CNRS Nantes University US2B US2B
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***  AF-1F0N_recycle_9  ***

CA distance fluctuations for 2402070233561794441

---  normal mode 10  ---

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
GLN 24 0.18 SER 1 -0.51 LEU 218
TYR 9 0.37 ARG 2 -0.66 LEU 218
TYR 9 0.75 PRO 3 -0.60 GLU 217
TYR 9 0.50 GLY 4 -0.51 LEU 218
VAL 7 0.24 LEU 5 -0.39 LEU 218
PRO 3 0.28 PRO 6 -0.32 LEU 218
PRO 3 0.57 VAL 7 -0.28 LEU 218
PRO 3 0.67 GLU 8 -0.25 LEU 218
PRO 3 0.75 TYR 9 -0.23 LEU 218
PRO 3 0.61 LEU 10 -0.21 ASN 222
PRO 3 0.61 GLN 11 -0.23 ASP 45
PRO 3 0.50 VAL 12 -0.21 ASN 222
PRO 3 0.48 PRO 13 -0.23 ALA 89
PRO 3 0.41 SER 14 -0.21 ALA 89
PRO 3 0.39 PRO 15 -0.22 ALA 89
TYR 82 0.42 SER 16 -0.21 GLN 140
PRO 3 0.38 MET 17 -0.22 ALA 89
PRO 3 0.41 GLY 18 -0.27 ALA 89
PRO 3 0.46 ARG 19 -0.30 ALA 89
PRO 3 0.51 ASP 20 -0.29 ALA 89
PRO 3 0.48 ILE 21 -0.23 ASP 45
PRO 3 0.55 LYS 22 -0.23 ASN 222
PRO 3 0.49 VAL 23 -0.21 ASN 222
PRO 3 0.52 GLN 24 -0.21 ASN 222
PRO 3 0.42 PHE 25 -0.20 LEU 218
PRO 3 0.33 GLN 26 -0.19 LEU 218
PRO 3 0.26 SER 27 -0.15 ASN 222
HIS 138 0.16 GLY 28 -0.14 PRO 257
PRO 3 0.17 GLY 29 -0.13 PRO 257
PRO 185 0.21 ASN 30 -0.11 ASN 222
PRO 185 0.23 ASN 31 -0.10 ASN 222
HIS 138 0.19 SER 32 -0.10 ASN 222
HIS 138 0.20 PRO 33 -0.09 PRO 224
PRO 3 0.21 ALA 34 -0.11 ASN 222
PRO 3 0.17 VAL 35 -0.10 ASN 222
PRO 3 0.21 TYR 36 -0.15 ASN 222
PRO 3 0.16 LEU 37 -0.16 ASN 222
PRO 3 0.17 LEU 38 -0.20 ASN 222
PRO 3 0.13 ASP 39 -0.23 ASN 222
VAL 232 0.17 GLY 40 -0.31 ASN 222
VAL 232 0.29 LEU 41 -0.43 ASN 222
PHE 231 0.30 ARG 42 -0.36 ASN 222
PHE 231 0.18 ALA 43 -0.29 ASN 222
PRO 3 0.20 GLN 44 -0.29 ALA 170
PRO 3 0.33 ASP 45 -0.23 GLN 11
PRO 3 0.40 ASP 46 -0.24 ALA 170
PRO 3 0.36 TYR 47 -0.27 ALA 221
PRO 3 0.25 ASN 48 -0.25 ASN 222
PRO 3 0.09 GLY 49 -0.28 ALA 166
ASN 271 0.11 TRP 50 -0.22 ALA 166
GLN 92 0.10 ASP 51 -0.31 LEU 218
ASN 271 0.10 ILE 52 -0.38 LEU 218
ASN 271 0.14 ASN 53 -0.41 LEU 218
ASN 271 0.13 THR 54 -0.40 LEU 218
ASP 46 0.11 PRO 55 -0.45 LEU 218
TRP 59 0.12 ALA 56 -0.29 TYR 265
SER 1 0.09 PHE 57 -0.27 LEU 218
GLN 11 0.08 GLU 58 -0.34 PRO 257
ALA 56 0.12 TRP 59 -0.30 PRO 257
HIS 138 0.09 TYR 60 -0.23 PRO 257
HIS 138 0.09 TYR 61 -0.25 PRO 257
GLY 64 0.16 GLN 62 -0.20 PRO 257
HIS 138 0.11 SER 63 -0.17 PRO 257
GLN 62 0.16 GLY 64 -0.13 PRO 257
HIS 138 0.14 LEU 65 -0.12 PRO 257
PRO 3 0.21 SER 66 -0.13 ASN 222
PRO 3 0.22 ILE 67 -0.14 ASN 222
PRO 3 0.30 VAL 68 -0.17 ASN 222
PRO 3 0.32 MET 69 -0.19 ASN 222
