Should you encounter any unexpected behaviour,
please let us know.

* tdp183p *

CA distance fluctuations for 22120809540522465

--- 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 increase ref largest decrease
ILE 383 0.12 MET 1 -0.05 LYS 408

ALA 321 0.12 SER 2 -0.08 LYS 408

ALA 321 0.13 GLU 3 -0.10 SER 407

ALA 321 0.14 TYR 4 -0.13 SER 407

ALA 321 0.14 ILE 5 -0.16 SER 407

ALA 321 0.16 ARG 6 -0.19 SER 407

ALA 321 0.16 VAL 7 -0.20 SER 407

ALA 321 0.17 THR 8 -0.22 SER 407

ALA 321 0.18 GLU 9 -0.21 SER 407

ALA 321 0.20 ASP 10 -0.24 SER 407

ALA 321 0.21 GLU 11 -0.27 SER 407

ALA 321 0.22 ASN 12 -0.27 SER 407

ALA 321 0.20 ASP 13 -0.24 SER 407

ALA 321 0.19 GLU 14 -0.22 SER 407

ALA 321 0.17 PRO 15 -0.21 SER 407

ALA 321 0.16 ILE 16 -0.18 SER 407

ALA 321 0.15 GLU 17 -0.16 SER 407

ALA 321 0.14 ILE 18 -0.14 SER 407

ALA 321 0.13 PRO 19 -0.12 SER 407

ALA 321 0.13 SER 20 -0.11 LYS 408

ALA 321 0.12 GLU 21 -0.09 LYS 408

ALA 321 0.11 ASP 22 -0.07 LYS 408

ALA 321 0.11 ASP 23 -0.07 LYS 408

ALA 321 0.12 GLY 24 -0.09 LYS 408

ALA 321 0.12 THR 25 -0.11 LYS 408

ALA 321 0.13 VAL 26 -0.13 LYS 408

ALA 321 0.12 LEU 27 -0.12 LYS 408

ALA 321 0.13 LEU 28 -0.14 SER 410

ALA 321 0.13 SER 29 -0.13 SER 410

ALA 321 0.13 THR 30 -0.13 LYS 408

ALA 321 0.14 VAL 31 -0.15 SER 407

ALA 321 0.14 THR 32 -0.15 SER 407

ALA 321 0.13 ALA 33 -0.14 SER 407

ALA 321 0.14 GLN 34 -0.15 SER 407

ALA 321 0.15 PHE 35 -0.16 SER 407

ALA 321 0.14 PRO 36 -0.15 SER 407

ALA 325 0.14 GLY 37 -0.16 SER 410

ALA 325 0.14 ALA 38 -0.17 SER 410

ALA 325 0.14 CYS 39 -0.17 SER 410

ALA 325 0.14 GLY 40 -0.19 SER 410

ALA 325 0.15 LEU 41 -0.20 SER 410

ALA 325 0.16 ARG 42 -0.24 SER 410

ALA 325 0.16 TYR 43 -0.27 SER 410

ALA 325 0.17 ARG 44 -0.32 SER 410

ALA 325 0.16 ASN 45 -0.36 SER 410

ALA 321 0.16 PRO 46 -0.39 SER 410

ALA 328 0.15 VAL 47 -0.50 SER 410

MET 336 0.16 SER 48 -0.48 SER 410

ALA 325 0.18 GLN 49 -0.42 SER 410

GLY 335 0.18 CYS 50 -0.38 SER 410

ALA 325 0.17 MET 51 -0.32 SER 410

GLY 335 0.16 ARG 52 -0.29 SER 410

GLY 335 0.15 GLY 53 -0.24 SER 410

GLY 335 0.14 VAL 54 -0.21 SER 410

GLY 335 0.14 ARG 55 -0.18 SER 410

GLY 335 0.13 LEU 56 -0.16 SER 410

