Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
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* secyeg_itasser *

CA distance fluctuations for 260811042802127475

--- normal mode 16 ---

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 increase ref largest decrease
VAL 499 0.09 MET 1 -0.48 LYS 433

VAL 499 0.10 ASN 2 -0.51 LYS 433

VAL 499 0.11 VAL 3 -0.56 LYS 433

VAL 499 0.13 GLY 4 -0.60 LYS 433

VAL 499 0.15 ALA 5 -0.59 LYS 433

VAL 499 0.16 ARG 6 -0.62 LYS 433

VAL 499 0.17 GLY 7 -0.69 LYS 433

ARG 418 0.21 ASN 8 -0.74 LYS 433

ALA 503 0.23 ALA 9 -0.77 LYS 433

ALA 503 0.23 GLY 10 -0.70 LYS 433

ALA 503 0.20 LEU 11 -0.63 LYS 433

VAL 499 0.21 PHE 12 -0.63 LYS 433

ALA 503 0.24 TRP 13 -0.61 LYS 433

ALA 503 0.22 ARG 14 -0.55 LYS 433

VAL 499 0.18 PHE 15 -0.52 LYS 433

VAL 499 0.23 GLY 16 -0.52 LYS 433

ALA 503 0.23 PHE 17 -0.48 LYS 433

ALA 503 0.19 THR 18 -0.45 LYS 433

VAL 499 0.17 LEU 19 -0.43 LYS 433

VAL 499 0.24 LEU 20 -0.42 LYS 433

ALA 503 0.23 ALA 21 -0.40 LYS 433

ALA 503 0.17 LEU 22 -0.38 LYS 433

VAL 499 0.19 ILE 23 -0.37 LYS 433

VAL 499 0.25 VAL 24 -0.35 LYS 433

ALA 503 0.20 TYR 25 -0.34 LYS 433

ALA 503 0.14 ARG 26 -0.33 LYS 433

VAL 499 0.20 LEU 27 -0.32 LYS 433

ALA 503 0.24 GLY 28 -0.31 LYS 433

ALA 503 0.16 THR 29 -0.30 LYS 433

ALA 503 0.12 TYR 30 -0.29 LYS 433

ALA 503 0.21 ILE 31 -0.28 LYS 433

ALA 503 0.15 PRO 32 -0.27 LYS 433

ALA 503 0.20 ILE 33 -0.26 LYS 433

ALA 503 0.23 PRO 34 -0.24 LYS 433

ALA 503 0.14 GLY 35 -0.23 LYS 433

ALA 503 0.07 VAL 36 -0.24 LYS 433

GLY 16 0.05 ASN 37 -0.23 LYS 433

GLY 16 0.06 PRO 38 -0.24 LYS 433

ASP 486 0.06 SER 39 -0.32 TYR 501

LEU 201 0.06 VAL 40 -0.27 TYR 501

LEU 201 0.06 VAL 41 -0.24 LYS 433

LEU 201 0.08 GLU 42 -0.28 TYR 501

LEU 201 0.11 ASP 43 -0.32 TYR 501

ASN 205 0.11 ILE 44 -0.25 TYR 501

LEU 201 0.11 ILE 45 -0.24 TYR 501

LEU 201 0.16 SER 46 -0.30 TYR 501

ASN 205 0.17 SER 47 -0.26 TYR 501

ASN 205 0.18 HSD 48 -0.24 TYR 501

ASN 205 0.15 ALA 49 -0.22 LYS 433

LEU 202 0.13 THR 50 -0.23 LYS 433

LEU 202 0.16 GLY 51 -0.24 LYS 433

LEU 202 0.13 VAL 52 -0.24 LYS 433

LEU 202 0.10 LEU 53 -0.25 LYS 433

LEU 202 0.10 GLY 54 -0.26 LYS 433

LEU 202 0.08 ILE 55 -0.27 LYS 433

LEU 202 0.06 PHE 56 -0.27 LYS 433

SER 253 0.06 ASN 57 -0.28 LYS 433

SER 253 0.06 VAL 58 -0.29 LYS 433

SER 253 0.06 PHE 59 -0.30 LYS 433

SER 253 0.06 SER 60 -0.30 LYS 433

SER 253 0.06 GLY 61 -0.31 LYS 433

SER 253 0.06 GLY 62 -0.29 LYS 433

SER 253 0.06 ALA 63 -0.29 LYS 433

SER 253 0.05 LEU 64 -0.27 LYS 433

GLY 16 0.05 GLY 65 -0.27 LYS 433

GLY 16 0.06 ARG 66 -0.27 LYS 433

GLY 16 0.05 MET 67 -0.26 LYS 433

ALA 503 0.12 THR 68 -0.28 LYS 433

ALA 503 0.20 ILE 69 -0.28 LYS 433

ALA 503 0.16 PHE 70 -0.29 LYS 433

ALA 503 0.11 ALA 71 -0.28 LYS 433

ALA 503 0.10 LEU 72 -0.28 LYS 433

