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 260711061254520762

--- 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
ARG 1 LEU 2 -0.0000

LEU 2 GLU 3 -0.0003

GLU 3 GLU 4 -0.0013

GLU 4 ALA 5 0.0004

ALA 5 GLN 6 -0.0000

GLN 6 GLN 7 -0.0016

GLN 7 ALA 8 -0.0000

ALA 8 LYS 9 0.0001

LYS 9 ASP 10 -0.0011

ASP 10 LYS 11 -0.0001

LYS 11 GLY 12 0.0003

GLY 12 ASN 13 -0.0003

ASN 13 LYS 14 0.0003

LYS 14 ALA 15 -0.0003

ALA 15 PHE 16 0.0022

PHE 16 LYS 17 0.0003

LYS 17 GLY 18 0.0001

GLY 18 GLY 19 -0.0003

GLY 19 LYS 20 -0.0000

LYS 20 TYR 21 0.0001

TYR 21 GLU 22 0.0007

GLU 22 GLU 23 0.0001

GLU 23 ALA 24 0.0000

ALA 24 ILE 25 -0.0035

ILE 25 GLU 26 0.0001

GLU 26 CYS 27 0.0001

CYS 27 TYR 28 0.0011

TYR 28 SER 29 0.0001

SER 29 LYS 30 -0.0002

LYS 30 ALA 31 -0.0002

ALA 31 ILE 32 0.0001

ILE 32 GLU 33 -0.0003

GLU 33 LEU 34 -0.0017

LEU 34 CYS 35 0.0002

CYS 35 PRO 36 -0.0001

PRO 36 GLU 37 -0.0030

GLU 37 GLU 38 0.0002

GLU 38 ASN 39 -0.0000

ASN 39 LYS 40 -0.0015

LYS 40 LYS 41 0.0002

LYS 41 ASN 42 0.0000

ASN 42 LEU 43 -0.0027

LEU 43 ALA 44 0.0002

ALA 44 VAL 45 0.0001

VAL 45 PHE 46 0.0019

PHE 46 TYR 47 0.0000

TYR 47 SER 48 0.0001

SER 48 ASN 49 -0.0002

ASN 49 ARG 50 -0.0003

ARG 50 ALA 51 -0.0002

ALA 51 ALA 52 -0.0018

ALA 52 CYS 53 0.0003

CYS 53 TYR 54 0.0001

TYR 54 ALA 55 0.0027

ALA 55 LYS 56 0.0001

LYS 56 LEU 57 0.0000

LEU 57 ASN 58 0.0038

ASN 58 GLU 59 -0.0002

GLU 59 TYR 60 0.0002

TYR 60 GLU 61 0.0033

GLU 61 LYS 62 0.0001

LYS 62 VAL 63 -0.0000

VAL 63 VAL 64 -0.0019

VAL 64 GLU 65 -0.0000

GLU 65 ASP 66 0.0001

ASP 66 CYS 67 -0.0000

CYS 67 THR 68 -0.0000

THR 68 LYS 69 0.0001

LYS 69 ALA 70 0.0021

ALA 70 LEU 71 0.0002

LEU 71 GLU 72 0.0001

GLU 72 LEU 73 0.0000

LEU 73 ASP 74 0.0001

ASP 74 PRO 75 0.0003

PRO 75 LYS 76 -0.0021

LYS 76 TYR 77 0.0001

TYR 77 VAL 78 -0.0002

VAL 78 LYS 79 0.0014

LYS 79 ALA 80 0.0004

ALA 80 LEU 81 0.0000

LEU 81 ASN 82 -0.0010

ASN 82 ARG 83 0.0004

ARG 83 ARG 84 0.0000

ARG 84 ALA 85 0.0059

ALA 85 THR 86 -0.0002

THR 86 ALA 87 -0.0001

ALA 87 TYR 88 -0.0008

TYR 88 GLU 89 0.0001

GLU 89 LYS 90 0.0001

LYS 90 LEU 91 0.0011

LEU 91 GLY 92 0.0001

GLY 92 GLU 93 0.0002

GLU 93 TYR 94 -0.0054

TYR 94 GLU 95 -0.0001

GLU 95 GLU 96 0.0003

GLU 96 ALA 97 0.0034

ALA 97 LEU 98 -0.0002

LEU 98 GLN 99 -0.0005

GLN 99 ASP 100 -0.0091

ASP 100 PHE 101 -0.0001

PHE 101 THR 102 0.0001

THR 102 ALA 103 0.0074

ALA 103 VAL 104 -0.0001

