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

* *

CA strain for 260611045752630730

--- normal mode 7 ---

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 ASN 2 -0.0009

ASN 2 HIS 3 0.0002

HIS 3 LYS 4 -0.0047

LYS 4 VAL 5 -0.0000

VAL 5 HIS 6 0.0004

HIS 6 HIS 7 0.0000

HIS 7 HIS 8 -0.0000

HIS 8 HIS 9 0.0002

HIS 9 HIS 10 -0.0016

HIS 10 HIS 11 0.0001

HIS 11 ILE 12 -0.0000

ILE 12 GLU 13 -0.0353

GLU 13 GLY 14 -0.0002

GLY 14 ARG 15 0.0000

ARG 15 HIS 16 0.0418

HIS 16 MET 17 -0.0000

MET 17 GLN 18 0.0000

GLN 18 ALA 19 0.0020

ALA 19 LYS 20 0.0000

LYS 20 LEU 21 0.0002

LEU 21 THR 22 -0.0005

THR 22 LYS 23 0.0004

LYS 23 LYS 24 -0.0000

LYS 24 GLU 25 -0.0003

GLU 25 PHE 26 -0.0001

PHE 26 ILE 27 0.0002

ILE 27 GLU 28 -0.0002

GLU 28 TRP 29 -0.0001

TRP 29 LEU 30 -0.0001

LEU 30 LYS 31 0.0001

LYS 31 THR 32 0.0003

THR 32 SER 33 0.0003

SER 33 GLU 34 -0.0000

GLU 34 GLY 35 -0.0002

GLY 35 LYS 36 0.0002

LYS 36 GLN 37 0.0000

GLN 37 PHE 38 -0.0002

PHE 38 ASN 39 -0.0001

ASN 39 VAL 40 0.0003

VAL 40 ASP 41 -0.0002

ASP 41 LEU 42 -0.0003

LEU 42 TRP 43 0.0001

TRP 43 TYR 44 -0.0003

TYR 44 GLY 45 -0.0003

GLY 45 PHE 46 0.0002

PHE 46 GLN 47 0.0002

GLN 47 CYS 48 0.0000

CYS 48 PHE 49 -0.0004

PHE 49 ASP 50 0.0002

ASP 50 TYR 51 -0.0001

TYR 51 ALA 52 -0.0000

ALA 52 ASN 53 0.0002

ASN 53 ALA 54 -0.0001

ALA 54 GLY 55 -0.0003

GLY 55 TRP 56 -0.0000

TRP 56 LYS 57 -0.0000

LYS 57 VAL 58 -0.0013

VAL 58 LEU 59 0.0001

LEU 59 PHE 60 0.0001

PHE 60 GLY 61 -0.0007

GLY 61 LEU 62 -0.0003

LEU 62 LEU 63 0.0004

LEU 63 LEU 64 -0.0006

LEU 64 LYS 65 0.0001

LYS 65 GLY 66 0.0002

GLY 66 LEU 67 -0.0005

LEU 67 GLY 68 -0.0002

GLY 68 ALA 69 0.0004

ALA 69 LYS 70 0.0005

LYS 70 ASP 71 -0.0001

ASP 71 ILE 72 0.0000

ILE 72 PRO 73 -0.0000

PRO 73 PHE 74 -0.0000

PHE 74 ALA 75 -0.0002

ALA 75 ASN 76 -0.0002

ASN 76 ASN 77 -0.0000

ASN 77 PHE 78 -0.0001

PHE 78 ASP 79 -0.0046

ASP 79 GLY 80 0.0000

GLY 80 LEU 81 -0.0001

LEU 81 ALA 82 -0.0019

ALA 82 THR 83 0.0001

THR 83 VAL 84 0.0003

VAL 84 TYR 85 -0.0017

TYR 85 GLN 86 -0.0003

GLN 86 ASN 87 0.0000

ASN 87 THR 88 -0.0006

THR 88 PRO 89 -0.0001

PRO 89 ASP 90 -0.0000

ASP 90 PHE 91 -0.0016

PHE 91 LEU 92 0.0001

LEU 92 ALA 93 -0.0003

ALA 93 GLN 94 0.0004

GLN 94 PRO 95 0.0001

PRO 95 GLY 96 0.0000

GLY 96 ASP 97 -0.0003

ASP 97 MET 98 0.0001

MET 98 VAL 99 -0.0005

VAL 99 VAL 100 0.0007

VAL 100 PHE 101 -0.0002

PHE 101 GLY 102 0.0002

GLY 102 SER 103 0.0001