ALA 503 0.12 ASN 73 -0.30 LYS 433

ALA 503 0.13 VAL 74 -0.31 LYS 433

ALA 503 0.10 MET 75 -0.29 LYS 433

ALA 503 0.14 PRO 76 -0.28 LYS 433

ALA 503 0.15 TYR 77 -0.30 LYS 433

ALA 503 0.12 ILE 78 -0.30 LYS 433

ALA 503 0.12 VAL 79 -0.28 LYS 433

ALA 503 0.15 SER 80 -0.28 LYS 433

ALA 503 0.14 SER 81 -0.29 LYS 433

ALA 503 0.11 ILE 82 -0.28 LYS 433

ALA 503 0.13 ILE 83 -0.26 LYS 433

ALA 503 0.15 VAL 84 -0.27 LYS 433

ALA 503 0.12 GLN 85 -0.27 LYS 433

ALA 503 0.11 LEU 86 -0.25 LYS 433

ALA 503 0.13 LEU 87 -0.24 LYS 433

ALA 503 0.13 SER 88 -0.25 LYS 433

ALA 503 0.12 VAL 89 -0.24 LYS 433

ALA 503 0.11 ALA 90 -0.23 LYS 433

ALA 503 0.13 ILE 91 -0.22 LYS 433

ALA 503 0.14 PRO 92 -0.21 LYS 433

ALA 503 0.16 THR 93 -0.21 LYS 433

ALA 503 0.16 LEU 94 -0.23 LYS 433

ALA 503 0.14 ASN 95 -0.23 LYS 433

ALA 503 0.15 GLU 96 -0.22 LYS 433

ALA 503 0.17 MET 97 -0.23 LYS 433

ALA 503 0.16 ARG 98 -0.25 LYS 433

ALA 503 0.16 GLN 99 -0.24 LYS 433

ALA 503 0.17 ASP 100 -0.23 LYS 433

ALA 503 0.17 GLY 101 -0.25 LYS 433

ALA 503 0.19 GLU 102 -0.28 LYS 433

ALA 503 0.20 LEU 103 -0.26 LYS 433

ALA 503 0.19 GLY 104 -0.25 LYS 433

ALA 503 0.19 ARG 105 -0.28 LYS 433

ALA 503 0.21 MET 106 -0.28 LYS 433

ALA 503 0.21 LYS 107 -0.26 LYS 433

ALA 503 0.19 MET 108 -0.27 LYS 433

ALA 503 0.20 SER 109 -0.29 LYS 433

ALA 503 0.23 THR 110 -0.28 LYS 433

ALA 503 0.21 TYR 111 -0.26 LYS 433

ALA 503 0.19 THR 112 -0.28 LYS 433

ALA 503 0.22 ARG 113 -0.29 LYS 433

ALA 503 0.23 TYR 114 -0.27 LYS 433

ALA 503 0.19 LEU 115 -0.26 LYS 433

ALA 503 0.19 SER 116 -0.28 LYS 433

ALA 503 0.22 VAL 117 -0.27 LYS 433

ALA 503 0.21 ALA 118 -0.25 LYS 433

ALA 503 0.17 PHE 119 -0.26 LYS 433

ALA 503 0.18 CYS 120 -0.27 LYS 433

ALA 503 0.21 ILE 121 -0.26 LYS 433

ALA 503 0.17 ALA 122 -0.24 LYS 433

ALA 503 0.14 GLN 123 -0.25 LYS 433

ALA 503 0.16 GLY 124 -0.25 LYS 433

ALA 503 0.16 LEU 125 -0.24 LYS 433

ALA 503 0.12 VAL 126 -0.23 LYS 433

ALA 503 0.09 ILE 127 -0.24 LYS 433

ALA 503 0.12 LEU 128 -0.23 LYS 433

ALA 503 0.12 LEU 129 -0.23 LYS 433

ALA 503 0.06 GLY 130 -0.22 LYS 433

ASN 205 0.07 LEU 131 -0.22 LYS 433

ASN 205 0.06 GLU 132 -0.22 LYS 433

ASN 205 0.06 ARG 133 -0.21 LYS 433

ASN 205 0.08 MET 134 -0.21 LYS 433

ASN 205 0.08 ASN 135 -0.20 LYS 433

ASN 205 0.07 SER 136 -0.20 LYS 433

ASN 205 0.06 ASP 137 -0.21 LYS 433

ASN 205 0.07 GLU 138 -0.21 LYS 433

ASN 205 0.08 VAL 139 -0.21 LYS 433

ASN 205 0.06 MET 140 -0.22 LYS 433

GLY 16 0.04 VAL 141 -0.22 LYS 433

GLY 16 0.04 VAL 142 -0.21 LYS 433

ALA 503 0.09 ILE 143 -0.21 LYS 433

ALA 503 0.10 ASN 144 -0.21 LYS 433

ALA 503 0.11 PRO 145 -0.21 LYS 433

ALA 503 0.17 GLY 146 -0.21 LYS 433

ALA 503 0.21 ILE 147 -0.21 LYS 433

ALA 503 0.26 MET 148 -0.22 LYS 433

ALA 503 0.22 PHE 149 -0.22 LYS 433

ALA 503 0.20 ARG 150 -0.23 LYS 433

ALA 503 0.26 VAL 151 -0.23 LYS 433

