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

* 5csc_open_aligned *

CA distance fluctuations for 2604241127051943378

--- 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
ALA 321 0.04 ALA 1 -0.07 GLY 44

ALA 321 0.05 SER 2 -0.07 GLY 44

ALA 321 0.06 SER 3 -0.07 GLY 44

ALA 321 0.07 THR 4 -0.07 GLY 44

ALA 321 0.08 ASN 5 -0.08 GLY 44

ALA 321 0.08 LEU 6 -0.09 GLY 44

ALA 321 0.09 LYS 7 -0.09 GLY 44

ALA 321 0.09 ASP 8 -0.08 GLY 44

ALA 321 0.10 VAL 9 -0.08 GLY 44

ALA 321 0.11 LEU 10 -0.08 GLY 44

ALA 321 0.11 ALA 11 -0.07 GLY 44

ALA 321 0.12 ALA 12 -0.06 GLY 44

ALA 321 0.12 LEU 13 -0.08 GLU 17

ALA 321 0.14 ILE 14 -0.06 GLY 44

LEU 33 0.14 PRO 15 -0.05 GLY 44

LEU 33 0.14 LYS 16 -0.05 GLY 44

LEU 33 0.16 GLU 17 -0.08 LEU 13

LEU 33 0.17 GLN 18 -0.06 GLY 44

LEU 33 0.14 ALA 19 -0.06 GLY 44

LEU 33 0.17 ARG 20 -0.12 GLY 99

LEU 33 0.20 ILE 21 -0.13 GLY 99

LEU 33 0.13 LYS 22 -0.11 VAL 52

PRO 422 0.12 THR 23 -0.12 VAL 52

LEU 33 0.13 PHE 24 -0.19 GLU 54

PRO 422 0.16 ARG 25 -0.21 VAL 52

PRO 422 0.16 GLN 26 -0.16 GLY 50

PRO 422 0.15 GLN 27 -0.18 GLY 50

PRO 422 0.12 HIS 28 -0.25 GLY 50

PRO 422 0.16 GLY 29 -0.29 GLY 50

PRO 422 0.21 GLY 30 -0.25 GLY 50

PRO 422 0.18 THR 31 -0.17 GLY 50

PRO 422 0.18 ALA 32 -0.20 LYS 423

PRO 422 0.24 LEU 33 -0.13 LYS 423

ALA 368 0.16 GLY 34 -0.25 LYS 423

PRO 422 0.15 GLN 35 -0.26 LYS 423

PRO 422 0.16 ILE 36 -0.27 LYS 423

PRO 422 0.11 THR 37 -0.17 LEU 273

PRO 418 0.07 VAL 38 -0.20 LEU 273

ILE 431 0.06 ASP 39 -0.26 LEU 273

ALA 367 0.12 MET 40 -0.27 LYS 423

ALA 367 0.12 SER 41 -0.31 LYS 423

ALA 367 0.11 TYR 42 -0.25 LEU 273

ALA 367 0.16 GLY 43 -0.33 LEU 273

ALA 367 0.21 GLY 44 -0.45 PRO 422

ALA 321 0.23 MET 45 -0.40 LYS 423

ALA 367 0.22 ARG 46 -0.29 ASN 242

ALA 321 0.27 GLY 47 -0.27 LYS 423

ALA 321 0.23 MET 48 -0.32 LYS 423

ALA 321 0.27 LYS 49 -0.28 LYS 423

ALA 321 0.26 GLY 50 -0.29 GLY 29

ALA 321 0.25 LEU 51 -0.25 GLY 29

ALA 321 0.25 VAL 52 -0.27 GLY 29

ALA 321 0.23 TYR 53 -0.21 GLY 29

ALA 321 0.19 GLU 54 -0.20 GLY 29

ALA 321 0.15 THR 55 -0.18 HIS 28

ALA 321 0.17 SER 56 -0.18 HIS 28

LEU 58 0.28 VAL 57 -0.19 HIS 28

VAL 57 0.28 LEU 58 -0.18 ARG 46

LYS 355 0.15 ASP 59 -0.14 LYS 423

LYS 355 0.16 PRO 60 -0.13 LYS 423

