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 260710032716282038

--- normal mode 10 ---

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
PRO 1 LEU 2 -0.0004

LEU 2 ASP 3 0.0002

ASP 3 ARG 4 0.0039

ARG 4 ALA 5 -0.0002

ALA 5 GLN 6 -0.0001

GLN 6 ALA 7 0.0019

ALA 7 ALA 8 -0.0001

ALA 8 LYS 9 -0.0001

LYS 9 ASN 10 0.0001

ASN 10 LYS 11 -0.0000

LYS 11 GLY 12 0.0000

GLY 12 ASN 13 0.0003

ASN 13 LYS 14 -0.0001

LYS 14 TYR 15 -0.0001

TYR 15 PHE 16 -0.0006

PHE 16 LYS 17 -0.0002

LYS 17 ALA 18 0.0001

ALA 18 GLY 19 0.0015

GLY 19 LYS 20 -0.0001

LYS 20 TYR 21 -0.0001

TYR 21 GLU 22 -0.0019

GLU 22 GLN 23 -0.0000

GLN 23 ALA 24 0.0002

ALA 24 ILE 25 0.0043

ILE 25 GLN 26 -0.0001

GLN 26 CYS 27 0.0002

CYS 27 TYR 28 -0.0122

TYR 28 THR 29 -0.0001

THR 29 GLU 30 -0.0001

GLU 30 ALA 31 -0.0043

ALA 31 ILE 32 -0.0002

ILE 32 SER 33 -0.0002

SER 33 LEU 34 0.0157

LEU 34 CYS 35 -0.0002

CYS 35 PRO 36 0.0002

PRO 36 THR 37 -0.0074

THR 37 GLU 38 0.0004

GLU 38 LYS 39 -0.0001

LYS 39 LYS 40 -0.0037

LYS 40 VAL 41 0.0001

VAL 41 ASP 42 0.0002

ASP 42 LEU 43 0.0083

LEU 43 SER 44 0.0001

SER 44 THR 45 0.0000

THR 45 PHE 46 -0.0206

PHE 46 TYR 47 0.0002

TYR 47 GLN 48 0.0004

GLN 48 ASN 49 -0.0115

ASN 49 ARG 50 -0.0002

ARG 50 ALA 51 0.0001

ALA 51 ALA 52 0.0048

ALA 52 ALA 53 0.0001

ALA 53 PHE 54 -0.0001

PHE 54 GLU 55 0.0084

GLU 55 GLN 56 -0.0002

GLN 56 LEU 57 -0.0004

LEU 57 GLN 58 0.0355

GLN 58 LYS 59 -0.0001

LYS 59 TRP 60 0.0004

TRP 60 LYS 61 -0.0094

LYS 61 GLU 62 -0.0001

GLU 62 VAL 63 -0.0001

VAL 63 ALA 64 -0.0138

ALA 64 GLN 65 -0.0001

GLN 65 ASP 66 0.0000

ASP 66 CYS 67 -0.0071

CYS 67 THR 68 0.0004

THR 68 LYS 69 0.0000

LYS 69 ALA 70 -0.0084

ALA 70 VAL 71 -0.0004

VAL 71 GLU 72 0.0001

GLU 72 LEU 73 0.0154

LEU 73 ASN 74 -0.0004

ASN 74 PRO 75 -0.0001

PRO 75 ARG 76 -0.0071

ARG 76 TYR 77 -0.0001

TYR 77 VAL 78 0.0002

VAL 78 LYS 79 -0.0053

LYS 79 ALA 80 -0.0001

ALA 80 LEU 81 0.0001

LEU 81 PHE 82 0.0024

PHE 82 ARG 83 0.0001

ARG 83 ARG 84 -0.0003

ARG 84 ALA 85 0.0267

ALA 85 LYS 86 -0.0001

LYS 86 ALA 87 0.0002

ALA 87 HIS 88 0.0153

HIS 88 GLU 89 -0.0001

GLU 89 LYS 90 0.0003

LYS 90 LEU 91 -0.0148

LEU 91 ASP 92 -0.0004

ASP 92 ASN 93 0.0004

ASN 93 LYS 94 0.0497

LYS 94 LYS 95 -0.0003

LYS 95 GLU 96 -0.0002

GLU 96 CYS 97 -0.0135

CYS 97 LEU 98 0.0002

LEU 98 GLU 99 0.0002

GLU 99 ASP 100 0.0105

ASP 100 VAL 101 0.0003

VAL 101 THR 102 0.0000

THR 102 ALA 103 -0.0077