VAL 104 CYS 105 -0.0003

CYS 105 ILE 106 -0.0015

ILE 106 LEU 107 -0.0003

LEU 107 GLU 108 0.0001

GLU 108 GLY 109 0.0080

GLY 109 PHE 110 -0.0000

PHE 110 LYS 111 -0.0000

LYS 111 ASN 112 0.0046

ASN 112 GLN 113 -0.0001

GLN 113 GLN 114 -0.0001

GLN 114 ALA 115 -0.0066

ALA 115 MET 116 0.0002

MET 116 GLN 117 0.0003

GLN 117 ALA 118 -0.0057

ALA 118 ALA 119 -0.0002

ALA 119 GLU 120 -0.0003

GLU 120 ARG 121 -0.0006

ARG 121 VAL 122 -0.0002

VAL 122 LEU 123 0.0000

LEU 123 LYS 124 -0.0092

LYS 124 GLU 125 -0.0000

GLU 125 ILE 126 -0.0001

ILE 126 GLY 127 0.0033

GLY 127 LYS 128 0.0000

LYS 128 GLU 129 0.0001

GLU 129 LYS 130 -0.0066

LYS 130 ALA 131 0.0001

ALA 131 LYS 132 0.0000

LYS 132 GLU 133 0.0171

GLU 133 ILE 134 -0.0002

ILE 134 LEU 135 0.0003

LEU 135 LYS 136 0.0133

LYS 136 ASN 137 0.0000

ASN 137 ARG 138 0.0000

ARG 138 LYS 139 -0.0314

LYS 139 PRO 140 0.0001

PRO 140 ARG 141 0.0002

ARG 141 LEU 142 -0.0600

LEU 142 PRO 143 -0.0000

PRO 143 SER 144 0.0002

SER 144 PRO 145 -0.0003

PRO 145 THR 146 -0.0002

THR 146 PHE 147 -0.0006

PHE 147 ILE 148 0.0058

ILE 148 SER 149 0.0002

SER 149 SER 150 0.0002

SER 150 TYR 151 -0.0057

TYR 151 LEU 152 0.0001

LEU 152 ASP 153 -0.0004

ASP 153 SER 154 -0.0036

SER 154 PHE 155 0.0003

PHE 155 ARG 156 0.0001

ARG 156 SER 157 0.0054

SER 157 ASP 158 -0.0002

ASP 158 PRO 159 0.0001

PRO 159 LYS 160 -0.0015

LYS 160 HIS 161 0.0002

HIS 161 GLU 162 -0.0000

GLU 162 ALA 163 -0.0037

ALA 163 PRO 164 0.0000

PRO 164 THR 165 -0.0000

THR 165 GLU 166 0.0022

GLU 166 SER 167 0.0002

SER 167 GLU 168 -0.0001

GLU 168 GLU 169 0.0022

GLU 169 VAL 170 -0.0001

VAL 170 ASP 171 0.0003

ASP 171 GLU 172 0.0015

GLU 172 ASP 173 0.0003

ASP 173 LYS 174 0.0003

LYS 174 ASP 175 -0.0001

ASP 175 ASP 176 -0.0002

ASP 176 GLU 177 -0.0001

GLU 177 GLU 178 -0.0001

GLU 178 GLN 179 0.0004

GLN 179 GLY 180 -0.0000

GLY 180 ASP 181 0.0003

ASP 181 LEU 182 0.0001

LEU 182 TYR 183 0.0001

TYR 183 PHE 184 0.0015

PHE 184 LEU 185 0.0001

LEU 185 LYS 186 -0.0003

LYS 186 ALA 187 0.0001

ALA 187 LEU 188 0.0002

LEU 188 GLN 189 -0.0001

GLN 189 HIS 190 -0.0025

HIS 190 MET 191 -0.0000

MET 191 LYS 192 -0.0002

LYS 192 GLU 193 -0.0033

GLU 193 LYS 194 0.0004

LYS 194 LYS 195 -0.0002

LYS 195 TYR 196 -0.0002

TYR 196 GLU 197 0.0001

GLU 197 GLU 198 -0.0004

GLU 198 ALA 199 -0.0048

ALA 199 MET 200 -0.0003

MET 200 ASP 201 0.0001

ASP 201 ALA 202 -0.0026

ALA 202 PHE 203 0.0000

PHE 203 ASN 204 0.0001