SER 103 ASN 104 0.0001

ASN 104 TYR 105 -0.0004

TYR 105 GLY 106 0.0004

GLY 106 ALA 107 -0.0003

ALA 107 GLY 108 0.0002

GLY 108 TYR 109 0.0003

TYR 109 GLY 110 -0.0001

GLY 110 HIS 111 -0.0001

HIS 111 VAL 112 0.0002

VAL 112 ALA 113 0.0001

ALA 113 TRP 114 0.0001

TRP 114 VAL 115 0.0005

VAL 115 ILE 116 -0.0002

ILE 116 GLU 117 -0.0002

GLU 117 ALA 118 -0.0019

ALA 118 THR 119 -0.0003

THR 119 LEU 120 -0.0003

LEU 120 ASP 121 -0.0012

ASP 121 TYR 122 0.0004

TYR 122 ILE 123 0.0000

ILE 123 ILE 124 -0.0017

ILE 124 VAL 125 0.0000

VAL 125 TYR 126 -0.0004

TYR 126 GLU 127 0.0003

GLU 127 GLN 128 0.0001

GLN 128 ASN 129 -0.0004

ASN 129 TRP 130 -0.0001

TRP 130 LEU 131 0.0003

LEU 131 GLY 132 -0.0001

GLY 132 GLY 133 -0.0000

GLY 133 GLY 134 0.0002

GLY 134 TRP 135 -0.0004

TRP 135 THR 136 -0.0001

THR 136 ASP 137 -0.0003

ASP 137 ARG 138 -0.0004

ARG 138 ILE 139 0.0001

ILE 139 GLU 140 -0.0002

GLU 140 GLN 141 -0.0001

GLN 141 PRO 142 0.0001

PRO 142 GLY 143 0.0003

GLY 143 TRP 144 -0.0001

TRP 144 GLY 145 -0.0000

GLY 145 TRP 146 -0.0004

TRP 146 GLU 147 0.0002

GLU 147 LYS 148 0.0002

LYS 148 VAL 149 0.0002

VAL 149 THR 150 0.0003

THR 150 ARG 151 0.0003

ARG 151 ARG 152 0.0001

ARG 152 GLN 153 -0.0001

GLN 153 HIS 154 0.0001

HIS 154 ALA 155 -0.0000

ALA 155 TYR 156 -0.0001

TYR 156 ASP 157 -0.0000

ASP 157 PHE 158 -0.0003

PHE 158 PRO 159 -0.0000

PRO 159 MET 160 0.0000

MET 160 TRP 161 0.0002

TRP 161 PHE 162 0.0000

PHE 162 ILE 163 -0.0011

ILE 163 ARG 164 0.0004

ARG 164 PRO 165 0.0003

PRO 165 ASN 166 0.0011

ASN 166 PHE 167 0.0002

PHE 167 LYS 168 0.0000

LYS 168 SER 169 -0.0001

SER 169 GLU 170 0.0000

GLU 170 THR 171 0.0000

THR 171 ALA 172 0.0018

ALA 172 PRO 173 0.0004

PRO 173 ARG 174 0.0000

ARG 174 SER 175 -0.0001

SER 175 ILE 176 -0.0004

ILE 176 GLN 177 0.0000

GLN 177 SER 178 0.0003

SER 178 PRO 179 0.0001

PRO 179 THR 180 0.0003

THR 180 GLN 181 0.0011

GLN 181 ALA 182 0.0001

ALA 182 SER 183 0.0000

SER 183 LYS 184 0.0006

LYS 184 LYS 185 0.0003

LYS 185 GLU 186 -0.0002

GLU 186 THR 187 0.0005

THR 187 ALA 188 0.0000

ALA 188 LYS 189 -0.0000

LYS 189 PRO 190 0.0015

PRO 190 GLN 191 -0.0001

GLN 191 PRO 192 0.0001

PRO 192 LYS 193 0.0008

LYS 193 ALA 194 0.0000

ALA 194 VAL 195 -0.0002

VAL 195 GLU 196 0.0005

GLU 196 LEU 197 -0.0001

LEU 197 LYS 198 -0.0001

LYS 198 ILE 199 0.0005

ILE 199 ILE 200 -0.0001

ILE 200 LYS 201 0.0000

LYS 201 ASP 202 0.0004

ASP 202 VAL 203 -0.0005

VAL 203 VAL 204 0.0004