PRO 3 0.36 PRO 70 -0.21 ASN 222
PRO 3 0.38 VAL 71 -0.24 ASN 222
PRO 3 0.31 GLY 72 -0.25 ASN 222
PRO 3 0.26 GLY 73 -0.25 ASN 222
PHE 231 0.22 GLN 74 -0.30 ASN 222
VAL 232 0.23 SER 75 -0.37 ASN 222
PRO 3 0.18 SER 76 -0.31 PRO 224
SER 235 0.15 PHE 77 -0.35 PRO 224
PRO 3 0.22 TYR 78 -0.27 PRO 224
ALA 186 0.23 SER 79 -0.29 PRO 224
TRP 179 0.29 ASP 80 -0.27 PRO 224
SER 16 0.36 TRP 81 -0.32 PRO 224
SER 16 0.42 TYR 82 -0.33 PRO 224
SER 16 0.27 SER 83 -0.29 PRO 224
PRO 3 0.29 PRO 84 -0.24 ASN 222
PRO 3 0.25 ALA 85 -0.27 ASN 222
PRO 3 0.23 CYS 86 -0.25 ASN 222
PHE 231 0.24 GLY 87 -0.26 ASN 222
PHE 231 0.30 LYS 88 -0.23 ASP 20
PHE 231 0.28 ALA 89 -0.30 ARG 19
PRO 3 0.29 GLY 90 -0.20 GLY 18
PRO 3 0.32 CYS 91 -0.18 ASN 222
PRO 3 0.36 GLN 92 -0.23 THR 93
PRO 3 0.36 THR 93 -0.23 GLN 92
PRO 3 0.33 TYR 94 -0.23 ASN 222
TRP 81 0.35 LYS 95 -0.22 PRO 224
PRO 3 0.31 TRP 96 -0.22 ASN 222
ALA 186 0.35 GLU 97 -0.22 PRO 224
ALA 186 0.39 THR 98 -0.23 GLN 140
PRO 3 0.34 PHE 99 -0.19 ASN 222
PRO 3 0.31 LEU 100 -0.18 GLN 140
ALA 186 0.36 THR 101 -0.24 GLN 140
PRO 185 0.41 SER 102 -0.23 GLN 140
PRO 185 0.35 GLU 103 -0.18 GLN 140
PRO 3 0.36 LEU 104 -0.18 ASN 222
PRO 185 0.31 PRO 105 -0.15 ASN 222
PRO 185 0.36 GLN 106 -0.15 ASN 222
PRO 3 0.35 TRP 107 -0.17 ASN 222
PRO 3 0.34 LEU 108 -0.16 ASN 222
PRO 185 0.30 SER 109 -0.14 ASN 222
PRO 185 0.31 ALA 110 -0.15 ASN 222
PRO 3 0.35 ASN 111 -0.16 ASN 222
PRO 3 0.34 ARG 112 -0.16 ASN 222
PRO 3 0.26 ALA 113 -0.13 ASN 222
PRO 3 0.25 VAL 114 -0.13 ASN 222
PRO 185 0.26 LYS 115 -0.10 ASN 222
HIS 138 0.32 PRO 116 -0.11 GLU 103
HIS 138 0.28 THR 117 -0.17 SER 102
GLN 140 0.20 GLY 118 -0.13 SER 102
PRO 185 0.18 SER 119 -0.12 GLY 118
PRO 3 0.14 ALA 120 -0.10 PRO 224
PRO 3 0.14 ALA 121 -0.13 PRO 224
PRO 3 0.08 ILE 122 -0.12 PRO 224
ALA 43 0.08 GLY 123 -0.15 PRO 224
ALA 89 0.11 LEU 124 -0.23 GLY 159
ARG 42 0.20 SER 125 -0.31 GLY 159
ALA 150 0.24 MET 126 -0.35 PRO 224
LEU 41 0.12 ALA 127 -0.25 PRO 224
ALA 170 0.12 GLY 128 -0.21 PRO 224
ALA 170 0.14 SER 129 -0.27 PRO 224
PRO 3 0.13 SER 130 -0.26 PRO 224
PRO 3 0.12 ALA 131 -0.18 PRO 224
PRO 116 0.10 MET 132 -0.18 PRO 224
PRO 116 0.15 ILE 133 -0.23 PRO 224
PRO 116 0.19 LEU 134 -0.20 PRO 224
PRO 185 0.15 ALA 135 -0.15 PRO 224
PRO 116 0.17 ALA 136 -0.17 PRO 224
PRO 185 0.27 TYR 137 -0.20 PRO 224
PRO 116 0.32 HIS 138 -0.18 THR 98
PRO 185 0.22 PRO 139 -0.16 THR 98
PRO 185 0.21 GLN 140 -0.24 THR 101
HIS 138 0.30 GLN 141 -0.21 GLN 140
PRO 185 0.18 PHE 142 -0.12 PRO 224
GLU 217 0.16 ILE 143 -0.11 SER 16