GLY 335 0.13 VAL 57 -0.14 SER 410

GLY 335 0.12 GLU 58 -0.12 SER 410

GLY 335 0.12 GLY 59 -0.13 SER 410

ALA 325 0.12 ILE 60 -0.13 SER 410

ALA 325 0.13 LEU 61 -0.15 SER 410

GLY 335 0.12 HIS 62 -0.14 SER 410

ALA 321 0.13 ALA 63 -0.15 SER 410

MET 336 0.13 PRO 64 -0.18 SER 410

MET 336 0.13 ASP 65 -0.16 SER 410

ALA 321 0.12 ALA 66 -0.16 SER 410

ALA 321 0.13 GLY 67 -0.14 LYS 408

ALA 321 0.14 TRP 68 -0.16 LYS 408

ALA 321 0.14 GLY 69 -0.18 LYS 408

ALA 321 0.15 ASN 70 -0.22 SER 407

ALA 321 0.16 LEU 71 -0.24 SER 407

ALA 321 0.17 VAL 72 -0.25 SER 407

ALA 321 0.16 TYR 73 -0.22 LYS 408

ALA 321 0.17 VAL 74 -0.23 SER 410

ALA 321 0.16 VAL 75 -0.20 SER 410

ALA 325 0.16 ASN 76 -0.21 SER 410

ALA 325 0.16 TYR 77 -0.19 SER 410

ALA 329 0.15 PRO 78 -0.19 SER 410

ALA 329 0.16 LYS 79 -0.20 SER 410

TRP 334 0.15 ASP 80 -0.18 SER 410

TRP 334 0.15 ASN 81 -0.18 SER 410

TRP 334 0.14 LYS 82 -0.17 SER 410

TRP 334 0.14 ARG 83 -0.16 SER 410

TRP 334 0.13 LYS 84 -0.15 SER 410

TRP 334 0.12 MET 85 -0.14 SER 410

TRP 334 0.11 ASP 86 -0.13 SER 410

TRP 334 0.11 GLU 87 -0.12 SER 410

TRP 334 0.11 THR 88 -0.12 SER 410

ALA 325 0.11 ASP 89 -0.12 SER 410

MET 322 0.11 ALA 90 -0.12 SER 410

MET 322 0.12 SER 91 -0.13 SER 410

MET 322 0.13 SER 92 -0.14 SER 407

MET 322 0.14 ALA 93 -0.15 SER 407

MET 322 0.14 VAL 94 -0.16 SER 410

MET 322 0.16 LYS 95 -0.17 SER 407

MET 322 0.16 VAL 96 -0.19 SER 410

MET 322 0.18 LYS 97 -0.20 SER 407

MET 322 0.19 ARG 98 -0.20 SER 407

MET 322 0.20 ALA 99 -0.21 SER 407

MET 322 0.20 VAL 100 -0.20 PHE 401

MET 322 0.18 GLN 101 -0.19 PHE 401

MET 322 0.19 LYS 102 -0.20 PHE 401

ILE 318 0.18 THR 103 -0.19 GLY 399

ILE 318 0.17 SER 104 -0.20 PHE 397

ILE 318 0.16 ASP 105 -0.20 PHE 397

ILE 318 0.14 LEU 106 -0.18 PHE 397

ALA 326 0.12 ILE 107 -0.18 PHE 397

ILE 318 0.11 VAL 108 -0.17 PHE 397

ALA 326 0.10 LEU 109 -0.16 PHE 397

ALA 326 0.09 GLY 110 -0.16 PHE 397

PHE 313 0.09 LEU 111 -0.16 PHE 397

PHE 313 0.08 PRO 112 -0.16 GLY 394

MET 311 0.08 TRP 113 -0.17 GLY 394

MET 311 0.08 LYS 114 -0.17 TRP 385

PHE 313 0.09 THR 115 -0.17 GLY 394

PHE 313 0.11 THR 116 -0.19 GLY 394

PHE 313 0.12 GLU 117 -0.20 GLY 394

PHE 313 0.12 GLN 118 -0.19 GLY 394