ALA 103 VAL 104 -0.0001

VAL 104 CYS 105 0.0002

CYS 105 ILE 106 -0.0030

ILE 106 LEU 107 -0.0003

LEU 107 GLU 108 -0.0000

GLU 108 GLY 109 -0.0302

GLY 109 PHE 110 0.0001

PHE 110 GLN 111 -0.0000

GLN 111 ASN 112 -0.0049

ASN 112 GLN 113 -0.0000

GLN 113 GLN 114 -0.0004

GLN 114 SER 115 0.0037

SER 115 MET 116 0.0002

MET 116 LEU 117 -0.0000

LEU 117 LEU 118 -0.0070

LEU 118 ALA 119 0.0000

ALA 119 ASP 120 -0.0001

ASP 120 LYS 121 -0.0078

LYS 121 VAL 122 -0.0005

VAL 122 LEU 123 0.0004

LEU 123 LYS 124 -0.0038

LYS 124 LEU 125 -0.0001

LEU 125 LEU 126 0.0001

LEU 126 GLY 127 0.0933

GLY 127 LYS 128 0.0003

LYS 128 GLU 129 0.0003

GLU 129 LYS 130 0.0311

LYS 130 ALA 131 -0.0005

ALA 131 LYS 132 -0.0001

LYS 132 GLU 133 -0.0263

GLU 133 LYS 134 0.0001

LYS 134 TYR 135 -0.0003

TYR 135 LYS 136 -0.0186

LYS 136 ASN 137 0.0004

ASN 137 ARG 138 0.0000

ARG 138 GLU 139 0.0075

GLU 139 PRO 140 -0.0002

PRO 140 LEU 141 -0.0004

LEU 141 MET 142 0.0753

MET 142 PRO 143 -0.0004

PRO 143 SER 144 0.0000

SER 144 PRO 145 0.0482

PRO 145 GLN 146 0.0001

GLN 146 PHE 147 -0.0001

PHE 147 ILE 148 0.0099

ILE 148 LYS 149 -0.0002

LYS 149 SER 150 0.0002

SER 150 TYR 151 -0.0078

TYR 151 PHE 152 -0.0002

PHE 152 SER 153 0.0003

SER 153 SER 154 -0.0083

SER 154 PHE 155 -0.0002

PHE 155 THR 156 -0.0001

THR 156 ASP 157 0.0078

ASP 157 ASP 158 -0.0000

ASP 158 ILE 159 0.0000

ILE 159 ILE 160 -0.0373

ILE 160 SER 161 0.0000

SER 161 GLN 162 0.0000

GLN 162 PRO 163 0.1045

PRO 163 MET 164 -0.0001

MET 164 LEU 165 -0.0001

LEU 165 LYS 166 -0.0914

LYS 166 GLY 167 -0.0001

GLY 167 GLU 168 0.0001

GLU 168 LYS 169 -0.0313

LYS 169 SER 170 0.0004

SER 170 ASP 171 -0.0001

ASP 171 GLU 172 0.0245

GLU 172 ASP 173 0.0001

ASP 173 LYS 174 -0.0001

LYS 174 ALA 175 0.0851

ALA 175 LEU 176 0.0001

LEU 176 GLU 177 -0.0002

GLU 177 VAL 178 0.0314

VAL 178 LYS 179 0.0000

LYS 179 GLU 180 -0.0001

GLU 180 ASN 181 0.1135

ASN 181 SER 182 0.0003

SER 182 GLY 183 -0.0001

GLY 183 TYR 184 -0.0410

TYR 184 LEU 185 -0.0001

LEU 185 LYS 186 0.0001

LYS 186 ALA 187 0.0719

ALA 187 LYS 188 0.0002

LYS 188 GLN 189 0.0003

GLN 189 TYR 190 0.0201

TYR 190 MET 191 0.0003

MET 191 GLU 192 0.0002

GLU 192 GLU 193 0.0211

GLU 193 GLU 194 -0.0002

GLU 194 ASN 195 0.0003

ASN 195 TYR 196 0.0032

TYR 196 ASP 197 -0.0003

ASP 197 LYS 198 0.0002

LYS 198 ILE 199 -0.0039

ILE 199 ILE 200 -0.0001

ILE 200 SER 201 -0.0002

SER 201 GLU 202 0.0053

GLU 202 CYS 203 0.0002