VAL 204 LYS 205 0.0000

LYS 205 GLY 206 0.0000

GLY 206 TYR 207 -0.0000

TYR 207 ASP 208 -0.0001

ASP 208 LEU 209 -0.0001

LEU 209 PRO 210 0.0000

PRO 210 LYS 211 0.0000

LYS 211 ARG 212 -0.0001

ARG 212 GLY 213 -0.0001

GLY 213 GLY 214 -0.0004

GLY 214 ASN 215 0.0004

ASN 215 PRO 216 -0.0003

PRO 216 LYS 217 -0.0001

LYS 217 GLY 218 -0.0000

GLY 218 ILE 219 -0.0000

ILE 219 VAL 220 -0.0005

VAL 220 ILE 221 0.0005

ILE 221 HIS 222 -0.0004

HIS 222 ASN 223 -0.0001

ASN 223 ASP 224 0.0002

ASP 224 ALA 225 -0.0002

ALA 225 GLY 226 0.0002

GLY 226 SER 227 -0.0002

SER 227 LYS 228 0.0004

LYS 228 GLY 229 0.0001

GLY 229 ALA 230 0.0003

ALA 230 THR 231 0.0000

THR 231 ALA 232 0.0003

ALA 232 GLU 233 0.0003

GLU 233 ALA 234 -0.0003

ALA 234 TYR 235 -0.0001

TYR 235 ARG 236 0.0000

ARG 236 ASN 237 -0.0001

ASN 237 GLY 238 -0.0002

GLY 238 LEU 239 0.0000

LEU 239 VAL 240 0.0002

VAL 240 ASN 241 0.0003

ASN 241 ALA 242 -0.0003

ALA 242 PRO 243 0.0003

PRO 243 LEU 244 0.0000

LEU 244 SER 245 -0.0001

SER 245 ARG 246 -0.0002

ARG 246 LEU 247 -0.0001

LEU 247 GLU 248 -0.0001

GLU 248 ALA 249 0.0001

ALA 249 GLY 250 0.0002

GLY 250 ILE 251 0.0001

ILE 251 ALA 252 0.0000

ALA 252 HIS 253 0.0001

HIS 253 SER 254 -0.0001

SER 254 TYR 255 0.0002

TYR 255 VAL 256 0.0000

VAL 256 SER 257 -0.0003

SER 257 GLY 258 -0.0001

GLY 258 ASN 259 0.0001

ASN 259 THR 260 -0.0003

THR 260 VAL 261 0.0005

VAL 261 TRP 262 0.0003

TRP 262 GLN 263 -0.0000

GLN 263 ALA 264 -0.0001

ALA 264 LEU 265 0.0003

LEU 265 ASP 266 -0.0002

ASP 266 GLU 267 0.0000

GLU 267 SER 268 -0.0003

SER 268 GLN 269 -0.0002

GLN 269 VAL 270 0.0001

VAL 270 GLY 271 -0.0002

GLY 271 TRP 272 -0.0000

TRP 272 HIS 273 -0.0001

HIS 273 THR 274 -0.0001

THR 274 ALA 275 0.0003

ALA 275 ASN 276 0.0001

ASN 276 GLN 277 0.0001

GLN 277 LEU 278 0.0002

LEU 278 GLY 279 -0.0001

GLY 279 ASN 280 -0.0001

ASN 280 LYS 281 -0.0001

LYS 281 TYR 282 0.0001

TYR 282 TYR 283 -0.0002

TYR 283 TYR 284 0.0001

TYR 284 GLY 285 0.0001

GLY 285 ILE 286 0.0000

ILE 286 GLU 287 0.0002

GLU 287 VAL 288 -0.0002

VAL 288 CYS 289 -0.0002

CYS 289 GLN 290 0.0005

GLN 290 SER 291 0.0002

SER 291 MET 292 0.0003

MET 292 GLY 293 -0.0000

GLY 293 ALA 294 -0.0003

ALA 294 ASP 295 -0.0007

ASP 295 ASN 296 0.0001

ASN 296 ALA 297 0.0004

ALA 297 THR 298 -0.0003

THR 298 PHE 299 0.0005

PHE 299 LEU 300 -0.0001

LEU 300 LYS 301 -0.0001

LYS 301 ASN 302 0.0001

ASN 302 GLU 303 0.0002

GLU 303 GLN 304 0.0000