ALA 503 0.30 VAL 152 -0.24 LYS 433

ALA 503 0.23 GLY 153 -0.24 LYS 433

ALA 503 0.24 ILE 154 -0.25 LYS 433

ALA 503 0.30 SER 155 -0.25 LYS 433

ALA 503 0.29 SER 156 -0.26 LYS 433

ALA 503 0.23 LEU 157 -0.27 LYS 433

ALA 503 0.27 LEU 158 -0.27 LYS 433

ALA 503 0.32 ALA 159 -0.28 LYS 433

ALA 503 0.26 GLY 160 -0.29 LYS 433

ALA 503 0.23 THR 161 -0.30 LYS 433

ALA 503 0.28 MET 162 -0.30 LYS 433

ALA 503 0.29 PHE 163 -0.32 LYS 433

ALA 503 0.23 LEU 164 -0.33 LYS 433

ALA 503 0.23 LEU 165 -0.33 LYS 433

ALA 503 0.28 TRP 166 -0.34 LYS 433

ALA 503 0.25 LEU 167 -0.36 LYS 433

ALA 503 0.21 GLY 168 -0.37 LYS 433

ALA 503 0.23 GLU 169 -0.37 LYS 433

ALA 503 0.26 ARG 170 -0.40 LYS 433

ALA 503 0.21 ILE 171 -0.42 LYS 433

ALA 503 0.20 ASN 172 -0.41 LYS 433

ALA 503 0.23 ALA 173 -0.42 LYS 433

ALA 503 0.24 LYS 174 -0.48 LYS 433

ALA 503 0.21 GLY 175 -0.48 LYS 433

ALA 503 0.17 ILE 176 -0.46 LYS 433

ALA 503 0.14 GLY 177 -0.43 LYS 433

ALA 503 0.15 ASN 178 -0.39 LYS 433

ALA 503 0.17 GLY 179 -0.39 LYS 433

ALA 503 0.14 ILE 180 -0.35 LYS 433

ALA 503 0.10 SER 181 -0.36 LYS 433

ALA 503 0.11 LEU 182 -0.39 LYS 433

ALA 503 0.11 ILE 183 -0.36 LYS 433

SER 253 0.08 ILE 184 -0.34 LYS 433

SER 253 0.07 PHE 185 -0.36 LYS 433

SER 253 0.07 VAL 186 -0.36 LYS 433

SER 253 0.06 GLY 187 -0.34 LYS 433

SER 253 0.06 ILE 188 -0.33 LYS 433

SER 253 0.06 ILE 189 -0.34 LYS 433

SER 46 0.07 SER 190 -0.34 LYS 433

GLY 51 0.07 GLU 191 -0.31 LYS 433

GLY 51 0.06 LEU 192 -0.32 LYS 433

SER 46 0.09 PRO 193 -0.33 LYS 433

SER 46 0.12 SER 194 -0.31 LYS 433

GLY 51 0.10 SER 195 -0.31 TYR 501

HSD 48 0.08 ILE 196 -0.30 LYS 433

SER 46 0.13 SER 197 -0.36 GLY 498

SER 46 0.16 SER 198 -0.42 TYR 501

HSD 48 0.12 VAL 199 -0.37 TYR 501

HSD 48 0.12 PHE 200 -0.37 ALA 502

HSD 48 0.17 LEU 201 -0.45 ALA 502

HSD 48 0.18 LEU 202 -0.46 ALA 502

HSD 48 0.13 GLY 203 -0.41 ALA 502

HSD 48 0.15 LYS 204 -0.44 ALA 502

HSD 48 0.18 ASN 205 -0.50 ALA 502

HSD 48 0.16 GLY 206 -0.46 ALA 502

ALA 386 0.18 GLU 207 -0.45 ALA 502

ALA 386 0.14 VAL 208 -0.40 ALA 502

TYR 384 0.08 SER 209 -0.36 ALA 502

HSD 48 0.06 GLY 210 -0.33 ALA 502

LYS 450 0.06 LEU 211 -0.30 ALA 502

LYS 450 0.07 VAL 212 -0.30 TYR 501

LYS 450 0.05 VAL 213 -0.29 TYR 501

LYS 450 0.05 LEU 214 -0.27 LYS 433

LYS 450 0.06 SER 215 -0.25 LYS 433

LYS 450 0.06 MET 216 -0.27 LYS 433

SER 253 0.05 LEU 217 -0.28 LYS 433

GLY 345 0.05 LEU 218 -0.27 LYS 433

ALA 453 0.06 ALA 219 -0.27 LYS 433

SER 253 0.06 PHE 220 -0.29 LYS 433

SER 253 0.06 PHE 221 -0.30 LYS 433

ASN 252 0.06 ALA 222 -0.28 LYS 433

SER 253 0.06 LEU 223 -0.28 LYS 433

SER 253 0.07 PHE 224 -0.31 LYS 433

SER 253 0.06 LEU 225 -0.30 LYS 433

SER 233 0.07 LEU 226 -0.28 LYS 433

SER 253 0.07 ILE 227 -0.30 LYS 433

GLY 540 0.08 ILE 228 -0.32 LYS 433

GLY 540 0.08 PHE 229 -0.29 LYS 433

