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

* TBC_AF *

CA strain for 2609111810563696908

--- normal mode 9 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
MET 1 ASP 2 0.0002

ASP 2 SER 3 -0.0003

SER 3 PRO 4 -0.0158

PRO 4 GLY 5 -0.0000

GLY 5 TYR 6 -0.0002

TYR 6 ASN 7 0.0128

ASN 7 CYS 8 -0.0003

CYS 8 PHE 9 -0.0001

PHE 9 VAL 10 0.0022

VAL 10 ASP 11 0.0002

ASP 11 LYS 12 0.0000

LYS 12 ASP 13 -0.0021

ASP 13 LYS 14 -0.0003

LYS 14 MET 15 -0.0003

MET 15 ASP 16 -0.0039

ASP 16 ALA 17 -0.0004

ALA 17 ALA 18 0.0003

ALA 18 ILE 19 -0.0026

ILE 19 GLN 20 0.0003

GLN 20 ASP 21 0.0001

ASP 21 LEU 22 -0.0017

LEU 22 GLY 23 0.0000

GLY 23 PRO 24 -0.0002

PRO 24 LYS 25 0.0028

LYS 25 GLU 26 0.0000

GLU 26 LEU 27 -0.0000

LEU 27 SER 28 -0.0031

SER 28 CYS 29 -0.0002

CYS 29 THR 30 0.0003

THR 30 GLU 31 -0.0013

GLU 31 LEU 32 -0.0002

LEU 32 GLN 33 -0.0003

GLN 33 GLU 34 -0.0040

GLU 34 LEU 35 -0.0001

LEU 35 LYS 36 0.0002

LYS 36 GLN 37 -0.0021

GLN 37 LEU 38 -0.0001

LEU 38 ALA 39 -0.0001

ALA 39 ARG 40 0.0093

ARG 40 GLN 41 0.0000

GLN 41 GLY 42 0.0002

GLY 42 TYR 43 0.0090

TYR 43 TRP 44 0.0004

TRP 44 ALA 45 0.0003

ALA 45 GLN 46 0.0065

GLN 46 SER 47 0.0001

SER 47 HIS 48 0.0000

HIS 48 ALA 49 -0.0095

ALA 49 LEU 50 0.0005

LEU 50 ARG 51 -0.0001

ARG 51 GLY 52 -0.0030

GLY 52 LYS 53 -0.0003

LYS 53 VAL 54 0.0002

VAL 54 TYR 55 -0.0022

TYR 55 GLN 56 -0.0001

GLN 56 ARG 57 -0.0000

ARG 57 LEU 58 0.0099

LEU 58 ILE 59 -0.0000

ILE 59 ARG 60 -0.0003

ARG 60 ASP 61 0.0106

ASP 61 ILE 62 -0.0002

ILE 62 PRO 63 0.0002

PRO 63 CYS 64 0.0024

CYS 64 ARG 65 0.0004

ARG 65 THR 66 0.0000

THR 66 VAL 67 0.0010

VAL 67 THR 68 -0.0001

THR 68 PRO 69 -0.0001

PRO 69 ASP 70 -0.0035

ASP 70 ALA 71 -0.0001

ALA 71 SER 72 -0.0002

SER 72 VAL 73 -0.0056

VAL 73 TYR 74 0.0002

TYR 74 SER 75 -0.0001

SER 75 ASP 76 -0.0026

ASP 76 ILE 77 -0.0001

ILE 77 VAL 78 -0.0003

VAL 78 GLY 79 0.0016

GLY 79 LYS 80 0.0001

LYS 80 ILE 81 -0.0002

ILE 81 VAL 82 0.0012

VAL 82 GLY 83 -0.0002

GLY 83 LYS 84 0.0000

LYS 84 HIS 85 -0.0044

HIS 85 SER 86 0.0001

SER 86 SER 87 0.0000

SER 87 SER 88 0.0037

SER 88 CYS 89 0.0002

CYS 89 LEU 90 -0.0000

LEU 90 PRO 91 -0.0160

PRO 91 LEU 92 0.0001

LEU 92 PRO 93 0.0002

PRO 93 GLU 94 -0.0481

GLU 94 PHE 95 0.0002

PHE 95 VAL 96 0.0002