ASN 204 LYS 205 -0.0025

LYS 205 ALA 206 -0.0003

ALA 206 ILE 207 -0.0000

ILE 207 ASP 208 -0.0002

ASP 208 GLU 209 -0.0002

GLU 209 ASP 210 0.0000

ASP 210 GLY 211 0.0007

GLY 211 PRO 212 0.0005

PRO 212 HIS 213 -0.0001

HIS 213 GLN 214 -0.0014

GLN 214 ALA 215 -0.0001

ALA 215 GLN 216 -0.0001

GLN 216 ALA 217 -0.0014

ALA 217 PHE 218 0.0001

PHE 218 ASN 219 0.0001

ASN 219 MET 220 -0.0023

MET 220 ARG 221 -0.0001

ARG 221 GLY 222 0.0001

GLY 222 THR 223 0.0003

THR 223 PHE 224 0.0001

PHE 224 TYR 225 -0.0003

TYR 225 PHE 226 -0.0001

PHE 226 LEU 227 -0.0000

LEU 227 MET 228 -0.0004

MET 228 GLY 229 0.0030

GLY 229 ASP 230 0.0000

ASP 230 VAL 231 0.0002

VAL 231 ASP 232 0.0020

ASP 232 GLU 233 -0.0000

GLU 233 ALA 234 -0.0002

ALA 234 LEU 235 0.0001

LEU 235 GLU 236 0.0002

GLU 236 ASP 237 -0.0002

ASP 237 PHE 238 -0.0009

PHE 238 ASP 239 -0.0002

ASP 239 ARG 240 0.0000

ARG 240 ALA 241 0.0004

ALA 241 LEU 242 0.0001

LEU 242 GLU 243 -0.0004

GLU 243 LEU 244 -0.0006

LEU 244 ASP 245 -0.0004

ASP 245 PRO 246 -0.0000

PRO 246 SER 247 0.0017

SER 247 GLY 248 -0.0001

GLY 248 VAL 249 0.0001

VAL 249 LYS 250 -0.0012

LYS 250 LEU 251 -0.0003

LEU 251 ASN 252 -0.0004

ASN 252 VAL 253 0.0003

VAL 253 ASN 254 -0.0002

ASN 254 ALA 255 -0.0000

ALA 255 LEU 256 -0.0018

LEU 256 ILE 257 0.0002

ILE 257 LYS 258 -0.0000

LYS 258 ARG 259 -0.0003

ARG 259 ALA 260 -0.0000

ALA 260 SER 261 0.0002

SER 261 ILE 262 0.0004

ILE 262 TYR 263 0.0000

TYR 263 MET 264 0.0004

MET 264 GLU 265 0.0209

GLU 265 GLN 266 -0.0002

GLN 266 GLY 267 0.0000

GLY 267 ASP 268 0.0014

ASP 268 VAL 269 0.0002

VAL 269 ASP 270 0.0001

ASP 270 GLU 271 -0.0012

GLU 271 ALA 272 0.0005

ALA 272 LEU 273 0.0001

LEU 273 GLU 274 -0.0019

GLU 274 ASP 275 0.0002

ASP 275 PHE 276 -0.0001

PHE 276 GLU 277 0.0007

GLU 277 LYS 278 -0.0001

LYS 278 ALA 279 -0.0001

ALA 279 ILE 280 0.0003

ILE 280 LYS 281 0.0000

LYS 281 LEU 282 0.0000

LEU 282 ASP 283 0.0013

ASP 283 PRO 284 -0.0002

PRO 284 ASP 285 -0.0000

ASP 285 ASN 286 -0.0017

ASN 286 PRO 287 -0.0001

PRO 287 ASP 288 0.0002

ASP 288 ILE 289 0.0003

ILE 289 TYR 290 -0.0000

TYR 290 TYR 291 -0.0000

TYR 291 HIS 292 0.0003

HIS 292 ARG 293 -0.0001

ARG 293 GLY 294 -0.0003

GLY 294 GLN 295 -0.0001

GLN 295 LEU 296 -0.0002

LEU 296 HIS 297 -0.0003

HIS 297 PHE 298 -0.0043

PHE 298 LEU 299 0.0000

LEU 299 GLN 300 -0.0001

GLN 300 GLY 301 -0.0062

GLY 301 ASP 302 0.0001

ASP 302 PHE 303 -0.0002