CYS 203 THR 204 -0.0001

THR 204 LYS 205 -0.0192

LYS 205 GLU 206 -0.0000

GLU 206 ILE 207 -0.0000

ILE 207 ASP 208 -0.0036

ASP 208 ALA 209 -0.0002

ALA 209 GLN 210 -0.0003

GLN 210 GLY 211 -0.0185

GLY 211 LYS 212 0.0001

LYS 212 TYR 213 0.0002

TYR 213 MET 214 -0.0997

MET 214 ALA 215 -0.0002

ALA 215 GLU 216 -0.0000

GLU 216 ALA 217 0.0035

ALA 217 LEU 218 0.0002

LEU 218 LEU 219 -0.0000

LEU 219 LEU 220 -0.0096

LEU 220 ARG 221 0.0004

ARG 221 ALA 222 0.0002

ALA 222 THR 223 -0.0079

THR 223 PHE 224 0.0001

PHE 224 TYR 225 0.0004

TYR 225 LEU 226 0.0080

LEU 226 LEU 227 -0.0002

LEU 227 ILE 228 -0.0002

ILE 228 GLY 229 0.0324

GLY 229 ASN 230 0.0002

ASN 230 ALA 231 -0.0000

ALA 231 ASN 232 0.0008

ASN 232 ALA 233 0.0002

ALA 233 ALA 234 -0.0003

ALA 234 LYS 235 0.0180

LYS 235 PRO 236 -0.0001

PRO 236 ASP 237 0.0000

ASP 237 LEU 238 0.0050

LEU 238 ASP 239 0.0003

ASP 239 GLN 240 -0.0004

GLN 240 VAL 241 0.0104

VAL 241 ILE 242 -0.0003

ILE 242 SER 243 -0.0001

SER 243 MET 244 -0.0110

MET 244 GLU 245 -0.0001

GLU 245 GLU 246 -0.0001

GLU 246 ALA 247 -0.0164

ALA 247 ASN 248 -0.0001

ASN 248 VAL 249 -0.0000

VAL 249 LYS 250 -0.0032

LYS 250 LEU 251 0.0001

LEU 251 ARG 252 0.0000

ARG 252 ALA 253 -0.0016

ALA 253 ASN 254 -0.0000

ASN 254 ALA 255 -0.0001

ALA 255 LEU 256 -0.0072

LEU 256 ILE 257 0.0001

ILE 257 LYS 258 -0.0001

LYS 258 ARG 259 0.0019

ARG 259 GLY 260 -0.0000

GLY 260 SER 261 -0.0003

SER 261 MET 262 0.0017

MET 262 TYR 263 0.0002

TYR 263 MET 264 0.0000

MET 264 GLN 265 0.0223

GLN 265 GLN 266 -0.0002

GLN 266 GLN 267 -0.0001

GLN 267 GLN 268 0.0188

GLN 268 PRO 269 -0.0004

PRO 269 LEU 270 0.0004

LEU 270 LEU 271 -0.0021

LEU 271 SER 272 -0.0001

SER 272 THR 273 -0.0001

THR 273 GLN 274 -0.0076

GLN 274 ASP 275 0.0000

ASP 275 PHE 276 -0.0002

PHE 276 ASN 277 0.0037

ASN 277 MET 278 0.0001

MET 278 ALA 279 0.0000

ALA 279 ALA 280 0.0013

ALA 280 ASP 281 0.0002

ASP 281 ILE 282 -0.0002

ILE 282 ASP 283 0.0066

ASP 283 PRO 284 -0.0000

PRO 284 GLN 285 -0.0001

GLN 285 ASN 286 -0.0107

ASN 286 ALA 287 -0.0001

ALA 287 ASP 288 0.0001

ASP 288 VAL 289 -0.0050

VAL 289 TYR 290 -0.0002

TYR 290 HIS 291 0.0000

HIS 291 HIS 292 0.0012

HIS 292 ARG 293 0.0001

ARG 293 GLY 294 -0.0001

GLY 294 GLN 295 -0.0023

GLN 295 LEU 296 0.0001

LEU 296 LYS 297 -0.0002

LYS 297 ILE 298 -0.0162

ILE 298 LEU 299 0.0000

LEU 299 LEU 300 0.0001

LEU 300 ASP 301 -0.0181

ASP 301 GLN 302 -0.0005

GLN 302 VAL 303 0.0003