GLN 304 ALA 305 -0.0002

ALA 305 THR 306 -0.0001

THR 306 PHE 307 -0.0003

PHE 307 GLN 308 0.0000

GLN 308 GLU 309 -0.0000

GLU 309 CYS 310 -0.0001

CYS 310 ALA 311 -0.0001

ALA 311 ARG 312 0.0001

ARG 312 LEU 313 0.0005

LEU 313 LEU 314 0.0000

LEU 314 LYS 315 -0.0002

LYS 315 LYS 316 0.0002

LYS 316 TRP 317 -0.0001

TRP 317 GLY 318 -0.0001

GLY 318 LEU 319 0.0002

LEU 319 PRO 320 -0.0001

PRO 320 ALA 321 0.0001

ALA 321 ASN 322 0.0002

ASN 322 ARG 323 -0.0005

ARG 323 ASN 324 -0.0001

ASN 324 THR 325 0.0015

THR 325 ILE 326 -0.0001

ILE 326 ARG 327 -0.0002

ARG 327 LEU 328 -0.0008

LEU 328 HIS 329 0.0003

HIS 329 ASN 330 -0.0003

ASN 330 GLU 331 -0.0008

GLU 331 PHE 332 -0.0000

PHE 332 THR 333 0.0001

THR 333 SER 334 -0.0003

SER 334 THR 335 -0.0004

THR 335 SER 336 -0.0000

SER 336 CYS 337 0.0001

CYS 337 PRO 338 0.0001

PRO 338 HIS 339 0.0002

HIS 339 ARG 340 -0.0004

ARG 340 SER 341 0.0001

SER 341 SER 342 -0.0002

SER 342 VAL 343 -0.0007

VAL 343 LEU 344 -0.0005

LEU 344 HIS 345 0.0001

HIS 345 THR 346 0.0000

THR 346 GLY 347 -0.0002

GLY 347 PHE 348 0.0000

PHE 348 ASP 349 -0.0002

ASP 349 PRO 350 0.0003

PRO 350 VAL 351 0.0004

VAL 351 THR 352 -0.0004

THR 352 ARG 353 -0.0001

ARG 353 GLY 354 -0.0000

GLY 354 LEU 355 -0.0001

LEU 355 LEU 356 0.0001

LEU 356 PRO 357 -0.0001

PRO 357 GLU 358 0.0002

GLU 358 ASP 359 0.0003

ASP 359 LYS 360 -0.0001

LYS 360 GLN 361 -0.0001

GLN 361 LEU 362 0.0004

LEU 362 GLN 363 0.0000

GLN 363 LEU 364 -0.0005

LEU 364 LYS 365 0.0003

LYS 365 ASP 366 -0.0002

ASP 366 TYR 367 -0.0008

TYR 367 PHE 368 -0.0000

PHE 368 ILE 369 -0.0003

ILE 369 LYS 370 0.0002

LYS 370 GLN 371 0.0000

GLN 371 ILE 372 0.0001

ILE 372 ARG 373 -0.0000

ARG 373 VAL 374 -0.0002

VAL 374 TYR 375 -0.0001

TYR 375 MET 376 0.0002

MET 376 ASP 377 0.0002

ASP 377 GLY 378 0.0003

GLY 378 LYS 379 0.0001

LYS 379 ILE 380 -0.0001

ILE 380 PRO 381 0.0003

PRO 381 VAL 382 0.0015

VAL 382 ALA 383 -0.0000

ALA 383 THR 384 0.0002

THR 384 VAL 385 0.0006

VAL 385 SER 386 -0.0005

SER 386 ASN 387 0.0001

ASN 387 GLU 388 -0.0003

GLU 388 SER 389 0.0005

SER 389 SER 390 -0.0002

SER 390 ALA 391 0.0006

ALA 391 SER 392 0.0000

SER 392 SER 393 0.0001

SER 393 ASN 394 -0.0006

ASN 394 THR 395 0.0005

THR 395 VAL 396 -0.0001

VAL 396 LYS 397 0.0003

LYS 397 PRO 398 0.0000

PRO 398 VAL 399 0.0001

VAL 399 ALA 400 -0.0004

ALA 400 SER 401 -0.0001

SER 401 ALA 402 0.0002

ALA 402 TRP 403 -0.0004

TRP 403 LYS 404 -0.0001

