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

CA distance fluctuations for 2402070233561794441

---  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
TRP 59 0.16 SER 1 -0.79 ASN 222
TRP 59 0.28 ARG 2 -0.78 ASN 222
GLY 275 0.22 PRO 3 -0.75 ASP 46
GLY 275 0.29 GLY 4 -0.64 ASN 222
GLY 275 0.23 LEU 5 -0.59 ASN 222
ASN 250 0.18 PRO 6 -0.52 ASN 222
ASN 250 0.14 VAL 7 -0.51 ASN 222
ASN 250 0.11 GLU 8 -0.48 PRO 224
ASN 250 0.09 TYR 9 -0.49 PRO 224
ASN 250 0.07 LEU 10 -0.44 PRO 224
ASP 46 0.07 GLN 11 -0.41 PRO 224
ASP 46 0.07 VAL 12 -0.38 PRO 224
ASP 46 0.08 PRO 13 -0.35 PRO 224
GLN 92 0.14 SER 14 -0.34 PRO 224
GLN 92 0.20 PRO 15 -0.31 PRO 224
GLN 92 0.26 SER 16 -0.32 PRO 224
GLN 92 0.27 MET 17 -0.36 PRO 224
ALA 89 0.22 GLY 18 -0.34 PRO 224
ALA 89 0.14 ARG 19 -0.37 PRO 224
ASP 45 0.13 ASP 20 -0.38 PRO 224
ASP 46 0.10 ILE 21 -0.43 PRO 224
ASP 46 0.07 LYS 22 -0.48 PRO 224
TYR 144 0.07 VAL 23 -0.48 PRO 224
ASN 250 0.09 GLN 24 -0.52 PRO 224
ASN 250 0.12 PHE 25 -0.47 PRO 224
ASN 250 0.17 GLN 26 -0.46 ASN 222
ASN 203 0.19 SER 27 -0.41 ASN 222
ASN 203 0.23 GLY 28 -0.39 ASN 222
ASN 203 0.22 GLY 29 -0.37 ASN 222
ASN 203 0.22 ASN 30 -0.32 ASN 222
ASN 203 0.23 ASN 31 -0.29 ASN 222
ASN 203 0.24 SER 32 -0.32 ASN 222
ASN 203 0.25 PRO 33 -0.30 ASN 222
ASN 203 0.17 ALA 34 -0.34 PRO 224
TYR 144 0.15 VAL 35 -0.35 PRO 224
SER 79 0.09 TYR 36 -0.39 PRO 224
ILE 122 0.09 LEU 37 -0.44 PRO 224
VAL 71 0.08 LEU 38 -0.46 PRO 224
GLN 44 0.08 ASP 39 -0.58 PRO 224
GLN 44 0.06 GLY 40 -0.64 PRO 224
LEU 162 0.06 LEU 41 -0.73 PRO 224
ARG 19 0.09 ARG 42 -0.99 PRO 224
ASP 20 0.07 ALA 43 -0.78 PRO 224
ASP 20 0.09 GLN 44 -0.77 PRO 224
ASP 20 0.13 ASP 45 -0.65 PRO 224
ASP 20 0.12 ASP 46 -0.75 PRO 3
GLY 49 0.07 TYR 47 -0.69 PRO 224
LEU 270 0.07 ASN 48 -0.67 PRO 224
GLY 267 0.08 GLY 49 -0.80 PRO 224
LEU 270 0.08 TRP 50 -0.66 PRO 224
ASN 271 0.12 ASP 51 -0.70 PRO 224
GLY 267 0.13 ILE 52 -0.83 PRO 224
GLY 267 0.23 ASN 53 -0.92 ASN 222
LEU 270 0.16 THR 54 -0.76 ASN 222
ASN 271 0.16 PRO 55 -0.72 ASN 222
ASN 250 0.14 ALA 56 -0.61 ASN 222
GLY 275 0.18 PHE 57 -0.58 ASN 222
TRP 59 0.32 GLU 58 -0.60 ASN 222
GLU 58 0.32 TRP 59 -0.53 ASN 222
GLY 275 0.26 TYR 60 -0.47 ASN 222
GLY 275 0.30 TYR 61 -0.51 ASN 222
SER 63 0.41 GLN 62 -0.42 ASN 222
GLN 62 0.41 SER 63 -0.39 ASN 222
GLN 62 0.33 GLY 64 -0.36 ASN 222
ASN 203 0.25 LEU 65 -0.37 ASN 222
ASN 203 0.20 SER 66 -0.39 ASN 222
ASN 250 0.16 ILE 67 -0.43 PRO 224
TYR 144 0.10 VAL 68 -0.44 PRO 224
ALA 121 0.08 MET 69 -0.50 PRO 224
VAL 71 0.10 PRO 70 -0.49 PRO 224