PHE 313 0.11 ASP 119 -0.18 GLY 394

PHE 313 0.11 LEU 120 -0.18 GLY 394

PHE 316 0.12 LYS 121 -0.18 GLY 394

PHE 316 0.11 GLU 122 -0.17 GLY 394

PHE 316 0.11 TYR 123 -0.16 PHE 397

PHE 316 0.12 PHE 124 -0.16 PHE 397

PHE 316 0.13 SER 125 -0.17 PHE 397

PHE 316 0.12 THR 126 -0.15 PHE 397

PHE 316 0.12 PHE 127 -0.15 PHE 397

PHE 316 0.13 GLY 128 -0.16 PHE 397

PHE 316 0.15 GLU 129 -0.18 PHE 397

PHE 316 0.15 VAL 130 -0.19 PHE 397

PHE 316 0.17 LEU 131 -0.21 PHE 397

PHE 316 0.17 MET 132 -0.21 PHE 397

PHE 316 0.14 VAL 133 -0.20 GLY 394

PHE 313 0.14 GLN 134 -0.21 GLY 394

PHE 313 0.12 VAL 135 -0.20 GLY 394

MET 311 0.11 LYS 136 -0.20 GLY 394

GLY 309 0.11 LYS 137 -0.20 GLY 394

ASN 302 0.11 ASP 138 -0.19 GLY 392

ASN 302 0.13 LEU 139 -0.21 TRP 385

ASN 302 0.14 LYS 140 -0.22 TRP 385

ASN 302 0.12 THR 141 -0.22 TRP 385

ASN 302 0.11 GLY 142 -0.22 TRP 385

ASN 302 0.10 HIS 143 -0.20 TRP 385

GLY 309 0.09 SER 144 -0.18 GLY 394

ASN 302 0.09 LYS 145 -0.18 GLY 394

MET 311 0.08 GLY 146 -0.17 GLY 394

PHE 313 0.09 PHE 147 -0.17 PHE 397

PHE 313 0.11 GLY 148 -0.18 PHE 397

PHE 316 0.13 PHE 149 -0.19 PHE 397

PHE 316 0.14 VAL 150 -0.19 PHE 397

PHE 316 0.16 ARG 151 -0.20 PHE 397

PHE 316 0.16 PHE 152 -0.19 PHE 397

PHE 316 0.17 THR 153 -0.19 PHE 397

ILE 318 0.16 GLU 154 -0.17 GLY 399

MET 322 0.16 TYR 155 -0.17 PHE 401

MET 322 0.14 GLU 156 -0.16 PHE 401

ILE 318 0.14 THR 157 -0.16 GLY 399

ILE 318 0.14 GLN 158 -0.16 GLY 399

MET 322 0.14 VAL 159 -0.15 SER 407

MET 322 0.12 LYS 160 -0.14 PHE 401

MET 322 0.12 VAL 161 -0.15 PHE 397

MET 322 0.12 MET 162 -0.15 PHE 401

MET 322 0.12 SER 163 -0.14 SER 407

MET 322 0.11 GLN 164 -0.14 PHE 401

ALA 326 0.10 ARG 165 -0.14 PHE 397

ILE 318 0.10 HIS 166 -0.14 PHE 397

ILE 318 0.09 MET 167 -0.14 PHE 397

PHE 316 0.09 ILE 168 -0.15 PHE 397

PHE 313 0.08 ASP 169 -0.15 GLY 394

PHE 316 0.07 GLY 170 -0.14 GLY 394

ILE 318 0.08 ARG 171 -0.14 PHE 397

ALA 326 0.08 TRP 172 -0.14 PHE 397

ALA 326 0.09 CYS 173 -0.15 PHE 397

ALA 326 0.10 ASP 174 -0.15 PHE 397

ALA 326 0.12 CYS 175 -0.16 PHE 397

ALA 326 0.13 LYS 176 -0.16 PHE 397

ALA 326 0.14 LEU 177 -0.17 PHE 401

ALA 326 0.14 PRO 178 -0.18 PHE 397