LYS 355 0.20 ASP 61 -0.12 HIS 28

LYS 355 0.20 GLU 62 -0.13 HIS 28

LYS 355 0.18 GLY 63 -0.12 HIS 28

LYS 355 0.16 ILE 64 -0.15 HIS 28

LYS 355 0.15 ARG 65 -0.17 HIS 28

LYS 355 0.13 PHE 66 -0.17 HIS 28

LYS 355 0.13 ARG 67 -0.19 HIS 28

LYS 355 0.14 GLY 68 -0.19 HIS 28

LYS 355 0.14 PHE 69 -0.16 HIS 28

LYS 355 0.16 SER 70 -0.15 HIS 28

LYS 355 0.15 ILE 71 -0.13 HIS 28

LYS 355 0.16 PRO 72 -0.13 HIS 28

LYS 355 0.15 GLU 73 -0.14 HIS 28

LYS 355 0.13 CYS 74 -0.13 HIS 28

LYS 355 0.11 GLN 75 -0.12 HIS 28

LYS 355 0.11 LYS 76 -0.12 HIS 28

LYS 355 0.11 LEU 77 -0.12 HIS 28

LYS 355 0.09 LEU 78 -0.12 HIS 28

LYS 355 0.07 PRO 79 -0.11 HIS 28

LYS 355 0.05 LYS 80 -0.10 HIS 28

LYS 355 0.03 GLY 81 -0.09 PRO 422

ASN 212 0.03 GLY 82 -0.09 HIS 28

GLU 389 0.03 GLY 84 -0.09 HIS 28

LYS 339 0.05 GLY 85 -0.10 HIS 28

LYS 355 0.05 GLU 86 -0.10 HIS 28

LYS 355 0.07 PRO 87 -0.11 HIS 28

LYS 355 0.06 LEU 88 -0.11 PRO 422

LYS 355 0.06 PRO 89 -0.12 PRO 422

LYS 355 0.06 GLU 90 -0.11 PRO 422

LYS 355 0.07 GLY 91 -0.11 HIS 28

LYS 355 0.09 LEU 92 -0.12 HIS 28

ALA 321 0.09 PHE 93 -0.12 PRO 422

LYS 355 0.08 TRP 94 -0.11 HIS 28

LYS 355 0.10 LEU 95 -0.13 HIS 28

ALA 321 0.11 LEU 96 -0.14 HIS 28

ALA 321 0.11 VAL 97 -0.13 PHE 24

ALA 321 0.10 THR 98 -0.14 PHE 24

LYS 355 0.11 GLY 99 -0.17 PHE 24

LYS 355 0.10 GLN 100 -0.14 PHE 24

LYS 355 0.10 ILE 101 -0.13 HIS 28

LYS 355 0.08 PRO 102 -0.11 PHE 24

LYS 355 0.08 THR 103 -0.10 HIS 28

LYS 355 0.06 GLY 104 -0.09 HIS 28

LYS 355 0.05 ALA 105 -0.08 GLY 43

LYS 355 0.06 GLN 106 -0.08 PHE 24

LYS 355 0.06 VAL 107 -0.09 GLY 43

ALA 321 0.04 SER 108 -0.09 GLY 43

ALA 321 0.05 TRP 109 -0.09 GLY 44

ALA 321 0.06 LEU 110 -0.10 GLY 44

ALA 321 0.05 SER 111 -0.10 GLY 43

ALA 321 0.05 LYS 112 -0.09 GLY 43

ALA 321 0.06 GLU 113 -0.09 GLY 44

ALA 321 0.06 TRP 114 -0.10 PRO 422

ALA 321 0.05 ALA 115 -0.10 PRO 422

ALA 321 0.05 LYS 116 -0.09 GLY 43

ALA 321 0.06 ARG 117 -0.10 PRO 422

ALA 321 0.05 ALA 118 -0.11 PRO 422

ALA 321 0.05 ALA 119 -0.11 PRO 422

ALA 321 0.05 LEU 120 -0.12 PRO 422

ALA 321 0.05 PRO 121 -0.12 LYS 290

ALA 321 0.04 SER 122 -0.14 LYS 290

ALA 321 0.05 HIS 123 -0.13 LYS 290

ALA 321 0.05 VAL 124 -0.14 PRO 422

ALA 119 0.04 VAL 125 -0.15 LYS 290