VAL 96 ASP 97 -0.0036

ASP 97 ASN 98 0.0002

ASN 98 THR 99 0.0000

THR 99 GLN 100 -0.0011

GLN 100 VAL 101 -0.0003

VAL 101 PRO 102 0.0002

PRO 102 SER 103 -0.0215

SER 103 TYR 104 0.0001

TYR 104 CYS 105 -0.0002

CYS 105 LEU 106 0.0044

LEU 106 ASN 107 -0.0001

ASN 107 ALA 108 -0.0003

ALA 108 ARG 109 0.0029

ARG 109 GLY 110 -0.0002

GLY 110 GLU 111 -0.0002

GLU 111 GLY 112 0.0043

GLY 112 ALA 113 -0.0001

ALA 113 VAL 114 -0.0001

VAL 114 ARG 115 0.0026

ARG 115 LYS 116 -0.0002

LYS 116 ILE 117 -0.0002

ILE 117 LEU 118 -0.0105

LEU 118 LEU 119 -0.0001

LEU 119 CYS 120 0.0001

CYS 120 LEU 121 0.0002

LEU 121 ALA 122 0.0000

ALA 122 ASN 123 0.0001

ASN 123 GLN 124 0.0035

GLN 124 PHE 125 -0.0001

PHE 125 PRO 126 0.0000

PRO 126 ASP 127 -0.0098

ASP 127 ILE 128 0.0001

ILE 128 SER 129 -0.0000

SER 129 PHE 130 -0.0008

PHE 130 CYS 131 -0.0004

CYS 131 PRO 132 0.0001

PRO 132 ALA 133 -0.0000

ALA 133 LEU 134 0.0001

LEU 134 PRO 135 -0.0001

PRO 135 ALA 136 0.0018

ALA 136 VAL 137 -0.0001

VAL 137 VAL 138 -0.0004

VAL 138 ALA 139 0.0014

ALA 139 LEU 140 -0.0002

LEU 140 LEU 141 0.0000

LEU 141 LEU 142 0.0094

LEU 142 HIS 143 0.0000

HIS 143 TYR 144 -0.0002

TYR 144 SER 145 -0.0007

SER 145 ILE 146 0.0003

ILE 146 ASP 147 0.0002

ASP 147 GLU 148 -0.0067

GLU 148 ALA 149 0.0003

ALA 149 GLU 150 0.0001

GLU 150 CYS 151 -0.0032

CYS 151 PHE 152 0.0000

PHE 152 GLU 153 0.0001

GLU 153 LYS 154 0.0011

LYS 154 ALA 155 -0.0000

ALA 155 CYS 156 -0.0004

CYS 156 ARG 157 0.0062

ARG 157 ILE 158 -0.0001

ILE 158 LEU 159 -0.0000

LEU 159 ALA 160 -0.0007

ALA 160 CYS 161 -0.0001

CYS 161 ASN 162 -0.0001

ASN 162 ASP 163 0.0143

ASP 163 PRO 164 -0.0002

PRO 164 GLY 165 0.0000

GLY 165 ARG 166 0.0144

ARG 166 ARG 167 -0.0001

ARG 167 LEU 168 -0.0001

LEU 168 ILE 169 -0.0071

ILE 169 ASP 170 -0.0003

ASP 170 GLN 171 0.0003

GLN 171 SER 172 -0.0302

SER 172 PHE 173 0.0001

PHE 173 LEU 174 0.0000

LEU 174 ALA 175 0.0023

ALA 175 PHE 176 0.0003

PHE 176 GLU 177 0.0002

GLU 177 SER 178 0.0053

SER 178 SER 179 0.0001

SER 179 CYS 180 0.0001

CYS 180 MET 181 -0.0105

MET 181 THR 182 0.0002

THR 182 PHE 183 0.0001

PHE 183 GLY 184 0.0026

GLY 184 ASP 185 0.0000

ASP 185 LEU 186 0.0000

LEU 186 VAL 187 -0.0064

VAL 187 ASN 188 0.0001

ASN 188 LYS 189 0.0002

LYS 189 TYR 190 0.0160

TYR 190 CYS 191 0.0004