PRO 70 0.10 VAL 71 -0.56 PRO 224
ASP 20 0.11 GLY 72 -0.60 PRO 224
ASP 20 0.07 GLY 73 -0.57 PRO 224
ARG 19 0.09 GLN 74 -0.70 PRO 224
ALA 170 0.07 SER 75 -0.61 PRO 224
ILE 143 0.07 SER 76 -0.48 PRO 224
ILE 143 0.07 PHE 77 -0.38 PRO 224
ALA 121 0.09 TYR 78 -0.37 PRO 224
GLN 141 0.16 SER 79 -0.31 PRO 224
TRP 81 0.30 ASP 80 -0.30 PRO 224
ASP 80 0.30 TRP 81 -0.33 PRO 224
HIS 138 0.23 TYR 82 -0.29 PRO 3
SER 102 0.21 SER 83 -0.35 PRO 224
THR 98 0.22 PRO 84 -0.43 PRO 224
THR 98 0.18 ALA 85 -0.51 PRO 224
SER 16 0.16 CYS 86 -0.57 PRO 224
THR 93 0.17 GLY 87 -0.69 PRO 224
GLY 18 0.17 LYS 88 -0.80 PRO 224
GLY 18 0.22 ALA 89 -0.76 PRO 224
GLY 18 0.19 GLY 90 -0.67 PRO 3
SER 16 0.22 CYS 91 -0.55 PRO 3
THR 93 0.33 GLN 92 -0.49 PRO 224
GLN 92 0.33 THR 93 -0.41 PRO 224
LYS 95 0.19 TYR 94 -0.41 PRO 224
THR 98 0.20 LYS 95 -0.35 PRO 224
LEU 100 0.13 TRP 96 -0.37 PRO 224
TRP 81 0.20 GLU 97 -0.30 PRO 224
PRO 84 0.22 THR 98 -0.29 PRO 224
LYS 95 0.16 PHE 99 -0.33 PRO 224
TRP 96 0.13 LEU 100 -0.33 PRO 224
PRO 116 0.21 THR 101 -0.28 PRO 224
SER 83 0.21 SER 102 -0.27 PRO 224
PRO 84 0.16 GLU 103 -0.31 PRO 224
LYS 95 0.10 LEU 104 -0.34 PRO 224
TYR 82 0.14 PRO 105 -0.31 PRO 224
SER 16 0.18 GLN 106 -0.29 PRO 224
PRO 15 0.15 TRP 107 -0.32 PRO 224
SER 16 0.10 LEU 108 -0.34 PRO 224
SER 16 0.13 SER 109 -0.31 PRO 224
SER 16 0.14 ALA 110 -0.30 PRO 224
PRO 15 0.10 ASN 111 -0.33 PRO 224
ASN 203 0.11 ARG 112 -0.35 PRO 224
ASN 203 0.14 ALA 113 -0.31 PRO 224
ASN 203 0.16 VAL 114 -0.32 PRO 224
ASN 202 0.17 LYS 115 -0.27 PRO 224
THR 101 0.21 PRO 116 -0.26 PRO 224
HIS 138 0.21 THR 117 -0.23 PRO 224
ASN 202 0.25 GLY 118 -0.22 PRO 224
GLN 62 0.19 SER 119 -0.25 PRO 224
GLN 62 0.18 ALA 120 -0.27 PRO 224
SER 79 0.13 ALA 121 -0.28 PRO 224
LEU 37 0.09 ILE 122 -0.32 PRO 224
LEU 162 0.09 GLY 123 -0.33 PRO 224
LEU 162 0.08 LEU 124 -0.39 PRO 224
LEU 162 0.14 SER 125 -0.34 PRO 224
LEU 162 0.14 MET 126 -0.35 PRO 224
LEU 162 0.10 ALA 127 -0.35 PRO 224
LEU 162 0.09 GLY 128 -0.24 PRO 224
LEU 162 0.09 SER 129 -0.17 PRO 224
ALA 131 0.11 SER 130 -0.24 PRO 224
ASN 190 0.11 ALA 131 -0.24 PRO 224
ASN 190 0.15 MET 132 -0.15 PRO 224
ASN 190 0.17 ILE 133 -0.16 PRO 224
TYR 82 0.18 LEU 134 -0.21 PRO 224
ILE 143 0.18 ALA 135 -0.16 PRO 224
ALA 186 0.21 ALA 136 -0.12 PRO 224
TYR 82 0.23 TYR 137 -0.15 PRO 224
TYR 82 0.23 HIS 138 -0.18 PRO 224
TYR 82 0.21 PRO 139 -0.15 PRO 224
TYR 82 0.22 GLN 140 -0.18 PRO 224
TYR 82 0.21 GLN 141 -0.21 PRO 224
GLN 62 0.19 PHE 142 -0.21 PRO 224
GLN 62 0.24 ILE 143 -0.16 PRO 224