ALA 321 0.03 THR 126 -0.15 LYS 290

ALA 321 0.04 MET 127 -0.15 LYS 290

ALA 119 0.03 LEU 128 -0.16 LYS 290

ILE 203 0.03 ASP 129 -0.18 LYS 290

ILE 203 0.03 ASN 130 -0.18 LYS 290

THR 220 0.03 PHE 131 -0.18 LYS 290

THR 220 0.03 PRO 132 -0.20 LYS 290

TYR 219 0.03 THR 133 -0.23 LYS 290

TYR 219 0.03 ASN 134 -0.22 LYS 290

TYR 219 0.04 LEU 135 -0.19 PRO 422

TYR 219 0.05 HIS 136 -0.21 PRO 422

TYR 219 0.05 PRO 137 -0.20 PRO 422

TYR 219 0.05 MET 138 -0.23 PRO 422

TYR 219 0.04 SER 139 -0.22 PRO 422

ALA 321 0.04 GLN 140 -0.20 PRO 422

ALA 321 0.05 LEU 141 -0.20 PRO 422

ALA 321 0.06 SER 142 -0.23 PRO 422

ALA 321 0.06 ALA 143 -0.20 PRO 422

ALA 321 0.06 ALA 144 -0.18 PRO 422

ALA 321 0.07 ILE 145 -0.18 PRO 422

ALA 321 0.08 THR 146 -0.19 PRO 422

ALA 321 0.07 ALA 147 -0.16 PRO 422

ALA 321 0.07 LEU 148 -0.15 PRO 422

ALA 321 0.08 ASN 149 -0.14 PRO 422

ALA 321 0.07 SER 150 -0.11 PRO 422

ALA 321 0.07 GLU 151 -0.10 PRO 422

ALA 321 0.09 SER 152 -0.10 GLY 44

ALA 321 0.09 ASN 153 -0.09 GLY 44

ALA 321 0.10 PHE 154 -0.10 GLY 44

ALA 321 0.10 ALA 155 -0.09 GLY 44

ALA 321 0.09 ARG 156 -0.08 GLY 44

LEU 33 0.10 ALA 157 -0.08 GLY 44

LEU 33 0.11 TYR 158 -0.07 GLY 44

LYS 423 0.11 ALA 159 -0.06 GLY 44

LEU 33 0.11 GLU 160 -0.06 GLY 44

LEU 33 0.13 GLY 161 -0.05 GLY 44

LEU 33 0.13 ILE 162 -0.06 GLY 44

LEU 33 0.14 LEU 163 -0.06 GLY 44

LEU 33 0.16 ARG 164 -0.07 GLY 44

LEU 33 0.15 THR 165 -0.06 GLY 44

LEU 33 0.13 LYS 166 -0.07 GLY 44

LEU 33 0.13 TYR 167 -0.08 GLY 44

ALA 321 0.13 TRP 168 -0.09 GLY 44

ALA 321 0.11 GLU 169 -0.09 GLY 44

ALA 321 0.11 MET 170 -0.09 GLY 44

ALA 321 0.11 VAL 171 -0.11 GLY 44

ALA 321 0.11 TYR 172 -0.11 GLY 44

ALA 321 0.09 GLU 173 -0.10 GLY 44

ALA 321 0.09 SER 174 -0.11 GLY 44

ALA 321 0.10 ALA 175 -0.12 GLY 44

ALA 321 0.08 MET 176 -0.11 GLY 44

ALA 321 0.08 ASP 177 -0.12 PRO 422

ALA 321 0.08 LEU 178 -0.14 PRO 422

ALA 321 0.07 ILE 179 -0.14 PRO 422

ALA 321 0.06 ALA 180 -0.12 PRO 422

ALA 321 0.06 LYS 181 -0.14 PRO 422

ALA 321 0.06 LEU 182 -0.16 PRO 422

ALA 321 0.04 PRO 183 -0.15 PRO 422

ALA 321 0.04 CYS 184 -0.14 PRO 422

ALA 321 0.04 VAL 185 -0.16 PRO 422

ALA 321 0.03 ALA 186 -0.17 PRO 422

THR 220 0.02 ALA 187 -0.16 LYS 290