ALA 326 0.15 ASN 179 -0.18 PHE 401

ALA 326 0.17 SER 180 -0.20 PHE 397

ALA 326 0.16 LYS 181 -0.21 PHE 397

ILE 318 0.18 GLN 182 -0.23 PHE 397

ILE 318 0.20 S1P 183 -0.25 PHE 397

MET 323 0.17 GLN 184 -0.24 PHE 397

ILE 318 0.24 ASP 185 -0.26 PHE 397

MET 323 0.26 GLU 186 -0.24 PHE 397

ALA 326 0.26 PRO 187 -0.22 PHE 401

ALA 326 0.21 LEU 188 -0.21 PHE 401

ALA 326 0.23 ARG 189 -0.21 PHE 401

ALA 326 0.20 SER 190 -0.19 PHE 401

ALA 326 0.19 ARG 191 -0.19 SER 410

LEU 330 0.19 LYS 192 -0.19 SER 410

LEU 330 0.22 VAL 193 -0.20 SER 410

SER 333 0.23 PHE 194 -0.20 SER 410

SER 333 0.25 VAL 195 -0.21 SER 410

SER 333 0.28 GLY 196 -0.21 TRP 412

TRP 334 0.28 ARG 197 -0.22 TRP 412

TRP 334 0.24 CYS 198 -0.21 TRP 412

TRP 334 0.22 THR 199 -0.20 TRP 412

TRP 334 0.18 GLU 200 -0.19 TRP 412

TRP 334 0.18 ASP 201 -0.19 TRP 412

TRP 334 0.19 MET 202 -0.19 TRP 412

TRP 334 0.17 THR 203 -0.18 TRP 412

SER 333 0.16 GLU 204 -0.18 TRP 412

TRP 334 0.16 ASP 205 -0.18 TRP 412

TRP 334 0.18 GLU 206 -0.19 TRP 412

SER 333 0.19 LEU 207 -0.20 TRP 412

SER 333 0.18 ARG 208 -0.19 SER 410

TRP 334 0.18 GLU 209 -0.19 SER 410

TRP 334 0.20 PHE 210 -0.21 SER 410

SER 333 0.20 PHE 211 -0.21 SER 410

SER 333 0.18 SER 212 -0.20 SER 410

SER 333 0.19 GLN 213 -0.21 SER 410

ALA 329 0.20 TYR 214 -0.22 SER 410

ALA 329 0.19 GLY 215 -0.20 SER 410

ALA 329 0.17 ASP 216 -0.19 SER 410

ALA 329 0.17 VAL 217 -0.19 SER 410

ALA 329 0.15 MET 218 -0.18 SER 410

SER 333 0.15 ASP 219 -0.17 SER 410

SER 333 0.16 VAL 220 -0.18 SER 410

SER 333 0.16 PHE 221 -0.17 SER 410

SER 333 0.16 ILE 222 -0.18 TRP 412

SER 333 0.14 PRO 223 -0.17 TRP 412

SER 333 0.12 LYS 224 -0.16 TRP 412

SER 333 0.12 PRO 225 -0.16 TRP 412

TRP 334 0.15 PHE 226 -0.18 TRP 412

SER 333 0.16 ARG 227 -0.18 TRP 412

TRP 334 0.20 ALA 228 -0.19 TRP 412

SER 333 0.21 PHE 229 -0.19 TRP 412

SER 333 0.20 ALA 230 -0.19 TRP 412

SER 333 0.19 PHE 231 -0.19 SER 410

SER 333 0.19 VAL 232 -0.19 SER 410

LEU 330 0.17 THR 233 -0.19 SER 410

ALA 329 0.18 PHE 234 -0.19 SER 410

ALA 326 0.17 ALA 235 -0.18 SER 410

ALA 326 0.19 ASP 236 -0.19 SER 407

ALA 326 0.21 ASP 237 -0.20 PHE 401

ALA 326 0.24 GLN 238 -0.21 SER 407

ALA 326 0.22 ILE 239 -0.22 SER 410