CYS 191 GLN 192 -0.0004

GLN 192 ALA 193 -0.0069

ALA 193 ALA 194 0.0002

ALA 194 HIS 195 0.0002

HIS 195 LYS 196 0.0081

LYS 196 LEU 197 -0.0001

LEU 197 MET 198 -0.0002

MET 198 VAL 199 -0.0000

VAL 199 ALA 200 0.0001

ALA 200 VAL 201 -0.0003

VAL 201 SER 202 0.0190

SER 202 GLU 203 0.0002

GLU 203 ASP 204 0.0003

ASP 204 VAL 205 -0.0017

VAL 205 LEU 206 0.0002

LEU 206 GLN 207 -0.0004

GLN 207 VAL 208 0.0053

VAL 208 TYR 209 -0.0006

TYR 209 ALA 210 -0.0002

ALA 210 ASP 211 -0.0157

ASP 211 TRP 212 0.0002

TRP 212 GLN 213 0.0000

GLN 213 ARG 214 0.0128

ARG 214 TRP 215 -0.0000

TRP 215 LEU 216 -0.0001

LEU 216 PHE 217 0.0069

PHE 217 GLY 218 0.0001

GLY 218 GLU 219 -0.0003

GLU 219 LEU 220 -0.0106

LEU 220 PRO 221 0.0001

PRO 221 LEU 222 0.0003

LEU 222 CYS 223 0.0103

CYS 223 TYR 224 -0.0005

TYR 224 PHE 225 -0.0002

PHE 225 ALA 226 -0.0206

ALA 226 ARG 227 -0.0003

ARG 227 VAL 228 -0.0002

VAL 228 PHE 229 0.0018

PHE 229 ASP 230 -0.0002

ASP 230 VAL 231 0.0004

VAL 231 PHE 232 -0.0059

PHE 232 LEU 233 -0.0000

LEU 233 VAL 234 -0.0002

VAL 234 GLU 235 0.0285

GLU 235 GLY 236 0.0002

GLY 236 TYR 237 -0.0001

TYR 237 LYS 238 0.0064

LYS 238 VAL 239 -0.0002

VAL 239 LEU 240 0.0004

LEU 240 TYR 241 0.0105

TYR 241 ARG 242 -0.0003

ARG 242 VAL 243 0.0002

VAL 243 ALA 244 0.0046

ALA 244 LEU 245 -0.0001

LEU 245 ALA 246 -0.0003

ALA 246 ILE 247 0.0068

ILE 247 LEU 248 0.0003

LEU 248 LYS 249 -0.0000

LYS 249 PHE 250 0.0028

PHE 250 PHE 251 -0.0001

PHE 251 HIS 252 -0.0000

HIS 252 LYS 253 -0.0008

LYS 253 VAL 254 -0.0004

VAL 254 ARG 255 -0.0001

ARG 255 ALA 256 0.0009

ALA 256 GLY 257 -0.0000

GLY 257 GLN 258 -0.0001

GLN 258 PRO 259 0.0022

PRO 259 LEU 260 -0.0005

LEU 260 GLU 261 -0.0000

GLU 261 SER 262 0.0032

SER 262 ASP 263 0.0003

ASP 263 SER 264 0.0002

SER 264 VAL 265 0.0034

VAL 265 LYS 266 -0.0002

LYS 266 GLN 267 -0.0001

GLN 267 ASP 268 0.0074

ASP 268 ILE 269 -0.0002

ILE 269 ARG 270 -0.0002

ARG 270 THR 271 0.0065

THR 271 PHE 272 -0.0002

PHE 272 VAL 273 0.0001

VAL 273 ARG 274 0.0071

ARG 274 ASP 275 -0.0002

ASP 275 ILE 276 0.0002

ILE 276 ALA 277 0.0017

ALA 277 LYS 278 0.0004

LYS 278 THR 279 0.0001

THR 279 VAL 280 -0.0020

VAL 280 SER 281 0.0001

SER 281 PRO 282 0.0004

PRO 282 GLU 283 0.0019

GLU 283 LYS 284 -0.0004

LYS 284 LEU 285 -0.0002