ASP 129 0.03 LYS 188 -0.17 LYS 290

TYR 219 0.04 ILE 189 -0.17 LYS 290

TYR 219 0.06 TYR 190 -0.20 LYS 290

THR 220 0.04 ARG 191 -0.21 LYS 290

THR 220 0.03 ASN 192 -0.20 LYS 290

TYR 219 0.05 LEU 193 -0.23 LYS 290

TYR 219 0.07 TYR 194 -0.26 LYS 290

THR 220 0.05 ARG 195 -0.25 LYS 290

THR 220 0.03 ALA 196 -0.25 LYS 290

THR 133 0.03 GLY 197 -0.22 LYS 290

ASN 130 0.03 SER 198 -0.21 LYS 290

ASP 129 0.02 SER 199 -0.18 LYS 290

ASP 129 0.03 ILE 200 -0.16 LYS 290

ASP 129 0.02 GLY 201 -0.15 LYS 290

ASP 129 0.03 ALA 202 -0.13 LYS 290

ASP 129 0.03 ILE 203 -0.11 LYS 290

ALA 321 0.03 ASP 204 -0.10 LYS 290

ALA 321 0.04 SER 205 -0.09 PRO 422

ALA 321 0.03 LYS 206 -0.09 GLY 43

ALA 321 0.03 LEU 207 -0.10 PRO 422

ALA 321 0.03 ASP 208 -0.10 PRO 422

ALA 321 0.04 TRP 209 -0.12 PRO 422

ALA 321 0.03 SER 210 -0.13 PRO 422

GLY 82 0.03 HIS 211 -0.12 PRO 422

GLY 82 0.03 ASN 212 -0.12 PRO 422

ALA 321 0.03 PHE 213 -0.13 PRO 422

TYR 194 0.03 THR 214 -0.13 PRO 422

GLY 82 0.03 ASN 215 -0.13 LYS 290

GLY 82 0.02 MET 216 -0.14 LYS 290

THR 220 0.04 LEU 217 -0.16 LYS 290

THR 220 0.05 GLY 218 -0.17 LYS 290

GLU 389 0.09 TYR 219 -0.13 LYS 290

GLU 389 0.07 THR 220 -0.11 LYS 290

GLU 389 0.06 ASP 221 -0.13 ASP 344

GLU 389 0.05 ALA 222 -0.10 PRO 422

GLU 389 0.05 GLN 223 -0.11 LEU 341

GLU 389 0.06 PHE 224 -0.11 PRO 422

GLU 389 0.05 THR 225 -0.11 PRO 422

GLU 389 0.04 GLU 226 -0.11 PRO 422

GLU 389 0.05 LEU 227 -0.12 PRO 422

TYR 219 0.04 MET 228 -0.13 PRO 422

LYS 355 0.03 ARG 229 -0.12 PRO 422

LYS 355 0.05 LEU 230 -0.12 PRO 422

LYS 355 0.05 TYR 231 -0.14 PRO 422

LYS 355 0.05 LEU 232 -0.15 PRO 422

LYS 355 0.08 THR 233 -0.13 PRO 422

LYS 355 0.10 ILE 234 -0.14 PRO 422

LYS 355 0.08 HIS 235 -0.17 PRO 422

ALA 321 0.09 SER 236 -0.16 PRO 422

ALA 321 0.15 ASP 237 -0.18 PRO 422

ALA 321 0.20 HIS 238 -0.20 ARG 46

ALA 321 0.26 GLU 239 -0.21 ARG 46

ALA 321 0.27 GLY 240 -0.23 PRO 422

ALA 321 0.32 GLY 241 -0.31 PRO 422

ALA 321 0.26 ASN 242 -0.32 PRO 422

ALA 321 0.19 VAL 243 -0.38 PRO 422

ALA 321 0.16 SER 244 -0.32 PRO 422

ALA 321 0.19 ALA 245 -0.30 PRO 422

ALA 321 0.22 HIS 246 -0.39 PRO 422

ALA 321 0.17 THR 247 -0.40 PRO 422

ALA 321 0.16 SER 248 -0.29 PRO 422

ALA 321 0.18 HIS 249 -0.29 PRO 422