ALA 329 0.23 ALA 240 -0.21 SER 410

ALA 326 0.27 GLN 241 -0.22 SER 407

ALA 329 0.28 SER 242 -0.24 SER 410

ALA 329 0.27 LEU 243 -0.24 SER 410

ALA 329 0.30 CYS 244 -0.23 SER 410

ALA 329 0.36 GLY 245 -0.24 SER 410

SER 333 0.32 GLU 246 -0.25 SER 410

SER 333 0.33 ASP 247 -0.26 SER 410

TRP 334 0.28 LEU 248 -0.25 TRP 412

TRP 334 0.28 ILE 249 -0.25 TRP 412

TRP 334 0.24 ILE 250 -0.23 TRP 412

TRP 334 0.23 LYS 251 -0.23 TRP 412

GLY 335 0.26 GLY 252 -0.25 TRP 412

TRP 334 0.28 ILE 253 -0.24 TRP 412

TRP 334 0.32 SER 254 -0.25 TRP 412

TRP 334 0.30 VAL 255 -0.23 TRP 412

SER 333 0.33 HIS 256 -0.23 TRP 412

SER 333 0.29 ILE 257 -0.23 SER 410

LEU 330 0.29 SER 258 -0.22 SER 410

LEU 330 0.26 ASN 259 -0.21 SER 410

LEU 330 0.21 ALA 260 -0.19 SER 410

LEU 330 0.19 GLU 261 -0.18 SER 410

LEU 330 0.15 PRO 262 -0.17 SER 410

LEU 330 0.12 LYS 263 -0.17 SER 410

LEU 330 0.10 HIS 264 -0.16 SER 410

PRO 349 0.08 ASN 265 -0.16 SER 410

PRO 349 0.08 SER 266 -0.15 SER 410

PRO 349 0.07 ASN 267 -0.15 PHE 401

PRO 349 0.08 ARG 268 -0.15 PHE 401

PRO 349 0.06 GLN 269 -0.14 PHE 397

SER 350 0.06 LEU 270 -0.14 PHE 397

PHE 316 0.23 GLU 271 -0.26 PHE 397

SER 350 0.07 ARG 272 -0.14 PHE 397

GLY 351 0.08 SER 273 -0.14 PHE 401

SER 350 0.08 GLY 274 -0.14 SER 403

SER 350 0.09 ARG 275 -0.14 SER 410

PRO 349 0.08 PHE 276 -0.14 TRP 412

PRO 349 0.09 GLY 277 -0.14 TRP 412

PRO 349 0.07 GLY 278 -0.14 TRP 412

PRO 349 0.06 ASN 279 -0.13 TRP 412

PRO 349 0.04 PRO 280 -0.13 TRP 412

PRO 349 0.03 GLY 281 -0.13 TRP 412

PRO 349 0.03 GLY 282 -0.12 TRP 412

PRO 349 0.02 PHE 283 -0.12 TRP 412

PRO 349 0.02 GLY 284 -0.12 TRP 412

PRO 349 0.02 ASN 285 -0.12 TRP 412

PRO 349 0.01 GLN 286 -0.11 TRP 412

PRO 349 0.01 GLY 287 -0.11 SER 410

PRO 349 0.01 GLY 288 -0.11 PHE 397

GLN 269 0.01 PHE 289 -0.11 PHE 397

THR 141 0.02 GLY 290 -0.12 ILE 383

THR 141 0.03 ASN 291 -0.12 ILE 383

THR 141 0.03 SER 292 -0.13 ILE 383

THR 141 0.04 ARG 293 -0.13 ILE 383

THR 141 0.05 GLY 294 -0.14 ILE 383

THR 141 0.06 GLY 295 -0.15 ILE 383

THR 141 0.08 GLY 296 -0.16 ALA 381

LYS 140 0.09 ALA 297 -0.15 ALA 381

LYS 140 0.10 GLY 298 -0.16 GLY 380

LYS 140 0.11 LEU 299 -0.16 GLY 380