LEU 285 LEU 286 -0.0029

LEU 286 GLU 287 0.0003

GLU 287 LYS 288 -0.0000

LYS 288 ALA 289 -0.0140

ALA 289 PHE 290 -0.0003

PHE 290 ALA 291 -0.0002

ALA 291 ILE 292 0.0252

ILE 292 ARG 293 -0.0001

ARG 293 LEU 294 0.0002

LEU 294 PHE 295 0.0451

PHE 295 SER 296 0.0000

SER 296 ARG 297 0.0000

ARG 297 LYS 298 0.0617

LYS 298 GLU 299 0.0002

GLU 299 ILE 300 0.0002

ILE 300 GLN 301 -0.0190

GLN 301 LEU 302 -0.0001

LEU 302 LEU 303 -0.0003

LEU 303 GLN 304 0.0198

GLN 304 MET 305 0.0000

MET 305 ALA 306 -0.0001

ALA 306 ASN 307 0.0048

ASN 307 GLU 308 0.0002

GLU 308 LYS 309 -0.0001

LYS 309 ALA 310 0.0002

ALA 310 LEU 311 -0.0002

LEU 311 LYS 312 0.0003

LYS 312 GLN 313 0.0018

GLN 313 LYS 314 0.0001

LYS 314 GLY 315 0.0000

GLY 315 ILE 316 -0.0120

ILE 316 THR 317 0.0003

THR 317 VAL 318 -0.0004

VAL 318 LYS 319 -0.0005

LYS 319 GLN 320 -0.0003

GLN 320 LYS 321 0.0001

LYS 321 SER 322 -0.0003

SER 322 VAL 323 0.0000

VAL 323 SER 324 -0.0003

SER 324 LEU 325 0.0147

LEU 325 SER 326 0.0001

SER 326 LYS 327 -0.0002

LYS 327 ARG 328 -0.0101

ARG 328 GLN 329 0.0004

GLN 329 PHE 330 0.0000

PHE 330 VAL 331 -0.0501

VAL 331 HIS 332 0.0004

HIS 332 LEU 333 -0.0003

LEU 333 ALA 334 -0.0099

ALA 334 VAL 335 0.0003

VAL 335 HIS 336 0.0001

HIS 336 ALA 337 -0.0084

ALA 337 GLU 338 -0.0001

GLU 338 ASN 339 0.0000

ASN 339 PHE 340 -0.0018

PHE 340 ARG 341 -0.0002

ARG 341 SER 342 0.0001

SER 342 GLU 343 -0.0171

GLU 343 ILE 344 -0.0001

ILE 344 VAL 345 -0.0002

VAL 345 SER 346 -0.0074

SER 346 VAL 347 0.0001

VAL 347 ARG 348 0.0002

ARG 348 GLU 349 -0.0023

GLU 349 MET 350 0.0005

MET 350 ARG 351 0.0000

ARG 351 ASP 352 0.0004

ASP 352 ILE 353 0.0002

ILE 353 TRP 354 -0.0001

TRP 354 SER 355 0.0154

SER 355 TRP 356 0.0002

TRP 356 VAL 357 0.0002

VAL 357 PRO 358 0.0026

PRO 358 GLU 359 0.0002

GLU 359 ARG 360 0.0004

ARG 360 PHE 361 -0.0078

PHE 361 ALA 362 0.0002

ALA 362 LEU 363 0.0000

LEU 363 CYS 364 -0.0152

CYS 364 GLN 365 -0.0001

GLN 365 PRO 366 -0.0003

PRO 366 LEU 367 -0.0072

LEU 367 LEU 368 0.0004

LEU 368 LEU 369 0.0000

LEU 369 PHE 370 -0.0176

PHE 370 SER 371 0.0001

SER 371 SER 372 -0.0001

SER 372 LEU 373 -0.0007

LEU 373 GLN 374 -0.0000

GLN 374 HIS 375 0.0004

HIS 375 GLY 376 -0.0017

GLY 376 TYR 377 -0.0002

TYR 377 SER 378 0.0000

SER 378 LEU 379 0.0032