SER 233 0.11 PHE 230 -0.29 LYS 425

GLY 540 0.10 GLU 231 -0.31 LYS 425

GLY 540 0.10 ARG 232 -0.34 LYS 425

PHE 230 0.11 SER 233 -0.34 ALA 421

GLY 540 0.08 TYR 234 -0.40 ARG 418

GLY 345 0.08 ARG 235 -0.39 TYR 419

GLY 345 0.10 LYS 236 -0.44 TYR 419

GLY 345 0.10 VAL 237 -0.44 TYR 419

SER 460 0.08 PHE 238 -0.42 TYR 419

TYR 257 0.08 VAL 239 -0.42 TYR 419

LYS 462 0.07 GLN 240 -0.38 LEU 422

ALA 503 0.07 TYR 241 -0.37 LEU 422

ALA 503 0.09 PRO 242 -0.33 LEU 422

LYS 462 0.09 LYS 243 -0.26 LEU 422

LYS 431 0.11 ARG 244 -0.23 LEU 422

LYS 431 0.12 GLN 245 -0.23 LEU 422

LYS 431 0.14 THR 246 -0.21 LEU 422

ALA 503 0.09 GLY 247 -0.27 LEU 422

ALA 503 0.10 GLY 248 -0.31 MET 423

ALA 503 0.09 ARG 249 -0.39 MET 423

ALA 503 0.10 PHE 250 -0.35 LEU 422

ALA 503 0.12 TYR 251 -0.32 LEU 422

GLY 540 0.13 ASN 252 -0.42 LEU 422

PHE 541 0.18 SER 253 -0.51 LEU 422

GLY 540 0.16 ASP 254 -0.62 LEU 422

GLY 540 0.15 SER 255 -0.64 TYR 419

TYR 257 0.10 SER 256 -0.49 LEU 422

SER 256 0.10 TYR 257 -0.53 TYR 419

SER 255 0.12 ILE 258 -0.56 TYR 419

SER 255 0.12 PRO 259 -0.52 TYR 419

SER 255 0.09 LEU 260 -0.47 TYR 419

SER 255 0.11 LYS 261 -0.42 TYR 419

SER 255 0.09 ILE 262 -0.35 ALA 421

GLY 539 0.09 ASN 263 -0.34 ALA 421

GLY 539 0.13 THR 264 -0.37 TYR 415

GLY 540 0.13 ALA 265 -0.33 LYS 433

GLY 539 0.12 GLY 266 -0.34 LYS 433

SER 253 0.09 VAL 267 -0.32 LYS 433

SER 253 0.09 ILE 268 -0.32 LYS 433

SER 253 0.07 PRO 269 -0.30 LYS 433

SER 253 0.07 PRO 270 -0.29 LYS 433

SER 253 0.07 ILE 271 -0.30 LYS 433

SER 253 0.07 PHE 272 -0.29 LYS 433

GLU 207 0.06 ALA 273 -0.27 LYS 433

GLU 207 0.07 ASN 274 -0.28 LYS 433

GLU 207 0.06 ALA 275 -0.28 LYS 433

GLU 207 0.07 LEU 276 -0.26 LYS 433

GLU 207 0.08 LEU 277 -0.26 LYS 433

GLU 207 0.08 LEU 278 -0.26 LYS 433

GLU 207 0.07 SER 279 -0.25 LYS 433

GLU 207 0.08 SER 280 -0.24 LYS 433

GLU 207 0.09 ILE 281 -0.24 LYS 433

GLU 207 0.07 SER 282 -0.25 LYS 433

GLU 207 0.08 LEU 283 -0.24 LYS 433

GLU 207 0.09 VAL 284 -0.23 LYS 433

ASN 205 0.09 ARG 285 -0.23 LYS 433

ASN 205 0.08 PHE 286 -0.23 LYS 433

ASN 205 0.09 HSD 287 -0.22 LYS 433

ASN 205 0.11 SER 288 -0.22 LYS 433

ASN 205 0.12 GLY 289 -0.21 LYS 433

ASN 205 0.13 SER 290 -0.21 LYS 433

ASN 205 0.14 GLU 291 -0.20 LYS 433

GLU 207 0.12 TRP 292 -0.21 LYS 433

GLU 207 0.11 ALA 293 -0.22 LYS 433

ASN 205 0.13 ASP 294 -0.22 LYS 433

GLU 207 0.14 VAL 295 -0.21 LYS 433

GLU 207 0.13 LEU 296 -0.22 LYS 433

GLU 207 0.12 LEU 297 -0.23 LYS 433

GLU 207 0.15 ARG 298 -0.22 LYS 433

GLU 207 0.15 TYR 299 -0.22 LYS 433

GLU 207 0.13 LEU 300 -0.23 LYS 433

GLU 207 0.13 SER 301 -0.24 LYS 433

GLU 207 0.13 SER 302 -0.25 LYS 433

GLU 207 0.15 GLU 303 -0.24 LYS 433

GLU 207 0.14 GLY 304 -0.23 LYS 433

GLU 207 0.13 ILE 305 -0.23 LYS 433

GLU 207 0.12 LEU 306 -0.23 LYS 433