VAL 303 GLU 304 0.0016

GLU 304 GLU 305 -0.0002

GLU 305 ALA 306 0.0000

ALA 306 VAL 307 0.0015

VAL 307 ALA 308 -0.0002

ALA 308 ASP 309 0.0005

ASP 309 PHE 310 -0.0011

PHE 310 ASP 311 -0.0001

ASP 311 GLU 312 0.0001

GLU 312 CYS 313 0.0025

CYS 313 ILE 314 -0.0002

ILE 314 ARG 315 0.0003

ARG 315 LEU 316 -0.0025

LEU 316 ARG 317 -0.0000

ARG 317 PRO 318 -0.0002

PRO 318 ASP 319 -0.0081

ASP 319 SER 320 0.0001

SER 320 ALA 321 0.0001

ALA 321 LEU 322 0.0009

LEU 322 ALA 323 -0.0001

ALA 323 GLN 324 -0.0003

GLN 324 ALA 325 0.0014

ALA 325 GLN 326 -0.0002

GLN 326 LYS 327 -0.0003

LYS 327 CYS 328 0.0038

CYS 328 PHE 329 0.0002

PHE 329 ALA 330 -0.0001

ALA 330 LEU 331 -0.0034

LEU 331 TYR 332 0.0001

TYR 332 ARG 333 0.0002

ARG 333 GLN 334 0.0024

GLN 334 ALA 335 0.0004

ALA 335 TYR 336 0.0004

TYR 336 THR 337 -0.0012

THR 337 GLY 338 0.0001

GLY 338 ASN 339 0.0001

ASN 339 ASN 340 -0.0026

ASN 340 SER 341 -0.0002

SER 341 THR 342 -0.0002

THR 342 GLN 343 -0.0002

GLN 343 VAL 344 0.0002

VAL 344 GLN 345 -0.0001

GLN 345 ALA 346 0.0039

ALA 346 ALA 347 0.0001

ALA 347 MET 348 -0.0003

MET 348 LYS 349 0.0024

LYS 349 GLY 350 -0.0000

GLY 350 PHE 351 -0.0003

PHE 351 GLU 352 -0.0045

GLU 352 ASP 353 0.0000

ASP 353 VAL 354 -0.0000

VAL 354 ILE 355 0.0002

ILE 355 LYS 356 0.0000

LYS 356 LYS 357 0.0004

LYS 357 PHE 358 -0.0053

PHE 358 PRO 359 -0.0003

PRO 359 ARG 360 0.0001

ARG 360 CYS 361 0.0118

CYS 361 ALA 362 0.0000

ALA 362 GLU 363 0.0003

GLU 363 GLY 364 0.0014

GLY 364 TYR 365 0.0003

TYR 365 ALA 366 0.0003

ALA 366 LEU 367 -0.0006

LEU 367 TYR 368 -0.0001

TYR 368 ALA 369 0.0000

ALA 369 GLN 370 0.0016

GLN 370 ALA 371 0.0000

ALA 371 LEU 372 -0.0000

LEU 372 THR 373 0.0067

THR 373 ASP 374 0.0001

ASP 374 GLN 375 0.0002

GLN 375 GLN 376 0.0054

GLN 376 GLN 377 -0.0000

GLN 377 PHE 378 0.0002

PHE 378 GLY 379 0.0010

GLY 379 LYS 380 -0.0001

LYS 380 ALA 381 0.0000

ALA 381 ASP 382 0.0034

ASP 382 GLU 383 0.0000

GLU 383 MET 384 0.0001

MET 384 TYR 385 0.0055

TYR 385 ASP 386 0.0002

ASP 386 LYS 387 0.0002

LYS 387 CYS 388 0.0023

CYS 388 ILE 389 -0.0002

ILE 389 ASP 390 -0.0001

ASP 390 LEU 391 -0.0031

LEU 391 GLU 392 0.0001

GLU 392 PRO 393 0.0000

PRO 393 ASP 394 0.0026

ASP 394 ASN 395 0.0001

ASN 395 ALA 396 -0.0003

ALA 396 THR 397 0.0038

THR 397 THR 398 0.0003

THR 398 TYR 399 0.0003

TYR 399 VAL 400 -0.0017

VAL 400 HIS 401 -0.0003

HIS 401 LYS 402 0.0002

LYS 402 GLY 403 -0.0104