LYS 140 0.13 GLY 300 -0.17 GLY 380

LYS 140 0.13 ASN 301 -0.16 GLY 380

LYS 140 0.14 ASN 302 -0.17 GLY 380

LYS 140 0.13 GLN 303 -0.16 TYR 374

LYS 140 0.13 GLY 304 -0.18 TYR 374

LEU 139 0.12 SER 305 -0.19 TYR 374

GLN 184 0.13 ASN 306 -0.20 ASN 372

GLU 271 0.13 MET 307 -0.23 TYR 374

GLU 271 0.14 GLY 308 -0.24 ASN 372

GLU 271 0.16 GLY 309 -0.23 ASN 372

GLU 271 0.17 GLY 310 -0.23 SER 369

GLU 271 0.19 MET 311 -0.22 SER 369

GLU 271 0.19 ASN 312 -0.22 SER 369

GLU 271 0.22 PHE 313 -0.21 GLY 396

GLU 271 0.21 GLY 314 -0.21 GLY 396

GLU 271 0.21 ALA 315 -0.21 ASN 398

GLU 271 0.23 PHE 316 -0.25 ASN 398

GLU 271 0.20 SER 317 -0.23 ASN 398

ASP 185 0.24 ILE 318 -0.22 ASN 398

ASN 12 0.21 ASN 319 -0.22 GLY 400

GLU 186 0.21 PRO 320 -0.18 SER 403

ASN 12 0.22 ALA 321 -0.20 SER 403

SER 242 0.25 MET 322 -0.20 SER 403

GLU 186 0.26 MET 323 -0.17 SER 403

SER 242 0.23 ALA 324 -0.15 SER 403

SER 242 0.27 ALA 325 -0.17 SER 403

GLY 245 0.29 ALA 326 -0.17 SER 403

GLY 245 0.27 GLN 327 -0.14 SER 403

GLY 245 0.29 ALA 328 -0.14 SER 403

GLY 245 0.36 ALA 329 -0.15 SER 403

GLY 245 0.34 LEU 330 -0.13 SER 403

GLY 245 0.31 GLN 331 -0.12 SER 404

GLY 245 0.31 SER 332 -0.12 SER 409

ASP 247 0.33 SER 333 -0.14 GLY 413

ASP 247 0.33 TRP 334 -0.14 GLY 413

SER 254 0.30 GLY 335 -0.13 GLY 413

SER 254 0.26 MET 336 -0.11 GLY 413

SER 254 0.24 MET 337 -0.10 GLY 413

SER 254 0.21 GLY 338 -0.08 GLY 413

SER 254 0.19 MET 339 -0.05 GLY 413

SER 254 0.17 LEU 340 -0.04 GLY 413

SER 254 0.16 ALA 341 -0.03 GLY 413

SER 254 0.15 SER 342 -0.02 GLY 413

SER 254 0.14 GLN 343 -0.02 GLY 413

SER 254 0.13 GLN 344 -0.02 GLY 413

ASP 247 0.13 ASN 345 -0.02 GLY 413

ASP 247 0.12 GLN 346 -0.02 GLY 413

GLY 245 0.12 SER 347 -0.02 GLY 413

GLY 245 0.12 GLY 348 -0.02 GLY 413

GLY 245 0.12 PRO 349 -0.02 GLY 413

GLY 245 0.11 SER 350 -0.02 GLY 413

GLY 245 0.11 GLY 351 -0.02 GLY 413

GLY 245 0.11 ASN 352 -0.02 GLY 413

GLY 245 0.10 ASN 353 -0.02 GLY 413

ASP 185 0.10 GLN 354 -0.02 GLY 413

ASP 185 0.10 ASN 355 -0.02 GLN 303

ASP 185 0.09 GLN 356 -0.03 SER 305

GLN 49 0.09 GLY 357 -0.05 ASN 306

VAL 47 0.09 ASN 358 -0.06 ASN 306

VAL 47 0.09 MET 359 -0.07 GLY 310

VAL 47 0.09 GLN 360 -0.09 GLY 310