GLU 207 0.11 TYR 307 -0.24 LYS 433

GLU 207 0.11 VAL 308 -0.25 LYS 433

GLU 207 0.11 SER 309 -0.24 LYS 433

GLU 207 0.10 VAL 310 -0.24 LYS 433

GLU 207 0.09 TYR 311 -0.25 LYS 433

GLU 207 0.08 ILE 312 -0.26 LYS 433

GLU 207 0.08 ALA 313 -0.24 LYS 433

GLU 207 0.07 LEU 314 -0.25 LYS 433

GLU 207 0.06 ILE 315 -0.27 LYS 433

GLU 207 0.06 MET 316 -0.26 LYS 433

GLN 99 0.07 PHE 317 -0.25 LYS 433

GLN 99 0.07 PHE 318 -0.27 LYS 433

GLN 99 0.07 THR 319 -0.28 LYS 433

GLN 99 0.08 PHE 320 -0.28 ALA 421

GLN 99 0.08 PHE 321 -0.28 TYR 419

GLN 99 0.09 TYR 322 -0.30 ALA 421

ASP 254 0.09 THR 323 -0.34 TYR 419

GLN 99 0.08 SER 324 -0.34 TYR 419

GLN 99 0.10 LEU 325 -0.34 TYR 419

ASP 254 0.12 VAL 326 -0.38 TYR 419

ASP 254 0.09 PHE 327 -0.44 TYR 419

ASP 254 0.09 ASP 328 -0.48 TYR 419

ASP 357 0.07 THR 329 -0.47 TYR 419

ASP 357 0.06 LYS 330 -0.47 TYR 419

ASP 254 0.07 GLU 331 -0.54 TYR 419

ASP 254 0.08 THR 332 -0.57 TYR 419

ALA 503 0.05 SER 333 -0.50 TYR 419

ALA 503 0.06 GLU 334 -0.52 TYR 419

ALA 503 0.07 MET 335 -0.60 TYR 419

ALA 503 0.06 LEU 336 -0.54 TYR 419

ALA 503 0.06 LYS 337 -0.48 TYR 419

ALA 503 0.07 LYS 338 -0.51 TYR 419

ALA 503 0.08 ASN 339 -0.52 TYR 419

ALA 503 0.07 GLY 340 -0.43 TYR 419

ALA 503 0.07 GLY 341 -0.46 TYR 419

ALA 503 0.05 PHE 342 -0.40 TYR 419

SER 460 0.06 VAL 343 -0.40 TYR 419

SER 460 0.08 PRO 344 -0.34 TYR 419

VAL 237 0.10 GLY 345 -0.33 TYR 419

LYS 236 0.07 LYS 346 -0.37 TYR 419

GLN 455 0.06 ARG 347 -0.35 TYR 419

GLN 455 0.04 PRO 348 -0.39 TYR 419

GLN 455 0.04 GLY 349 -0.40 TYR 419

GLN 451 0.05 LYS 350 -0.37 TYR 419

GLN 455 0.07 ALA 351 -0.36 TYR 419

GLN 455 0.06 THR 352 -0.40 TYR 419

GLN 455 0.04 LYS 353 -0.41 TYR 419

GLN 451 0.06 GLU 354 -0.37 TYR 419

GLN 455 0.07 TYR 355 -0.37 TYR 419

GLN 455 0.05 PHE 356 -0.41 TYR 419

THR 329 0.07 ASP 357 -0.38 TYR 419

LYS 330 0.05 GLN 358 -0.34 TYR 419

GLU 207 0.05 VAL 359 -0.36 TYR 419

SER 255 0.06 ILE 360 -0.37 TYR 419

GLU 207 0.05 GLY 361 -0.32 TYR 419

GLU 207 0.06 ARG 362 -0.31 TYR 419

SER 255 0.05 ILE 363 -0.33 TYR 419

SER 255 0.06 THR 364 -0.31 TYR 419

GLU 207 0.06 VAL 365 -0.27 ALA 421

GLU 207 0.06 LEU 366 -0.27 ALA 421

SER 255 0.06 GLY 367 -0.28 ALA 421

GLN 99 0.06 ALA 368 -0.26 LYS 433

GLU 207 0.07 ILE 369 -0.24 LYS 433

GLU 207 0.07 TYR 370 -0.25 LYS 433

SER 255 0.06 LEU 371 -0.27 LYS 433

GLU 207 0.08 SER 372 -0.25 LYS 433

GLU 207 0.08 VAL 373 -0.25 LYS 433

GLU 207 0.07 VAL 374 -0.26 LYS 433

GLU 207 0.08 CYS 375 -0.27 LYS 433

GLU 207 0.10 VAL 376 -0.25 LYS 433

GLU 207 0.08 VAL 377 -0.25 LYS 433

GLU 207 0.09 PRO 378 -0.26 LYS 433

GLU 207 0.11 GLU 379 -0.25 LYS 433

GLU 207 0.12 ILE 380 -0.24 LYS 433

GLU 207 0.11 VAL 381 -0.25 LYS 433

GLU 207 0.14 ARG 382 -0.25 TYR 501

GLU 207 0.16 HSD 383 -0.26 TYR 501

GLU 207 0.16 TYR 384 -0.26 TYR 501

