 0.99 LEU 137 -0.33 GLU 221
TYR 220 1.05 ALA 138 -0.40 PRO 98
TYR 220 1.30 LYS 139 -0.43 PRO 98
TYR 220 1.51 THR 140 -0.51 PRO 98
TYR 220 1.39 CYS 141 -0.56 PRO 98
TYR 220 1.39 CYS 141 -0.56 PRO 98
TYR 220 1.41 PRO 142 -0.63 PRO 98
VAL 157 1.01 VAL 143 -0.76 ASN 200
LEU 257 0.97 GLN 144 -1.02 ASN 200
LEU 257 0.93 LEU 145 -1.23 ASN 200
PRO 128 0.81 TRP 146 -1.26 SER 99
PRO 128 0.70 VAL 147 -1.65 SER 99
ALA 129 0.82 ASP 148 -1.69 SER 99
ALA 129 0.55 SER 149 -1.57 SER 99
LEU 114 0.42 THR 150 -1.56 PRO 219
GLU 224 1.28 PRO 151 -1.22 SER 96
PRO 223 1.31 PRO 152 -1.17 SER 96
GLU 224 1.09 PRO 153 -1.09 SER 96
GLU 224 1.15 GLY 154 -1.19 SER 96
GLU 224 1.39 THR 155 -1.46 SER 96
THR 231 1.34 ARG 156 -1.68 SER 96
ILE 232 1.55 VAL 157 -1.43 PRO 98
ILE 232 0.60 ARG 158 -1.63 PRO 98
ILE 232 0.30 ALA 159 -1.20 PRO 98
ASP 208 0.32 MET 160 -0.95 GLU 221
THR 211 0.39 ALA 161 -0.80 GLU 221
THR 211 0.52 ILE 162 -0.80 GLY 262
THR 211 0.43 TYR 163 -0.89 GLY 262
THR 211 0.41 LYS 164 -0.84 GLY 262
SER 99 0.49 GLN 165 -1.10 GLY 262
SER 99 0.69 SER 166 -1.35 ASN 263
SER 99 0.69 SER 166 -1.35 ASN 263
ASN 247 0.70 GLN 167 -1.60 GLY 262
GLY 245 0.74 HIS 168 -1.57 GLY 262
GLY 245 0.45 MET 169 -1.43 GLY 262
GLY 245 0.49 THR 170 -1.64 GLU 258
GLY 245 0.68 GLU 171 -1.52 GLY 262
VAL 97 0.64 VAL 172 -1.03 GLY 262
VAL 97 0.35 VAL 173 -0.78 GLY 262
VAL 97 0.40 ARG 174 -0.67 THR 150
GLY 226 0.41 ARG 175 -0.57 THR 150
GLU 171 0.47 CYS 176 -0.52 THR 150
VAL 97 0.47 PRO 177 -0.54 THR 150
GLY 226 0.48 HIS 178 -0.45 THR 150
TYR 220 0.54 HIS 179 -0.45 THR 150
LEU 201 0.51 GLU 180 -0.55 THR 150
LEU 201 0.57 ARG 181 -0.51 THR 150
LEU 201 1.01 SER 185 -0.42 THR 150
LEU 201 1.27 ASP 186 -0.37 SER 99
LEU 201 1.45 GLY 187 -0.46 THR 150
VAL 203 1.34 LEU 188 -0.55 THR 150
VAL 203 1.03 ALA 189 -0.60 THR 150
LEU 201 0.61 PRO 190 -0.72 THR 150
LEU 201 0.63 PRO 191 -0.62 THR 150
LEU 201 0.44 GLN 192 -0.69 THR 150
VAL 218 0.44 HIS 193 -0.69 THR 150
TYR 220 0.49 LEU 194 -0.66 GLU 221
VAL 218 0.66 ILE 195 -0.75 GLU 221
VAL 218 1.01 ARG 196 -0.70 GLU 221
VAL 218 1.58 VAL 197 -0.71 PRO 98
VAL 218 1.19 GLU 198 -0.69 SER 99
PRO 219 1.15 GLY 199 -0.83 SER 99
ASP 186 1.16 ASN 200 -1.26 THR 230
GLY 187 1.45 LEU 201 -1.50 PRO 223
LEU 188 1.09 ARG 202 -1.27 PRO 222
LEU 188 1.34 VAL 203 -1.19 GLU 221
LEU 188 0.57 GLU 204 -1.00 GLU 221
LYS 101 0.34 TYR 205 -0.97 GLU 221
LYS 101 0.63 LEU 206 -0.94 THR 150
LYS 101 0.62 ASP 207 -0.99 THR 150
GLN 100 0.87 ASP 208 -1.17 THR 150
LYS 101 0.87 ARG 209 -1.11 THR 150
PRO 98 1.02 ASN 210 -1.19 THR 150
VAL 97 0.91 THR 211 -1.18 THR 150
VAL 97 0.78 PHE 212 -1.04 THR 150
GLN 100 0.44 ARG 213 -1.03 THR 150
GLN 100 0.33 HIS 214 -0.93 THR 150
GLN 100 0.39 SER 215 -1.03 GLU 221
ALA 189 0.57 VAL 216 -1.27 GLU 221