LEU 379 ALA 380 -0.0002

ALA 380 ARG 381 0.0002

ARG 381 PHE 382 -0.0002

PHE 382 TYR 383 -0.0002

TYR 383 PHE 384 0.0001

PHE 384 GLN 385 -0.0026

GLN 385 CYS 386 0.0001

CYS 386 GLU 387 0.0001

GLU 387 GLY 388 -0.0008

GLY 388 HIS 389 -0.0001

HIS 389 GLU 390 -0.0000

GLU 390 PRO 391 -0.0017

PRO 391 THR 392 0.0001

THR 392 LEU 393 0.0002

LEU 393 LEU 394 -0.0046

LEU 394 LEU 395 0.0002

LEU 395 ILE 396 -0.0001

ILE 396 LYS 397 -0.0003

LYS 397 THR 398 0.0002

THR 398 THR 399 0.0000

THR 399 GLN 400 -0.0001

GLN 400 LYS 401 0.0002

LYS 401 GLU 402 0.0002

GLU 402 VAL 403 -0.0017

VAL 403 CYS 404 0.0004

CYS 404 GLY 405 -0.0001

GLY 405 ALA 406 0.0009

ALA 406 TYR 407 -0.0000

TYR 407 LEU 408 -0.0003

LEU 408 SER 409 0.0076

SER 409 THR 410 0.0003

THR 410 ASP 411 0.0002

ASP 411 TRP 412 0.0015

TRP 412 SER 413 0.0000

SER 413 GLU 414 0.0002

GLU 414 ARG 415 -0.0172

ARG 415 ASN 416 -0.0004

ASN 416 LYS 417 0.0001

LYS 417 PHE 418 0.0063

PHE 418 GLY 419 -0.0003

GLY 419 GLY 420 -0.0001

GLY 420 LYS 421 -0.0220

LYS 421 LEU 422 -0.0000

LEU 422 GLY 423 0.0001

GLY 423 PHE 424 -0.0122

PHE 424 PHE 425 0.0003

PHE 425 GLY 426 0.0001

GLY 426 THR 427 0.0191

THR 427 GLY 428 0.0001

GLY 428 GLU 429 0.0002

GLU 429 CYS 430 0.0151

CYS 430 PHE 431 0.0002

PHE 431 VAL 432 -0.0002

VAL 432 PHE 433 -0.0017

PHE 433 ARG 434 0.0002

ARG 434 LEU 435 0.0002

LEU 435 GLN 436 0.0016

GLN 436 PRO 437 0.0004

PRO 437 GLU 438 -0.0001

GLU 438 VAL 439 0.0086

VAL 439 GLN 440 -0.0001

GLN 440 ARG 441 0.0002

ARG 441 TYR 442 -0.0077

TYR 442 GLU 443 0.0001

GLU 443 TRP 444 -0.0001

TRP 444 VAL 445 -0.0081

VAL 445 VAL 446 0.0001

VAL 446 ILE 447 0.0001

ILE 447 LYS 448 -0.0270

LYS 448 HIS 449 0.0002

HIS 449 PRO 450 -0.0002

PRO 450 GLU 451 0.0676

GLU 451 LEU 452 -0.0000

LEU 452 THR 453 0.0002

THR 453 LYS 454 0.0938

LYS 454 PRO 455 0.0001

PRO 455 PRO 456 -0.0000

PRO 456 PRO 457 -0.0023

PRO 457 LEU 458 -0.0003

LEU 458 MET 459 -0.0004

MET 459 ALA 460 -0.0127

ALA 460 ALA 461 -0.0000

ALA 461 GLU 462 0.0001

GLU 462 PRO 463 0.1279

PRO 463 THR 464 0.0000

THR 464 ALA 465 -0.0000

ALA 465 PRO 466 0.0548

PRO 466 LEU 467 -0.0002

LEU 467 SER 468 0.0002

SER 468 HIS 469 -0.0994

HIS 469 SER 470 -0.0000

SER 470 ALA 471 -0.0002

ALA 471 SER 472 -0.2263

SER 472 SER 473 -0.0000