GLU 207 0.15 CYS 385 -0.29 TYR 501

GLU 207 0.18 ALA 386 -0.31 TYR 501

LEU 202 0.11 VAL 387 -0.29 TYR 501

LEU 202 0.11 SER 388 -0.30 TYR 501

LEU 202 0.11 PHE 389 -0.27 LYS 433

SER 198 0.07 THR 390 -0.29 LYS 433

LEU 202 0.06 LEU 391 -0.29 LYS 433

GLU 207 0.08 GLY 392 -0.28 LYS 433

GLU 207 0.07 GLY 393 -0.28 LYS 433

SER 253 0.06 THR 394 -0.29 LYS 433

SER 253 0.06 SER 395 -0.30 LYS 433

SER 253 0.07 PHE 396 -0.31 LYS 433

SER 253 0.07 LEU 397 -0.30 LYS 433

SER 253 0.08 ILE 398 -0.32 LYS 433

SER 253 0.08 ILE 399 -0.34 LYS 433

SER 253 0.08 VAL 400 -0.34 LYS 433

SER 253 0.10 ASN 401 -0.33 LYS 433

SER 253 0.09 VAL 402 -0.36 LYS 433

SER 253 0.09 ILE 403 -0.38 LYS 433

GLY 540 0.10 ASN 404 -0.37 LYS 433

SER 253 0.14 ASP 405 -0.36 LYS 433

SER 253 0.11 THR 406 -0.41 LYS 433

SER 253 0.11 PHE 407 -0.41 LYS 433

SER 253 0.14 SER 408 -0.38 LYS 433

SER 253 0.16 GLN 409 -0.39 LYS 433

ALA 503 0.11 VAL 410 -0.46 LYS 433

SER 253 0.11 GLN 411 -0.40 LYS 433

SER 253 0.16 THR 412 -0.36 LYS 433

ALA 503 0.14 GLN 413 -0.44 LYS 433

ALA 503 0.15 VAL 414 -0.45 LYS 433

ALA 503 0.13 TYR 415 -0.41 GLU 331

ALA 503 0.16 SER 416 -0.45 GLU 331

GLY 549 0.31 GLY 417 -0.45 ALA 421

GLY 549 0.25 ARG 418 -0.51 SER 255

GLY 549 0.19 TYR 419 -0.64 SER 255

GLY 549 0.20 SER 420 -0.56 MET 335

ALA 503 0.19 ALA 421 -0.54 SER 255

ALA 503 0.18 LEU 422 -0.62 ASP 254

SER 426 0.21 MET 423 -0.57 ASP 254

ALA 503 0.16 LYS 424 -0.45 ASP 254

ALA 503 0.12 LYS 425 -0.48 SER 255

MET 423 0.21 SER 426 -0.39 ASP 254

ALA 503 0.11 GLU 427 -0.30 ASP 254

ALA 503 0.07 LEU 428 -0.46 LEU 548

LEU 428 0.04 TRP 429 -0.46 ASN 8

TYR 419 0.10 LYS 430 -0.34 ASN 8

THR 246 0.14 LYS 431 -0.43 ALA 9

THR 246 0.09 VAL 432 -0.59 ALA 9

THR 246 0.06 LYS 433 -0.77 ALA 9

GLU 207 0.07 MET 434 -0.20 ALA 421

GLU 207 0.09 PHE 435 -0.20 ALA 421

GLU 207 0.09 LEU 436 -0.20 ALA 421

GLU 207 0.07 ALA 437 -0.22 TYR 419

GLU 207 0.08 MET 438 -0.22 TYR 419

GLU 207 0.09 ILE 439 -0.22 ALA 421

GLU 207 0.08 GLY 440 -0.23 TYR 419

GLU 207 0.07 SER 441 -0.24 TYR 419

GLU 207 0.08 PHE 442 -0.23 TYR 419

GLU 207 0.08 ALA 443 -0.24 TYR 419

GLU 207 0.07 ARG 444 -0.26 TYR 419

GLU 207 0.07 PHE 445 -0.26 TYR 419

GLU 207 0.08 LEU 446 -0.25 ALA 421

GLU 207 0.08 CYS 447 -0.26 TYR 419

GLU 207 0.07 ASP 448 -0.29 TYR 419

GLU 207 0.07 VAL 449 -0.28 TYR 419

GLU 207 0.08 LYS 450 -0.27 ALA 421

TYR 355 0.07 GLN 451 -0.29 TYR 419

GLU 207 0.06 GLU 452 -0.32 TYR 419

GLU 207 0.07 ALA 453 -0.29 ALA 421

GLY 345 0.08 LEU 454 -0.29 ALA 421

GLY 345 0.10 GLN 455 -0.32 TYR 419

GLY 345 0.07 VAL 456 -0.33 ALA 421

GLY 345 0.09 SER 457 -0.34 ALA 421

GLY 345 0.09 TRP 458 -0.30 LYS 425

GLY 345 0.08 ALA 459 -0.29 LYS 425

GLY 345 0.09 SER 460 -0.30 LYS 425

LYS 243 0.08 ARG 461 -0.27 LYS 433

LYS 243 0.09 LYS 462 -0.30 LYS 433