ALA 321 0.18 LEU 250 -0.40 PRO 422

ALA 321 0.15 VAL 251 -0.31 PRO 422

ALA 321 0.15 GLY 252 -0.21 PRO 422

ALA 321 0.16 SER 253 -0.15 PRO 422

ALA 321 0.14 ALA 254 -0.13 PRO 422

ALA 321 0.14 LEU 255 -0.10 GLY 44

ALA 321 0.12 SER 256 -0.15 PRO 422

ALA 321 0.11 ASP 257 -0.13 PRO 422

ALA 321 0.12 PRO 258 -0.16 PRO 422

ALA 321 0.10 TYR 259 -0.18 PRO 422

ALA 321 0.11 LEU 260 -0.20 PRO 422

ALA 321 0.12 SER 261 -0.24 PRO 422

ALA 321 0.11 PHE 262 -0.24 PRO 422

ALA 321 0.09 ALA 263 -0.25 PRO 422

ALA 321 0.11 ALA 264 -0.31 PRO 422

ALA 321 0.12 ALA 265 -0.31 PRO 422

ALA 321 0.09 MET 266 -0.28 PRO 422

ALA 321 0.08 ASN 267 -0.31 PRO 422

ALA 321 0.11 GLY 268 -0.35 PRO 422

ALA 321 0.09 LEU 269 -0.29 PRO 422

GLY 319 0.05 ALA 270 -0.28 PRO 422

GLY 319 0.06 GLY 271 -0.30 PRO 422

TYR 219 0.04 PRO 272 -0.29 GLY 43

GLY 319 0.06 LEU 273 -0.33 GLY 43

GLY 319 0.09 HIS 274 -0.29 GLY 43

PRO 372 0.05 GLY 275 -0.25 PRO 422

TYR 219 0.04 LEU 276 -0.22 PRO 422

VAL 281 0.05 ALA 277 -0.19 PRO 422

VAL 243 0.04 ASN 278 -0.17 PRO 422

GLN 383 0.03 GLN 279 -0.18 PRO 422

LEU 273 0.03 GLU 280 -0.17 PRO 422

ASN 242 0.06 VAL 281 -0.16 ILE 305

GLY 50 0.03 LEU 282 -0.15 PRO 422

PRO 345 0.04 GLY 283 -0.17 TYR 304

GLY 50 0.06 TRP 284 -0.23 TYR 304

THR 331 0.07 LEU 285 -0.16 SER 300

ARG 313 0.05 ALA 286 -0.24 THR 388

ARG 313 0.11 GLN 287 -0.20 GLU 389

VAL 315 0.20 LEU 288 -0.18 THR 388

VAL 315 0.13 GLN 289 -0.24 THR 388

ARG 313 0.15 LYS 290 -0.26 TYR 194

ARG 313 0.18 ALA 291 -0.21 TYR 194

THR 326 0.10 ALA 295 -0.17 ALA 196

LYS 325 0.12 GLY 296 -0.16 ALA 196

LYS 325 0.13 ALA 297 -0.14 ALA 196

LYS 325 0.16 ASP 298 -0.12 ALA 196

LYS 325 0.15 ALA 299 -0.14 TRP 284

LYS 325 0.12 SER 300 -0.19 TRP 284

LYS 325 0.12 LEU 301 -0.19 TRP 284

LYS 325 0.14 ARG 302 -0.16 TRP 284

LYS 325 0.12 ASP 303 -0.17 TRP 284

ALA 291 0.12 TYR 304 -0.23 TRP 284

ALA 291 0.14 ILE 305 -0.21 TRP 284

LYS 325 0.10 TRP 306 -0.15 TRP 284

ALA 291 0.12 ASN 307 -0.15 TRP 284

ALA 291 0.18 THR 308 -0.15 TRP 284

ALA 291 0.13 LEU 309 -0.10 GLU 280

ALA 291 0.11 ASN 310 -0.11 ASN 134

ALA 291 0.14 SER 311 -0.13 ASN 134

ALA 291 0.14 GLY 312 -0.11 ASP 39

ALA 291 0.18 ARG 313 -0.14 ASP 39