GLY 403 LEU 404 -0.0000

LEU 404 LEU 405 -0.0000

LEU 405 GLN 406 0.0037

GLN 406 LEU 407 0.0002

LEU 407 GLN 408 0.0000

GLN 408 TRP 409 -0.0016

TRP 409 LYS 410 -0.0002

LYS 410 GLN 411 -0.0001

GLN 411 ASP 412 0.0151

ASP 412 LEU 413 0.0000

LEU 413 ASP 414 0.0004

ASP 414 LYS 415 -0.0209

LYS 415 GLY 416 0.0001

GLY 416 LEU 417 0.0001

LEU 417 GLU 418 -0.0192

GLU 418 LEU 419 -0.0000

LEU 419 ILE 420 -0.0003

ILE 420 SER 421 -0.0011

SER 421 LYS 422 0.0003

LYS 422 ALA 423 -0.0000

ALA 423 ILE 424 -0.0008

ILE 424 GLU 425 -0.0001

GLU 425 ILE 426 0.0003

ILE 426 ASP 427 0.0006

ASP 427 ASN 428 0.0000

ASN 428 LYS 429 -0.0001

LYS 429 CYS 430 0.0065

CYS 430 ASP 431 0.0003

ASP 431 PHE 432 0.0004

PHE 432 ALA 433 -0.0150

ALA 433 TYR 434 -0.0003

TYR 434 GLU 435 -0.0002

GLU 435 THR 436 -0.0010

THR 436 MET 437 0.0004

MET 437 GLY 438 -0.0000

GLY 438 THR 439 -0.0061

THR 439 ILE 440 -0.0001

ILE 440 GLU 441 0.0004

GLU 441 VAL 442 -0.0193

VAL 442 GLN 443 0.0002

GLN 443 ARG 444 0.0001

ARG 444 GLY 445 -0.0092

GLY 445 ASN 446 -0.0003

ASN 446 MET 447 -0.0001

MET 447 ASP 448 -0.0012

ASP 448 LYS 449 0.0002

LYS 449 ALA 450 -0.0001

ALA 450 ILE 451 0.0059

ILE 451 ASP 452 -0.0001

ASP 452 MET 453 -0.0003

MET 453 PHE 454 0.0015

PHE 454 ASN 455 -0.0002

ASN 455 LYS 456 0.0001

LYS 456 ALA 457 0.0009

ALA 457 ILE 458 -0.0000

ILE 458 ASN 459 -0.0002

ASN 459 LEU 460 0.0022

LEU 460 ALA 461 0.0002

ALA 461 LYS 462 0.0004

LYS 462 SER 463 0.0509

SER 463 GLU 464 0.0001

GLU 464 MET 465 0.0000

MET 465 GLU 466 -0.0073

GLU 466 MET 467 0.0000

MET 467 ALA 468 0.0001

ALA 468 HIS 469 -0.0011

HIS 469 LEU 470 0.0003

LEU 470 TYR 471 -0.0003

TYR 471 SER 472 0.0032

SER 472 LEU 473 -0.0004

LEU 473 CYS 474 -0.0003

CYS 474 ASP 475 0.0095

ASP 475 ALA 476 0.0001

ALA 476 ALA 477 -0.0001

ALA 477 TYR 478 -0.0041

TYR 478 ALA 479 -0.0004

ALA 479 GLN 480 0.0000

GLN 480 THR 481 0.0055

THR 481 GLU 482 0.0004

GLU 482 VAL 483 0.0001

VAL 483 ALA 484 0.0098

ALA 484 LYS 485 0.0001

LYS 485 LYS 486 -0.0003

LYS 486 TYR 487 0.0116

TYR 487 GLY 488 -0.0001

GLY 488 LEU 489 0.0001

LEU 489 LYS 490 -0.1167

LYS 490 PRO 491 0.0003

PRO 491 PRO 492 -0.0001

PRO 492 THR 493 -0.1020

THR 493 LEU 494 -0.0001

LEU 494 ASN 495 0.0002

ASN 495 VAL 496 -0.0003

VAL 496 MET 497 0.0000

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 260710032716282038

--- normal mode 10 ---

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

* *