SER 473 ASP 474 0.0002

ASP 474 PRO 475 0.0330

PRO 475 ALA 476 -0.0002

ALA 476 ASP 477 -0.0002

ASP 477 ARG 478 0.0020

ARG 478 LEU 479 0.0003

LEU 479 SER 480 -0.0000

SER 480 PRO 481 0.0330

PRO 481 PHE 482 -0.0002

PHE 482 LEU 483 0.0004

LEU 483 ALA 484 -0.0153

ALA 484 ALA 485 0.0001

ALA 485 ARG 486 -0.0001

ARG 486 HIS 487 -0.0090

HIS 487 PHE 488 -0.0003

PHE 488 ASN 489 -0.0004

ASN 489 LEU 490 0.0148

LEU 490 PRO 491 0.0000

PRO 491 SER 492 -0.0003

SER 492 LYS 493 -0.0481

LYS 493 THR 494 -0.0000

THR 494 GLU 495 0.0001

GLU 495 SER 496 -0.0051

SER 496 MET 497 -0.0002

MET 497 PHE 498 0.0003

PHE 498 MET 499 -0.0031

MET 499 ALA 500 0.0000

ALA 500 GLY 501 -0.0001

GLY 501 GLY 502 0.0012

GLY 502 SER 503 0.0000

SER 503 ASP 504 0.0003

ASP 504 CYS 505 -0.0027

CYS 505 LEU 506 -0.0001

LEU 506 ILE 507 0.0001

ILE 507 VAL 508 0.0051

VAL 508 GLY 509 0.0000

GLY 509 GLY 510 -0.0001

GLY 510 GLY 511 -0.0093

GLY 511 GLY 512 0.0003

GLY 512 GLY 513 -0.0000

GLY 513 GLN 514 -0.0024

GLN 514 ALA 515 0.0000

ALA 515 LEU 516 -0.0002

LEU 516 TYR 517 0.0051

TYR 517 ILE 518 -0.0002

ILE 518 ASP 519 -0.0001

ASP 519 GLY 520 0.0001

GLY 520 ASP 521 0.0002

ASP 521 LEU 522 0.0000

LEU 522 ASN 523 -0.0011

ASN 523 ARG 524 0.0001

ARG 524 GLY 525 -0.0002

GLY 525 ARG 526 -0.0006

ARG 526 THR 527 0.0003

THR 527 SER 528 -0.0002

SER 528 HIS 529 0.0035

HIS 529 CYS 530 0.0004

CYS 530 ASP 531 -0.0003

ASP 531 THR 532 -0.0010

THR 532 PHE 533 -0.0002

PHE 533 ASN 534 -0.0001

ASN 534 ASN 535 0.0108

ASN 535 GLN 536 -0.0001

GLN 536 PRO 537 -0.0000

PRO 537 LEU 538 -0.0091

LEU 538 CYS 539 0.0001

CYS 539 SER 540 0.0001

SER 540 GLU 541 -0.0055

GLU 541 ASN 542 0.0003

ASN 542 PHE 543 -0.0001

PHE 543 LEU 544 -0.0001

LEU 544 ILE 545 -0.0002

ILE 545 ALA 546 0.0000

ALA 546 ALA 547 -0.0088

ALA 547 VAL 548 0.0001

VAL 548 GLU 549 0.0002

GLU 549 ALA 550 -0.0077

ALA 550 TRP 551 0.0000

TRP 551 GLY 552 -0.0001

GLY 552 PHE 553 -0.0274

PHE 553 GLN 554 0.0000

GLN 554 ASP 555 -0.0001

ASP 555 PRO 556 -0.0110

PRO 556 ASP 557 0.0004

ASP 557 THR 558 -0.0001

THR 558 GLN 559 -0.0029

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.

*** TBC_AF ***

CA strain for 2609111810563696908

--- normal mode 9 ---

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

* TBC_AF *