LEU 288 0.18 VAL 314 -0.12 ASP 39

LEU 288 0.20 VAL 315 -0.19 PRO 316

LEU 288 0.12 PRO 316 -0.19 VAL 315

ASN 242 0.12 GLY 317 -0.10 ASP 39

GLY 241 0.15 TYR 318 -0.08 GLY 319

GLY 241 0.21 GLY 319 -0.08 TYR 318

GLY 241 0.25 HIS 320 -0.09 VAL 314

GLY 241 0.32 ALA 321 -0.12 ALA 366

VAL 52 0.22 VAL 322 -0.08 ASP 39

VAL 52 0.17 LEU 323 -0.08 LYS 423

ASN 359 0.18 ARG 324 -0.07 LYS 423

LYS 355 0.25 LYS 325 -0.07 HIS 28

LYS 355 0.27 THR 326 -0.08 HIS 28

LYS 355 0.18 ASP 327 -0.09 HIS 28

LYS 355 0.20 PRO 328 -0.10 HIS 28

LYS 355 0.14 ARG 329 -0.10 PRO 422

LYS 355 0.15 TYR 330 -0.10 PRO 422

LYS 355 0.19 THR 331 -0.09 HIS 28

LYS 355 0.13 CYS 332 -0.09 HIS 28

ALA 351 0.07 GLN 333 -0.10 PRO 422

CYS 332 0.09 ARG 334 -0.10 PRO 372

PRO 72 0.10 GLU 335 -0.09 TRP 371

GLN 75 0.06 PHE 336 -0.09 PRO 422

PRO 72 0.05 ALA 337 -0.09 PRO 422

LYS 76 0.08 LEU 338 -0.08 PRO 422

LYS 76 0.07 LYS 339 -0.08 PRO 422

TYR 385 0.05 HIS 340 -0.09 PRO 422

PRO 72 0.03 LEU 341 -0.12 ASP 221

PRO 72 0.06 PRO 342 -0.09 ASP 221

PRO 72 0.06 GLY 343 -0.11 ASP 221

THR 331 0.06 ASP 344 -0.13 ARG 195

THR 331 0.07 PRO 345 -0.15 ARG 195

THR 331 0.08 MET 346 -0.15 ARG 195

THR 331 0.10 PHE 347 -0.11 ARG 195

THR 331 0.12 LYS 348 -0.11 ARG 195

THR 331 0.11 LEU 349 -0.13 ARG 195

THR 331 0.13 VAL 350 -0.11 THR 388

THR 331 0.18 ALA 351 -0.09 ARG 195

THR 326 0.16 GLN 352 -0.10 ARG 195

THR 326 0.15 LEU 353 -0.09 THR 388

THR 326 0.24 TYR 354 -0.07 ARG 195

THR 326 0.27 LYS 355 -0.07 ARG 195

LYS 325 0.21 ILE 356 -0.10 TRP 284

LYS 325 0.17 VAL 357 -0.09 PRO 316

LYS 325 0.22 PRO 358 -0.06 LEU 338

LYS 325 0.22 ASN 359 -0.07 THR 388

LYS 325 0.15 VAL 360 -0.11 PRO 316

GLY 47 0.14 LEU 361 -0.08 PRO 316

GLY 47 0.18 LEU 362 -0.06 THR 388

GLY 47 0.16 GLU 363 -0.06 ARG 195

GLY 47 0.14 GLN 364 -0.08 PRO 316

ARG 46 0.19 GLY 365 -0.07 ALA 321

GLY 44 0.18 ALA 366 -0.12 ALA 321

GLY 47 0.23 ALA 367 -0.06 GLU 335

GLY 47 0.24 ALA 368 -0.06 GLU 335

GLY 241 0.19 ASN 369 -0.06 GLU 335

GLY 241 0.18 PRO 370 -0.07 GLU 335

GLY 241 0.17 TRP 371 -0.09 GLU 335

GLY 241 0.16 PRO 372 -0.10 ARG 334

HIS 238 0.15 ASN 373 -0.09 ASP 39

LYS 355 0.09 VAL 374 -0.12 PRO 422

ASN 242 0.09 ASP 375 -0.14 PRO 422

ASN 242 0.09 ALA 376 -0.11 PRO 422