GLY 540 0.09 GLU 463 -0.32 LYS 433

GLY 540 0.08 VAL 464 -0.31 LYS 433

LYS 243 0.07 SER 465 -0.31 LYS 433

GLY 540 0.08 VAL 466 -0.35 LYS 433

GLY 540 0.09 PHE 467 -0.35 LYS 433

GLY 540 0.07 LEU 468 -0.33 LYS 433

SER 253 0.07 LEU 469 -0.36 LYS 433

SER 253 0.07 ILE 470 -0.39 LYS 433

SER 253 0.08 VAL 471 -0.37 LYS 433

SER 253 0.06 LEU 472 -0.36 LYS 433

SER 253 0.06 LEU 473 -0.39 LYS 433

SER 253 0.07 THR 474 -0.40 LYS 433

SER 253 0.07 VAL 475 -0.37 LYS 433

SER 253 0.06 VAL 476 -0.38 LYS 433

VAL 3 0.06 VAL 477 -0.41 LYS 433

SER 253 0.06 SER 478 -0.39 LYS 433

SER 46 0.06 SER 479 -0.37 LYS 433

ARG 6 0.07 ILE 480 -0.38 LYS 433

ARG 6 0.07 LEU 481 -0.39 LYS 433

SER 46 0.06 PHE 482 -0.36 LYS 433

SER 46 0.07 SER 483 -0.35 LYS 433

ARG 6 0.09 CYS 484 -0.36 LYS 433

PHE 12 0.09 VAL 485 -0.35 LYS 433

PHE 12 0.07 ASP 486 -0.33 LYS 433

PHE 12 0.09 PHE 487 -0.32 LYS 433

PHE 12 0.12 VAL 488 -0.32 LYS 433

GLY 16 0.10 PHE 489 -0.30 LYS 433

ALA 9 0.08 LEU 490 -0.29 LYS 433

ALA 9 0.12 ARG 491 -0.28 LYS 433

GLY 601 0.18 LEU 492 -0.27 LYS 433

ALA 9 0.10 VAL 493 -0.26 LYS 433

GLU 608 0.14 LYS 494 -0.33 LEU 201

GLY 606 0.27 ILE 495 -0.27 LEU 201

GLU 608 0.27 ALA 496 -0.24 LEU 201

GLU 608 0.23 LEU 497 -0.32 LEU 201

GLU 608 0.35 GLY 498 -0.44 ASN 205

GLU 608 0.54 VAL 499 -0.34 ASN 205

VAL 574 0.43 VAL 500 -0.32 ASN 205

LEU 578 0.36 TYR 501 -0.46 ASN 205

GLU 608 0.51 ALA 502 -0.50 ASN 205

CYS 509 0.61 ALA 503 -0.40 ASN 205

ALA 503 0.45 MET 504 -0.17 LYS 433

ALA 503 0.55 SER 505 -0.17 LYS 433

ALA 503 0.54 PHE 506 -0.18 LYS 433

ALA 503 0.46 VAL 507 -0.19 LYS 433

ALA 503 0.52 SER 508 -0.18 LYS 433

ALA 503 0.61 CYS 509 -0.19 LYS 433

ALA 503 0.51 LEU 510 -0.21 LYS 433

ALA 503 0.47 MET 511 -0.20 LYS 433

ALA 503 0.55 PHE 512 -0.21 LYS 433

ALA 503 0.57 LEU 513 -0.22 LYS 433

ALA 503 0.46 THR 514 -0.22 LYS 433

ALA 503 0.47 ALA 515 -0.22 LYS 433

ALA 503 0.53 ALA 516 -0.23 LYS 433

ALA 503 0.48 GLN 517 -0.24 LYS 433

ALA 503 0.41 VAL 518 -0.24 LYS 433

ALA 503 0.44 PHE 519 -0.24 LYS 433

ALA 503 0.46 LEU 520 -0.26 LYS 433

ALA 503 0.39 ALA 521 -0.26 LYS 433

ALA 503 0.37 PHE 522 -0.26 LYS 433

ALA 503 0.40 LEU 523 -0.27 LYS 433

ALA 503 0.38 LEU 524 -0.29 LYS 433

ALA 503 0.32 VAL 525 -0.28 LYS 433

ALA 503 0.33 LEU 526 -0.28 LYS 433

ALA 503 0.35 LEU 527 -0.30 LYS 433

ALA 503 0.30 VAL 528 -0.31 LYS 433

ALA 503 0.28 LEU 529 -0.30 LYS 433

ALA 503 0.30 LEU 530 -0.31 LYS 433

ALA 503 0.29 GLN 531 -0.34 LYS 433

ALA 503 0.25 SER 532 -0.33 LYS 433

ALA 503 0.22 PRO 533 -0.36 LYS 433

ALA 503 0.22 GLU 534 -0.36 LYS 433

ALA 503 0.20 SER 535 -0.34 LYS 433

ALA 503 0.19 ASP 536 -0.33 LYS 433

ALA 503 0.18 THR 537 -0.35 LYS 433

ALA 503 0.16 LEU 538 -0.33 LYS 433

SER 253 0.15 GLY 539 -0.31 LYS 433

SER 253 0.18 GLY 540 -0.31 LYS 433