ALA 189 0.52 VAL 217 -1.45 GLU 221
VAL 197 1.58 VAL 218 -1.39 SER 99
HIS 233 1.33 PRO 219 -1.56 THR 150
THR 140 1.51 TYR 220 -1.26 SER 96
ASP 259 1.62 GLU 221 -1.58 PRO 98
ASP 259 1.20 PRO 222 -1.57 SER 99
THR 155 1.36 PRO 223 -1.50 LEU 201
THR 155 1.39 GLU 224 -1.32 SER 99
PRO 151 1.16 VAL 225 -1.28 SER 99
VAL 122 1.38 GLY 226 -1.00 SER 99
LEU 114 1.53 SER 227 -1.08 SER 99
LEU 114 1.30 ASP 228 -1.23 SER 99
THR 155 1.05 CYS 229 -1.09 LEU 201
LEU 257 1.29 THR 230 -1.26 ASN 200
ARG 156 1.34 THR 231 -1.04 ASN 200
VAL 157 1.55 ILE 232 -0.95 ASN 200
VAL 157 1.34 HIS 233 -0.66 PRO 98
VAL 157 1.18 TYR 234 -0.66 PRO 98
TYR 220 1.03 ASN 235 -0.53 PRO 98
TYR 220 0.85 TYR 236 -0.53 GLU 221
TYR 220 0.75 MET 237 -0.48 GLU 221
TYR 220 0.67 CYS 238 -0.46 GLU 221
TYR 220 0.67 CYS 238 -0.47 GLU 221
TYR 220 0.72 ASN 239 -0.40 GLU 221
GLY 226 0.64 SER 240 -0.46 GLY 262
GLY 226 0.64 SER 241 -0.47 GLY 262
GLY 226 0.56 CYS 242 -0.51 GLY 262
GLU 171 0.60 MET 243 -0.62 GLY 262
HIS 168 0.66 GLY 244 -0.71 GLY 262
HIS 168 0.74 GLY 245 -0.72 GLY 262
HIS 168 0.69 MET 246 -0.71 GLY 262
HIS 168 0.72 ASN 247 -0.71 GLY 262
HIS 168 0.63 ARG 248 -0.63 GLY 262
HIS 168 0.65 SER 249 -0.73 GLY 262
GLY 226 0.54 PRO 250 -0.64 GLY 262
GLY 226 0.45 ILE 251 -0.62 GLY 262
SER 227 0.40 LEU 252 -0.63 GLU 221
TYR 220 0.41 THR 253 -0.75 GLU 221
ASP 208 0.42 ILE 254 -0.86 GLU 221
ASP 208 0.42 ILE 254 -0.86 GLU 221
ILE 232 0.44 ILE 255 -1.29 PRO 98
ILE 232 0.78 THR 256 -1.36 PRO 98
ILE 232 0.78 THR 256 -1.37 PRO 98
ILE 232 1.33 LEU 257 -1.51 SER 96
THR 230 1.12 GLU 258 -1.64 THR 170
GLU 221 1.62 ASP 259 -1.40 THR 170
GLU 221 1.41 SER 260 -1.23 THR 170
GLU 221 0.93 SER 261 -1.31 GLN 167
GLU 221 0.68 GLY 262 -1.60 GLN 167
THR 230 0.70 ASN 263 -1.55 GLN 167
THR 230 0.79 LEU 264 -1.40 VAL 97
THR 230 1.07 LEU 265 -1.75 VAL 97
THR 230 0.74 GLY 266 -1.55 VAL 97
ILE 232 0.40 ARG 267 -1.11 VAL 97
ASN 210 0.35 ASN 268 -0.75 GLU 221
ASN 210 0.46 SER 269 -0.77 GLU 221
LEU 111 0.71 PHE 270 -0.60 GLN 100
TYR 220 0.62 GLU 271 -0.52 LYS 101
TYR 220 0.77 VAL 272 -0.42 GLU 221
TYR 220 0.77 VAL 272 -0.42 GLU 221
TYR 220 0.81 ARG 273 -0.36 GLU 221
TYR 220 0.88 VAL 274 -0.37 GLU 221
TYR 220 0.90 CYS 275 -0.28 GLU 221
GLY 226 0.95 ALA 276 -0.24 LYS 101
GLY 226 1.04 CYS 277 -0.28 LYS 101
GLY 226 1.05 CYS 277 -0.28 LYS 101
GLY 226 1.06 PRO 278 -0.33 LYS 101
GLY 226 1.17 GLY 279 -0.36 LYS 101
GLY 226 1.06 ARG 280 -0.34 LYS 101
GLY 226 0.94 ASP 281 -0.37 LYS 101
GLY 226 0.97 ARG 282 -0.44 LYS 101
GLY 226 1.00 ARG 283 -0.42 LYS 101
GLY 226 0.90 THR 284 -0.38 LYS 101
GLY 226 0.82 GLU 285 -0.43 LYS 101
GLY 226 0.87 GLU 286 -0.47 LYS 101
GLY 226 0.86 GLU 287 -0.41 LYS 101

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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.