ASN 242 0.07 HIS 377 -0.11 PRO 422

ASN 242 0.05 SER 378 -0.13 PRO 422

VAL 243 0.03 GLY 379 -0.15 PRO 422

ASN 242 0.03 VAL 380 -0.13 PRO 422

HIS 340 0.03 LEU 381 -0.13 PRO 422

HIS 340 0.04 LEU 382 -0.14 PRO 422

GLN 279 0.03 GLN 383 -0.14 GLN 289

HIS 340 0.04 TYR 384 -0.14 GLY 218

HIS 340 0.05 TYR 385 -0.15 GLY 218

GLN 223 0.04 GLY 386 -0.17 ARG 195

THR 388 0.12 MET 387 -0.16 LEU 217

MET 387 0.12 THR 388 -0.25 LYS 290

TYR 219 0.09 GLU 389 -0.24 LYS 290

TYR 219 0.05 MET 390 -0.20 ALA 286

TYR 219 0.07 ASN 391 -0.19 PRO 422

TYR 219 0.08 TYR 392 -0.19 PRO 422

TYR 219 0.07 TYR 393 -0.19 PRO 422

TYR 219 0.06 THR 394 -0.21 PRO 422

TYR 219 0.06 VAL 395 -0.20 PRO 422

TYR 219 0.07 LEU 396 -0.18 PRO 422

TYR 219 0.05 PHE 397 -0.20 PRO 422

ALA 321 0.07 GLY 398 -0.22 PRO 422

ALA 321 0.06 VAL 399 -0.19 PRO 422

ALA 321 0.07 SER 400 -0.18 PRO 422

ALA 321 0.11 ARG 401 -0.20 PRO 422

ALA 321 0.10 ALA 402 -0.19 PRO 422

ALA 321 0.10 LEU 403 -0.16 PRO 422

ALA 321 0.13 GLY 404 -0.17 PRO 422

ALA 321 0.15 VAL 405 -0.20 PRO 422

ALA 321 0.13 LEU 406 -0.16 PRO 422

ALA 321 0.13 ALA 407 -0.13 GLY 44

ALA 321 0.16 GLN 408 -0.14 GLY 44

ALA 321 0.15 LEU 409 -0.14 GLY 44

ALA 321 0.14 ILE 410 -0.12 GLY 44

ALA 321 0.16 TRP 411 -0.11 GLY 44

ALA 321 0.17 SER 412 -0.11 GLY 44

ALA 321 0.15 ARG 413 -0.10 GLY 44

ALA 321 0.15 ALA 414 -0.08 GLY 44

LEU 33 0.18 LEU 415 -0.07 GLY 44

LEU 33 0.19 GLY 416 -0.07 GLY 44

LEU 33 0.20 PHE 417 -0.07 GLY 44

LEU 33 0.21 PRO 418 -0.06 GLY 44

ALA 321 0.17 LEU 419 -0.09 GLY 44

ALA 321 0.18 GLU 420 -0.14 PRO 422

ALA 321 0.16 ARG 421 -0.09 GLY 44

LEU 33 0.24 PRO 422 -0.45 GLY 44

GLY 161 0.12 LYS 423 -0.40 MET 45

ALA 368 0.12 SER 424 -0.08 GLY 429

ALA 368 0.09 MET 425 -0.11 GLY 271

ALA 367 0.08 SER 426 -0.09 PRO 272

ALA 367 0.08 THR 427 -0.08 PRO 272

ALA 367 0.06 ASP 428 -0.10 GLN 35

ALA 367 0.06 GLY 429 -0.12 GLN 35

ALA 367 0.05 LEU 430 -0.17 ILE 36

TYR 42 0.11 ILE 431 -0.15 GLN 35

TYR 42 0.05 ALA 432 -0.20 GLN 35

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.

*** 5csc_open_aligned ***

CA distance fluctuations for 2604241127051943378

--- 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.

* 5csc_open_aligned *