PHE 303 ASP 304 -0.0003

ASP 304 GLU 305 0.0002

GLU 305 ALA 306 -0.0002

ALA 306 ILE 307 0.0003

ILE 307 LYS 308 -0.0000

LYS 308 ASP 309 0.0001

ASP 309 PHE 310 -0.0016

PHE 310 GLN 311 0.0004

GLN 311 LYS 312 0.0001

LYS 312 CYS 313 -0.0001

CYS 313 ILE 314 0.0001

ILE 314 GLU 315 -0.0004

GLU 315 LEU 316 -0.0001

LEU 316 ASP 317 -0.0001

ASP 317 PRO 318 -0.0001

PRO 318 ASP 319 -0.0015

ASP 319 PHE 320 0.0000

PHE 320 VAL 321 -0.0000

VAL 321 LEU 322 -0.0017

LEU 322 ALA 323 0.0002

ALA 323 HIS 324 -0.0001

HIS 324 ILE 325 0.0009

ILE 325 GLN 326 0.0003

GLN 326 LEU 327 -0.0002

LEU 327 ALA 328 0.0023

ALA 328 MET 329 0.0002

MET 329 ALA 330 -0.0001

ALA 330 GLN 331 -0.0004

GLN 331 TYR 332 -0.0001

TYR 332 LYS 333 -0.0001

LYS 333 MET 334 -0.0007

MET 334 GLY 335 0.0002

GLY 335 SER 336 0.0003

SER 336 THR 337 -0.0008

THR 337 GLN 338 0.0001

GLN 338 GLN 339 0.0001

GLN 339 SER 340 -0.0033

SER 340 PRO 341 -0.0002

PRO 341 SER 342 -0.0001

SER 342 LEU 343 0.0007

LEU 343 ILE 344 -0.0003

ILE 344 GLN 345 -0.0002

GLN 345 GLU 346 0.0015

GLU 346 ALA 347 0.0001

ALA 347 MET 348 0.0000

MET 348 LYS 349 0.0047

LYS 349 THR 350 -0.0002

THR 350 PHE 351 -0.0001

PHE 351 GLU 352 -0.0012

GLU 352 LYS 353 -0.0001

LYS 353 ALA 354 0.0001

ALA 354 VAL 355 -0.0012

VAL 355 GLU 356 -0.0001

GLU 356 LYS 357 -0.0002

LYS 357 PHE 358 -0.0056

PHE 358 PRO 359 0.0001

PRO 359 ASP 360 0.0001

ASP 360 SER 361 0.0025

SER 361 PRO 362 0.0001

PRO 362 GLU 363 0.0002

GLU 363 VAL 364 -0.0041

VAL 364 TYR 365 -0.0001

TYR 365 ASN 366 -0.0002

ASN 366 TYR 367 -0.0002

TYR 367 TYR 368 0.0001

TYR 368 GLY 369 0.0000

GLY 369 GLU 370 0.0008

GLU 370 LEU 371 -0.0000

LEU 371 LEU 372 0.0004

LEU 372 MET 373 0.0087

MET 373 ASP 374 -0.0001

ASP 374 GLN 375 -0.0001

GLN 375 GLY 376 -0.0037

GLY 376 GLN 377 0.0001

GLN 377 PHE 378 -0.0002

PHE 378 ASP 379 0.0019

ASP 379 GLU 380 0.0001

GLU 380 ALA 381 -0.0002

ALA 381 MET 382 -0.0050

MET 382 GLU 383 0.0000

GLU 383 GLN 384 0.0003

GLN 384 PHE 385 -0.0010

PHE 385 ASP 386 -0.0001

ASP 386 LYS 387 -0.0004

LYS 387 ALA 388 -0.0013

ALA 388 ILE 389 -0.0002

ILE 389 GLU 390 -0.0002

GLU 390 LEU 391 0.0017

LEU 391 GLU 392 0.0001

GLU 392 PRO 393 0.0003

PRO 393 ASP 394 -0.0040

ASP 394 ASN 395 -0.0001

ASN 395 PRO 396 -0.0000

PRO 396 MET 397 -0.0000

MET 397 PRO 398 -0.0000

PRO 398 TYR 399 -0.0002

TYR 399 VAL 400 0.0124

VAL 400 ASN 401 -0.0002

ASN 401 LYS 402 0.0003

LYS 402 ALA 403 0.0086