GLU 217 0.18 TYR 144 -0.09 SER 16
GLU 217 0.15 ALA 145 -0.10 PRO 224
GLU 217 0.16 GLY 146 -0.10 GLU 58
ALA 170 0.13 SER 147 -0.13 GLU 58
ALA 170 0.12 LEU 148 -0.21 GLY 159
ALA 170 0.20 SER 149 -0.28 GLY 159
ALA 170 0.27 ALA 150 -0.37 LEU 151
ALA 166 0.34 LEU 151 -0.37 ALA 150
ALA 166 0.25 LEU 152 -0.26 PRO 224
ALA 166 0.25 ASP 153 -0.35 PRO 224
ILE 163 0.24 PRO 154 -0.54 PRO 224
SER 102 0.19 SER 155 -0.52 PRO 224
SER 102 0.16 GLN 156 -0.51 PRO 224
ALA 242 0.22 GLY 157 -0.61 PRO 224
LYS 238 0.27 MET 158 -0.74 PRO 224
SER 161 0.20 GLY 159 -0.77 PRO 224
SER 102 0.13 PRO 160 -0.77 PRO 224
GLY 159 0.20 SER 161 -0.87 PRO 224
LYS 238 0.23 LEU 162 -1.08 PRO 224
PRO 154 0.24 ILE 163 -0.87 PRO 224
LYS 174 0.18 GLY 164 -0.78 PRO 224
SER 235 0.26 LEU 165 -0.90 PRO 224
PHE 231 0.42 ALA 166 -0.79 PRO 224
PHE 231 0.30 MET 167 -0.55 PRO 224
PHE 231 0.31 GLY 168 -0.50 ASN 222
PHE 231 0.47 ASP 169 -0.51 ASN 222
PHE 231 0.43 ALA 170 -0.44 ASN 222
PHE 231 0.34 GLY 171 -0.33 ASN 222
PHE 231 0.30 GLY 172 -0.36 ASN 222
PHE 231 0.21 TYR 173 -0.39 ASN 222
GLY 164 0.18 LYS 174 -0.46 PRO 224
SER 16 0.15 ALA 175 -0.57 PRO 224
SER 16 0.21 ALA 176 -0.51 PRO 224
SER 16 0.22 ASP 177 -0.39 PRO 224
SER 16 0.23 MET 178 -0.41 PRO 224
SER 16 0.30 TRP 179 -0.46 PRO 224
SER 16 0.31 GLY 180 -0.49 PRO 224
SER 16 0.27 PRO 181 -0.60 PRO 224
SER 102 0.24 SER 182 -0.65 PRO 224
SER 102 0.29 SER 183 -0.59 PRO 224
SER 102 0.37 ASP 184 -0.51 PRO 224
SER 102 0.41 PRO 185 -0.44 PRO 224
SER 102 0.41 ALA 186 -0.41 PRO 224
SER 102 0.26 TRP 187 -0.48 PRO 224
ARG 189 0.30 GLU 188 -0.41 PRO 224
GLU 188 0.30 ARG 189 -0.33 PRO 224
SER 102 0.24 ASN 190 -0.36 PRO 224
SER 102 0.18 ASP 191 -0.35 PRO 224
ALA 166 0.14 PRO 192 -0.24 PRO 224
ALA 166 0.18 THR 193 -0.22 PRO 224
GLY 157 0.17 GLN 194 -0.26 PRO 224
PRO 116 0.16 GLN 195 -0.22 PRO 224
GLY 157 0.15 ILE 196 -0.15 PRO 224
GLY 157 0.16 PRO 197 -0.15 TYR 82
PRO 139 0.16 LYS 198 -0.17 TRP 81
GLU 217 0.17 LEU 199 -0.14 TRP 81
GLU 217 0.21 VAL 200 -0.13 TYR 82
GLU 217 0.19 ALA 201 -0.15 TYR 82
GLU 217 0.19 ASN 202 -0.15 TRP 81
GLU 217 0.24 ASN 203 -0.13 THR 98
GLU 217 0.22 THR 204 -0.13 THR 98
GLU 217 0.25 ARG 205 -0.10 ASN 250
GLU 217 0.25 LEU 206 -0.08 ASP 241
GLU 217 0.26 TRP 207 -0.15 MET 273
TYR 209 0.26 VAL 208 -0.16 ASN 236
VAL 208 0.26 TYR 209 -0.23 ALA 272
GLY 259 0.18 CYS 210 -0.24 ARG 2
ASN 254 0.22 GLY 211 -0.33 ARG 2
ILE 223 0.20 ASN 212 -0.32 ARG 2
ILE 223 0.22 GLY 213 -0.40 GLY 159
ASN 254 0.25 THR 214 -0.39 ARG 2
ASN 254 0.31 PRO 215 -0.44 ARG 2