LYS 404 ARG 405 -0.0002

ARG 405 ASN 406 0.0001

ASN 406 LYS 407 0.0002

LYS 407 TYR 408 0.0001

TYR 408 GLY 409 -0.0002

GLY 409 THR 410 0.0001

THR 410 TYR 411 -0.0001

TYR 411 TYR 412 -0.0003

TYR 412 MET 413 0.0000

MET 413 GLU 414 0.0001

GLU 414 GLU 415 -0.0003

GLU 415 ASN 416 0.0002

ASN 416 ALA 417 0.0001

ALA 417 ARG 418 0.0001

ARG 418 PHE 419 0.0002

PHE 419 THR 420 -0.0002

THR 420 ASN 421 0.0000

ASN 421 GLY 422 -0.0000

GLY 422 ASN 423 -0.0001

ASN 423 GLN 424 -0.0003

GLN 424 PRO 425 0.0002

PRO 425 ILE 426 -0.0004

ILE 426 THR 427 0.0003

THR 427 VAL 428 -0.0002

VAL 428 ARG 429 -0.0001

ARG 429 LYS 430 0.0002

LYS 430 ILE 431 -0.0005

ILE 431 GLY 432 -0.0001

GLY 432 PRO 433 -0.0001

PRO 433 PHE 434 0.0004

PHE 434 LEU 435 -0.0000

LEU 435 SER 436 -0.0001

SER 436 CYS 437 -0.0001

CYS 437 PRO 438 -0.0001

PRO 438 VAL 439 0.0000

VAL 439 ALA 440 0.0003

ALA 440 TYR 441 -0.0001

TYR 441 GLN 442 0.0002

GLN 442 PHE 443 -0.0000

PHE 443 GLN 444 0.0002

GLN 444 PRO 445 -0.0000

PRO 445 GLY 446 -0.0002

GLY 446 GLY 447 -0.0001

GLY 447 TYR 448 0.0002

TYR 448 CYS 449 0.0002

CYS 449 ASP 450 -0.0002

ASP 450 TYR 451 0.0004

TYR 451 THR 452 -0.0003

THR 452 GLU 453 0.0003

GLU 453 VAL 454 -0.0001

VAL 454 MET 455 -0.0002

MET 455 LEU 456 -0.0001

LEU 456 GLN 457 0.0000

GLN 457 ASP 458 0.0001

ASP 458 GLY 459 0.0003

GLY 459 HIS 460 0.0003

HIS 460 VAL 461 -0.0001

VAL 461 TRP 462 0.0002

TRP 462 VAL 463 0.0000

VAL 463 GLY 464 0.0000

GLY 464 TYR 465 -0.0002

TYR 465 THR 466 0.0001

THR 466 TRP 467 -0.0001

TRP 467 GLU 468 0.0001

GLU 468 GLY 469 0.0001

GLY 469 GLN 470 0.0001

GLN 470 ARG 471 0.0002

ARG 471 TYR 472 -0.0004

TYR 472 TYR 473 0.0003

TYR 473 LEU 474 -0.0001

LEU 474 PRO 475 -0.0001

PRO 475 ILE 476 -0.0002

ILE 476 ARG 477 -0.0000

ARG 477 THR 478 -0.0001

THR 478 TRP 479 -0.0001

TRP 479 ASN 480 -0.0001

ASN 480 GLY 481 0.0001

GLY 481 SER 482 -0.0001

SER 482 ALA 483 -0.0003

ALA 483 PRO 484 0.0002

PRO 484 PRO 485 0.0005

PRO 485 ASN 486 0.0001

ASN 486 GLN 487 0.0001

GLN 487 ILE 488 0.0000

ILE 488 LEU 489 -0.0002

LEU 489 GLY 490 0.0004

GLY 490 ASP 491 -0.0003

ASP 491 LEU 492 0.0001

LEU 492 TRP 493 0.0001

TRP 493 GLY 494 0.0003

GLY 494 GLU 495 0.0000

GLU 495 ILE 496 -0.0002

ILE 496 SER 497 0.0003

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.

*** ***

CA strain for 260611045752630730

--- normal mode 7 ---

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

* *