ALA 403 MET 404 0.0005

MET 404 LEU 405 -0.0003

LEU 405 LEU 406 0.0005

LEU 406 LEU 407 -0.0003

LEU 407 GLN 408 -0.0001

GLN 408 VAL 409 0.0036

VAL 409 LYS 410 0.0000

LYS 410 GLN 411 0.0001

GLN 411 ASP 412 0.0059

ASP 412 ALA 413 0.0001

ALA 413 ASP 414 -0.0001

ASP 414 GLU 415 0.0001

GLU 415 ALA 416 0.0000

ALA 416 VAL 417 -0.0001

VAL 417 LYS 418 -0.0084

LYS 418 LEU 419 0.0002

LEU 419 LEU 420 -0.0003

LEU 420 LYS 421 0.0117

LYS 421 LYS 422 -0.0001

LYS 422 ALA 423 -0.0003

ALA 423 ILE 424 -0.0077

ILE 424 GLU 425 -0.0003

GLU 425 ILE 426 0.0004

ILE 426 ASP 427 0.0015

ASP 427 PRO 428 -0.0001

PRO 428 ARG 429 -0.0003

ARG 429 CYS 430 -0.0005

CYS 430 ASP 431 -0.0001

ASP 431 VAL 432 -0.0001

VAL 432 ALA 433 -0.0224

ALA 433 TYR 434 0.0002

TYR 434 VAL 435 0.0000

VAL 435 THR 436 0.0074

THR 436 LEU 437 -0.0002

LEU 437 ALA 438 0.0001

ALA 438 GLN 439 -0.0165

GLN 439 LEU 440 0.0001

LEU 440 TYR 441 -0.0001

TYR 441 LEU 442 0.0083

LEU 442 GLN 443 0.0001

GLN 443 GLN 444 -0.0001

GLN 444 GLY 445 0.0108

GLY 445 LYS 446 0.0001

LYS 446 VAL 447 -0.0003

VAL 447 ASP 448 0.0231

ASP 448 GLU 449 -0.0001

GLU 449 ALA 450 0.0001

ALA 450 ILE 451 0.0094

ILE 451 GLU 452 0.0002

GLU 452 LEU 453 0.0002

LEU 453 PHE 454 0.0052

PHE 454 ASP 455 0.0003

ASP 455 LYS 456 0.0002

LYS 456 ALA 457 0.0046

ALA 457 ILE 458 0.0005

ILE 458 ASP 459 0.0000

ASP 459 LEU 460 -0.0160

LEU 460 ALA 461 0.0001

ALA 461 ARG 462 0.0002

ARG 462 THR 463 0.0274

THR 463 GLU 464 -0.0001

GLU 464 ALA 465 -0.0001

ALA 465 GLU 466 -0.0106

GLU 466 LEU 467 0.0003

LEU 467 ALA 468 0.0001

ALA 468 ASN 469 -0.0119

ASN 469 ALA 470 0.0001

ALA 470 PHE 471 0.0001

PHE 471 SER 472 0.0181

SER 472 MET 473 -0.0002

MET 473 ARG 474 0.0001

ARG 474 GLU 475 -0.0095

GLU 475 ALA 476 -0.0001

ALA 476 ALA 477 0.0000

ALA 477 LYS 478 0.0214

LYS 478 ALA 479 -0.0001

ALA 479 GLN 480 -0.0000

GLN 480 LEU 481 0.0185

LEU 481 LYS 482 0.0000

LYS 482 VAL 483 0.0002

VAL 483 THR 484 0.0017

THR 484 LYS 485 0.0003

LYS 485 LYS 486 0.0002

LYS 486 LEU 487 -0.0011

LEU 487 GLY 488 0.0003

GLY 488 VAL 489 -0.0002

VAL 489 THR 490 0.0281

THR 490 LEU 491 0.0001

LEU 491 ALA 492 -0.0002

ALA 492 THR 493 0.0008

THR 493 MET 494 0.0001

MET 494 ALA 495 -0.0006

ALA 495 GLN 496 0.0046

GLN 496 MET 497 0.0005

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 260711061254520762

--- 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.

* *