ASN 254 0.40 ASN 216 -0.53 ARG 2
ASN 254 0.40 GLU 217 -0.62 ARG 2
ASN 254 0.38 LEU 218 -0.66 ARG 2
ASN 254 0.29 GLY 219 -0.53 ARG 2
ASN 254 0.23 GLY 220 -0.53 LEU 162
ASN 254 0.23 ALA 221 -0.58 LEU 162
THR 214 0.18 ASN 222 -0.73 LEU 162
THR 214 0.25 ILE 223 -0.79 LEU 162
THR 214 0.11 PRO 224 -1.08 LEU 162
ASN 254 0.10 ALA 225 -0.81 LEU 162
ASN 254 0.16 GLU 226 -0.61 LEU 162
ALA 170 0.19 PHE 227 -0.58 GLY 159
ALA 170 0.31 LEU 228 -0.74 GLY 159
ALA 170 0.22 GLU 229 -0.48 GLY 159
ASP 169 0.27 ASN 230 -0.38 GLY 157
ASP 169 0.47 PHE 231 -0.46 GLY 157
ASP 169 0.40 VAL 232 -0.35 GLN 156
ASP 169 0.31 ARG 233 -0.22 SER 183
ASP 169 0.37 SER 234 -0.19 SER 183
ALA 166 0.37 SER 235 -0.19 SER 183
ASP 169 0.28 ASN 236 -0.19 ALA 272
ASP 169 0.27 LEU 237 -0.22 ALA 272
ALA 166 0.29 LYS 238 -0.17 ALA 272
ALA 166 0.24 PHE 239 -0.14 ALA 272
PRO 257 0.24 GLN 240 -0.17 ALA 272
PRO 257 0.25 ASP 241 -0.16 ALA 272
MET 158 0.22 ALA 242 -0.12 ALA 272
PRO 257 0.22 TYR 243 -0.10 MET 273
PRO 257 0.29 ASN 244 -0.11 ASP 276
PRO 257 0.25 ALA 245 -0.09 MET 273
PRO 257 0.21 ALA 246 -0.10 TYR 82
GLU 217 0.26 GLY 247 -0.10 TYR 82
GLU 217 0.28 GLY 248 -0.10 TYR 82
GLU 217 0.35 HIS 249 -0.08 TYR 82
GLU 217 0.34 ASN 250 -0.10 ARG 205
GLU 217 0.32 ALA 251 -0.12 ASP 276
GLU 217 0.39 VAL 252 -0.17 GLN 240
GLU 217 0.34 PHE 253 -0.24 ALA 272
GLU 217 0.40 ASN 254 -0.29 ALA 272
HIS 249 0.28 PHE 255 -0.30 ARG 2
ASN 216 0.34 PRO 256 -0.39 ARG 2
HIS 249 0.31 PRO 257 -0.43 ARG 2
PRO 256 0.33 ASN 258 -0.45 ARG 2
ASN 254 0.37 GLY 259 -0.42 ARG 2
ASN 254 0.22 THR 260 -0.44 LEU 162
ASN 254 0.13 HIS 261 -0.51 LEU 162
ASN 254 0.13 SER 262 -0.46 LEU 162
GLN 269 0.17 TRP 263 -0.37 LEU 162
ALA 268 0.23 GLU 264 -0.47 ARG 2
VAL 252 0.22 TYR 265 -0.43 ARG 2
GLN 269 0.14 TRP 266 -0.32 PRO 55
TRP 263 0.16 GLY 267 -0.33 PRO 55
GLU 264 0.23 ALA 268 -0.37 ARG 2
LEU 218 0.26 GLN 269 -0.27 ARG 2
LEU 218 0.12 LEU 270 -0.25 GLU 58
ASN 53 0.14 ASN 271 -0.30 PRO 256
LEU 218 0.35 ALA 272 -0.30 PHE 255
LEU 218 0.28 MET 273 -0.23 PHE 253
GLU 217 0.18 LYS 274 -0.17 PHE 255
GLU 217 0.27 GLY 275 -0.16 PHE 253
GLU 217 0.30 ASP 276 -0.15 VAL 252
GLU 217 0.20 LEU 277 -0.12 VAL 252
GLU 217 0.18 GLN 278 -0.11 VAL 252
GLU 217 0.24 SER 279 -0.11 ASP 241
GLU 217 0.23 SER 280 -0.08 ASP 241
GLU 217 0.16 LEU 281 -0.08 GLU 103
GLU 217 0.16 GLY 282 -0.07 VAL 252
GLN 140 0.13 ALA 283 -0.10 SER 32
GLU 217 0.12 GLY 284 -0.10 GLY 29

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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.