SER 253 0.18 PHE 541 -0.34 LYS 433

SER 253 0.15 GLY 542 -0.37 LYS 433

ALA 503 0.15 GLY 543 -0.41 LYS 433

ALA 503 0.18 PRO 544 -0.46 LYS 433

ALA 503 0.17 GLN 545 -0.47 LYS 433

ALA 503 0.21 CYS 546 -0.58 LYS 433

ALA 503 0.19 ASN 547 -0.60 LYS 433

GLY 417 0.29 LEU 548 -0.70 LYS 433

GLY 417 0.31 GLY 549 -0.70 LYS 433

ALA 503 0.23 SER 550 -0.54 LYS 433

ALA 503 0.24 MET 551 -0.49 LYS 433

ALA 503 0.26 PHE 552 -0.56 LYS 433

ALA 503 0.28 GLY 553 -0.49 LYS 433

ALA 503 0.33 LYS 554 -0.52 LYS 433

ALA 503 0.33 SER 555 -0.44 LYS 433

ALA 503 0.33 SER 556 -0.37 LYS 433

ALA 503 0.31 SER 557 -0.35 LYS 433

ALA 503 0.33 SER 558 -0.36 LYS 433

ALA 503 0.37 SER 559 -0.37 LYS 433

ALA 503 0.39 PHE 560 -0.33 LYS 433

ALA 503 0.37 ILE 561 -0.33 LYS 433

ALA 503 0.36 ALA 562 -0.35 LYS 433

ALA 503 0.42 LYS 563 -0.34 LYS 433

ALA 503 0.43 LEU 564 -0.31 LYS 433

ALA 503 0.39 THR 565 -0.32 LYS 433

ALA 503 0.41 ALA 566 -0.33 LYS 433

ALA 503 0.49 VAL 567 -0.31 LYS 433

ALA 503 0.46 VAL 568 -0.29 LYS 433

ALA 503 0.42 ALA 569 -0.30 LYS 433

ALA 503 0.49 ALA 570 -0.30 LYS 433

ALA 503 0.56 ALA 571 -0.27 LYS 433

ALA 503 0.46 PHE 572 -0.27 LYS 433

ALA 503 0.44 ILE 573 -0.28 LYS 433

ALA 503 0.58 VAL 574 -0.26 LYS 433

ALA 503 0.56 ASN 575 -0.25 LYS 433

ALA 503 0.43 THR 576 -0.25 LYS 433

ALA 503 0.45 ILE 577 -0.25 LYS 433

ALA 503 0.59 LEU 578 -0.24 LYS 433

ALA 503 0.46 LEU 579 -0.23 LYS 433

ALA 503 0.32 VAL 580 -0.23 LYS 433

ALA 503 0.39 GLY 581 -0.23 LYS 433

ALA 503 0.44 THR 582 -0.22 LYS 433

ALA 503 0.28 ASN 583 -0.22 LYS 433

ALA 503 0.14 ALA 584 -0.22 LYS 433

ALA 9 0.06 ARG 585 -0.22 LYS 433

GLY 16 0.05 ARG 586 -0.22 LYS 433

GLY 16 0.06 VAL 587 -0.22 LYS 433

GLY 16 0.06 ARG 588 -0.24 LYS 433

ALA 503 0.09 GLU 589 -0.24 LYS 433

GLY 16 0.07 VAL 590 -0.24 LYS 433

GLY 16 0.07 SER 591 -0.25 LYS 433

ALA 503 0.11 VAL 592 -0.26 LYS 433

ALA 503 0.22 VAL 593 -0.25 LYS 433

ALA 503 0.09 SER 594 -0.26 LYS 433

VAL 499 0.10 LYS 595 -0.28 LYS 433

ALA 503 0.23 THR 596 -0.28 LYS 433

VAL 499 0.32 GLU 597 -0.27 LYS 433

VAL 499 0.18 ALA 598 -0.29 LYS 433

VAL 499 0.18 VAL 599 -0.31 LYS 433

VAL 499 0.29 SER 600 -0.32 LYS 433

VAL 499 0.32 GLY 601 -0.31 LYS 433

VAL 499 0.24 GLN 602 -0.34 LYS 433

VAL 499 0.29 GLU 603 -0.35 LYS 433

VAL 499 0.41 SER 604 -0.33 LYS 433

VAL 499 0.37 ASN 605 -0.35 LYS 433

VAL 499 0.48 GLY 606 -0.32 LYS 433

ALA 503 0.49 SER 607 -0.33 LYS 433

ALA 503 0.60 GLU 608 -0.30 LYS 433

ALA 503 0.58 VAL 609 -0.30 LYS 433

ALA 503 0.60 PRO 610 -0.27 LYS 433

ALA 503 0.54 PHE 611 -0.28 LYS 433

ALA 503 0.54 GLU 612 -0.26 LYS 433

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** secyeg_itasser ***

CA distance fluctuations for 260811042802127475

--- normal mode 16 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* secyeg_itasser *