GLN 62 0.23 TYR 144 -0.18 PRO 224
GLN 62 0.18 ALA 145 -0.18 PRO 224
GLN 62 0.13 GLY 146 -0.21 PRO 224
LEU 151 0.08 SER 147 -0.18 PRO 224
LEU 151 0.06 LEU 148 -0.22 PRO 224
GLY 220 0.07 SER 149 -0.26 ALA 170
LEU 151 0.12 ALA 150 -0.21 ALA 170
ALA 150 0.12 LEU 151 -0.27 ALA 166
VAL 232 0.13 LEU 152 -0.18 ALA 166
PHE 231 0.16 ASP 153 -0.16 ALA 242
GLY 220 0.11 PRO 154 -0.20 PRO 3
ILE 143 0.12 SER 155 -0.19 PRO 3
PHE 227 0.20 GLN 156 -0.17 PRO 3
PHE 227 0.26 GLY 157 -0.20 LYS 238
PRO 224 0.24 MET 158 -0.25 SER 234
GLY 220 0.14 GLY 159 -0.24 SER 234
ILE 143 0.10 PRO 160 -0.25 PRO 3
GLY 220 0.13 SER 161 -0.27 PRO 3
GLY 220 0.14 LEU 162 -0.30 SER 234
SER 130 0.08 ILE 163 -0.33 PHE 231
LEU 165 0.11 GLY 164 -0.35 PRO 3
GLY 164 0.11 LEU 165 -0.51 PHE 227
GLY 18 0.06 ALA 166 -0.70 LEU 228
ASP 80 0.08 MET 167 -0.64 PRO 224
ASP 169 0.10 GLY 168 -0.67 PRO 224
GLY 18 0.12 ASP 169 -0.92 PRO 224
GLY 18 0.13 ALA 170 -1.08 PRO 224
GLY 18 0.16 GLY 171 -0.91 PRO 224
GLY 18 0.13 GLY 172 -0.73 PRO 224
THR 98 0.11 TYR 173 -0.60 PRO 224
THR 98 0.12 LYS 174 -0.44 PRO 224
TYR 137 0.12 ALA 175 -0.35 PRO 3
TYR 137 0.16 ALA 176 -0.32 PRO 3
TYR 137 0.17 ASP 177 -0.36 PRO 3
TYR 137 0.17 MET 178 -0.33 PRO 224
TYR 137 0.20 TRP 179 -0.27 PRO 3
TYR 137 0.19 GLY 180 -0.28 PRO 3
TYR 137 0.16 PRO 181 -0.26 PRO 3
TYR 137 0.13 SER 182 -0.23 PRO 3
TYR 137 0.14 SER 183 -0.21 PRO 3
TYR 137 0.19 ASP 184 -0.21 PRO 3
TYR 137 0.21 PRO 185 -0.18 PRO 3
TYR 137 0.22 ALA 186 -0.20 PRO 3
ALA 136 0.16 TRP 187 -0.20 PRO 3
ALA 136 0.16 GLU 188 -0.16 PRO 3
ALA 186 0.22 ARG 189 -0.15 PRO 3
ILE 143 0.17 ASN 190 -0.17 PRO 3
ILE 143 0.15 ASP 191 -0.15 PRO 3
SER 280 0.16 PRO 192 -0.11 PHE 77
SER 280 0.17 THR 193 -0.12 ALA 166
SER 280 0.16 GLN 194 -0.11 SER 16
LEU 281 0.19 GLN 195 -0.11 SER 16
SER 280 0.21 ILE 196 -0.11 SER 129
GLY 282 0.23 PRO 197 -0.08 SER 16
GLY 282 0.23 LYS 198 -0.07 SER 125
LEU 281 0.26 LEU 199 -0.10 MET 132
GLY 282 0.30 VAL 200 -0.08 SER 125
GLY 282 0.30 ALA 201 -0.08 SER 125
GLY 282 0.33 ASN 202 -0.09 PRO 224
GLY 282 0.40 ASN 203 -0.11 LEU 218
LEU 281 0.35 THR 204 -0.11 LEU 218
SER 280 0.32 ARG 205 -0.14 LEU 218
GLN 62 0.22 LEU 206 -0.13 LEU 218
GLN 62 0.19 TRP 207 -0.15 LEU 218
ASN 236 0.13 VAL 208 -0.15 ALA 170
ALA 272 0.12 TYR 209 -0.20 ALA 170
ASN 230 0.09 CYS 210 -0.27 ALA 170
GLY 213 0.11 GLY 211 -0.32 ASP 169
ILE 223 0.20 ASN 212 -0.42 ASP 169
ILE 223 0.17 GLY 213 -0.50 ASP 169
ILE 223 0.21 THR 214 -0.44 ASP 169
ALA 221 0.14 PRO 215 -0.34 ASP 169
ALA 221 0.12 ASN 216 -0.25 ASP 169