VAL 47 0.09 ARG 361 -0.10 GLY 310

VAL 47 0.09 GLU 362 -0.13 ASN 312

VAL 47 0.09 PRO 363 -0.15 ASN 312

VAL 47 0.09 ASN 364 -0.17 ASN 312

VAL 47 0.09 GLN 365 -0.19 ASN 312

VAL 47 0.09 ALA 366 -0.21 ASN 312

VAL 47 0.09 PHE 367 -0.21 ASN 312

PRO 46 0.09 GLY 368 -0.21 GLY 310

PRO 46 0.09 SER 369 -0.23 GLY 310

ASN 70 0.09 GLY 370 -0.22 GLY 310

ASN 70 0.10 ASN 371 -0.23 GLY 309

GLU 14 0.10 ASN 372 -0.24 GLY 308

GLU 14 0.10 SER 373 -0.22 GLY 308

GLU 14 0.11 TYR 374 -0.23 MET 307

GLU 14 0.11 SER 375 -0.20 MET 307

GLU 14 0.11 GLY 376 -0.19 MET 307

GLU 14 0.11 SER 377 -0.17 GLY 304

GLU 14 0.12 ASN 378 -0.17 GLY 304

GLU 14 0.12 SER 379 -0.17 GLY 304

GLU 14 0.13 GLY 380 -0.17 ASN 302

GLU 14 0.13 ALA 381 -0.18 LYS 140

GLU 14 0.12 ALA 382 -0.18 LYS 140

GLU 14 0.13 ILE 383 -0.21 LYS 140

GLU 14 0.12 GLY 384 -0.20 LYS 140

GLU 14 0.12 TRP 385 -0.22 GLY 142

ASN 70 0.11 GLY 386 -0.21 GLY 142

ASN 70 0.10 SER 387 -0.21 GLY 142

ASN 70 0.10 ALA 388 -0.21 LEU 139

ASN 70 0.10 SER 389 -0.20 LEU 139

ASN 70 0.10 ASN 390 -0.21 LEU 139

MET 1 0.09 ALA 391 -0.21 GLU 271

MET 1 0.09 GLY 392 -0.24 GLU 271

MET 1 0.08 SER 393 -0.23 GLU 271

MET 1 0.08 GLY 394 -0.25 GLU 271

MET 1 0.07 SER 395 -0.25 GLU 271

MET 1 0.07 GLY 396 -0.25 GLU 271

MET 1 0.07 PHE 397 -0.26 GLU 271

MET 1 0.06 ASN 398 -0.25 ASP 185

MET 1 0.05 GLY 399 -0.25 ASP 185

MET 1 0.03 GLY 400 -0.24 ASP 185

MET 1 0.02 PHE 401 -0.24 ASP 185

MET 1 0.01 GLY 402 -0.23 ASP 185

MET 1 0.00 SER 403 -0.22 GLU 186

SER 369 0.00 SER 404 -0.24 ASN 12

SER 369 0.00 MET 405 -0.27 GLN 49

PHE 367 0.00 ASP 406 -0.31 GLN 49

PHE 367 0.00 SER 407 -0.39 VAL 47

PHE 367 0.00 LYS 408 -0.43 VAL 47

PHE 367 0.00 SER 409 -0.44 VAL 47

PHE 367 0.00 SER 410 -0.50 VAL 47

PHE 367 0.00 GLY 411 -0.41 SER 48

PHE 367 0.00 TRP 412 -0.41 SER 48

PHE 367 0.00 GLY 413 -0.32 SER 48

PHE 367 0.00 MET 414 -0.30 SER 48

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).
Last modification: October 18th, 2018.

Should you encounter any unexpected behaviour, please let us know.

*** tdp183p ***

CA distance fluctuations for 22120809540522465

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.

* tdp183p *