ALA 221 0.18 GLU 217 -0.33 ALA 272
SER 262 0.10 LEU 218 -0.43 ALA 272
HIS 261 0.13 GLY 219 -0.47 PRO 55
ALA 225 0.19 GLY 220 -0.57 PRO 55
GLU 217 0.18 ALA 221 -0.63 ASN 53
GLY 157 0.22 ASN 222 -0.92 ASN 53
GLY 157 0.25 ILE 223 -0.86 ALA 170
GLY 157 0.26 PRO 224 -1.08 ALA 170
GLY 157 0.20 ALA 225 -0.71 ALA 170
ASN 230 0.19 GLU 226 -0.65 ASP 169
GLY 157 0.26 PHE 227 -0.82 ASP 169
GLY 157 0.23 LEU 228 -0.72 ASP 169
GLU 226 0.14 GLU 229 -0.50 ALA 170
ILE 223 0.23 ASN 230 -0.55 ASP 169
PHE 227 0.23 PHE 231 -0.57 ALA 166
THR 193 0.13 VAL 232 -0.46 ALA 166
ASN 230 0.22 ARG 233 -0.39 ALA 166
PHE 227 0.25 SER 234 -0.39 ALA 166
PHE 227 0.19 SER 235 -0.32 ALA 166
ASN 230 0.16 ASN 236 -0.26 ALA 166
ASN 230 0.19 LEU 237 -0.27 ALA 166
PHE 227 0.19 LYS 238 -0.25 ALA 166
SER 280 0.16 PHE 239 -0.21 ALA 166
SER 280 0.19 GLN 240 -0.19 ALA 166
SER 280 0.19 ASP 241 -0.20 ALA 166
SER 280 0.20 ALA 242 -0.18 ALA 166
SER 280 0.23 TYR 243 -0.16 ALA 166
SER 279 0.25 ASN 244 -0.15 ALA 166
SER 279 0.23 ALA 245 -0.18 GLY 157
GLY 282 0.25 ALA 246 -0.13 ALA 166
GLY 282 0.29 GLY 247 -0.12 ALA 166
SER 280 0.33 GLY 248 -0.11 ALA 166
SER 279 0.36 HIS 249 -0.12 ALA 170
SER 280 0.44 ASN 250 -0.13 LEU 218
SER 280 0.28 ALA 251 -0.13 LEU 218
MET 273 0.24 VAL 252 -0.15 LEU 218
MET 273 0.21 PHE 253 -0.17 ASP 169
ALA 272 0.20 ASN 254 -0.19 ASP 169
ASN 254 0.16 PHE 255 -0.25 ASP 169
PRO 257 0.24 PRO 256 -0.26 ASP 169
PRO 256 0.24 PRO 257 -0.33 ASP 169
ILE 223 0.12 ASN 258 -0.32 ASP 169
TYR 265 0.04 GLY 259 -0.30 ASP 169
GLY 220 0.11 THR 260 -0.37 ALA 170
GLY 220 0.17 HIS 261 -0.39 ALA 170
GLY 219 0.13 SER 262 -0.72 TRP 263
TRP 266 0.11 TRP 263 -0.72 SER 262
MET 158 0.07 GLU 264 -0.45 ASN 222
PRO 257 0.07 TYR 265 -0.30 ALA 268
TRP 263 0.11 TRP 266 -0.34 LEU 270
ASN 53 0.23 GLY 267 -0.46 ASN 222
ASN 53 0.17 ALA 268 -0.39 LEU 218
THR 54 0.15 GLN 269 -0.29 LEU 218
THR 54 0.16 LEU 270 -0.36 ASN 222
ARG 2 0.19 ASN 271 -0.43 LEU 218
ASN 254 0.20 ALA 272 -0.43 LEU 218
VAL 252 0.24 MET 273 -0.32 LEU 218
GLU 58 0.24 LYS 274 -0.36 LEU 218
GLN 62 0.34 GLY 275 -0.36 LEU 218
GLN 62 0.30 ASP 276 -0.30 LEU 218
ASN 250 0.32 LEU 277 -0.29 LEU 218
ASN 250 0.35 GLN 278 -0.31 LEU 218
ASN 250 0.40 SER 279 -0.29 LEU 218
ASN 250 0.44 SER 280 -0.24 LEU 218
ASN 203 0.39 LEU 281 -0.24 LEU 218
ASN 203 0.40 GLY 282 -0.27 LEU 218
ASN 203 0.33 ALA 283 -0.30 LEU 218
ASN 203 0.30 GLY 284 -0.35 LEU 218

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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.