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 260711055515516635

--- normal mode 8 ---

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
SER 1 LEU 2 -0.0001

LEU 2 ASP 3 0.0001

ASP 3 ARG 4 -0.0004

ARG 4 ALA 5 0.0002

ALA 5 GLN 6 -0.0000

GLN 6 ALA 7 0.0025

ALA 7 ALA 8 -0.0001

ALA 8 LYS 9 -0.0001

LYS 9 ASN 10 0.0019

ASN 10 LYS 11 0.0003

LYS 11 GLY 12 -0.0001

GLY 12 ASN 13 -0.0011

ASN 13 LYS 14 -0.0002

LYS 14 TYR 15 -0.0004

TYR 15 PHE 16 -0.0018

PHE 16 LYS 17 -0.0001

LYS 17 ALA 18 -0.0003

ALA 18 GLY 19 -0.0078

GLY 19 LYS 20 0.0001

LYS 20 TYR 21 -0.0004

TYR 21 GLU 22 0.0012

GLU 22 GLN 23 0.0001

GLN 23 ALA 24 -0.0003

ALA 24 ILE 25 -0.0033

ILE 25 GLN 26 -0.0001

GLN 26 CYS 27 0.0001

CYS 27 TYR 28 0.0037

TYR 28 THR 29 -0.0002

THR 29 GLU 30 -0.0002

GLU 30 ALA 31 0.0015

ALA 31 ILE 32 -0.0000

ILE 32 SER 33 -0.0001

SER 33 LEU 34 -0.0006

LEU 34 CYS 35 -0.0001

CYS 35 PRO 36 0.0000

PRO 36 THR 37 -0.0014

THR 37 GLU 38 -0.0003

GLU 38 LYS 39 -0.0001

LYS 39 ASN 40 0.0025

ASN 40 VAL 41 -0.0001

VAL 41 ASP 42 0.0000

ASP 42 LEU 43 -0.0027

LEU 43 SER 44 0.0001

SER 44 THR 45 0.0002

THR 45 PHE 46 0.0061

PHE 46 TYR 47 0.0001

TYR 47 GLN 48 -0.0003

GLN 48 ASN 49 0.0116

ASN 49 ARG 50 -0.0000

ARG 50 ALA 51 -0.0001

ALA 51 ALA 52 -0.0009

ALA 52 ALA 53 0.0003

ALA 53 PHE 54 0.0002

PHE 54 GLU 55 -0.0036

GLU 55 GLN 56 -0.0004

GLN 56 LEU 57 0.0002

LEU 57 GLN 58 -0.0219

GLN 58 LYS 59 -0.0002

LYS 59 TRP 60 -0.0000

TRP 60 LYS 61 0.0054

LYS 61 GLU 62 0.0001

GLU 62 VAL 63 0.0000

VAL 63 ALA 64 0.0004

ALA 64 GLN 65 0.0001

GLN 65 ASP 66 0.0002

ASP 66 CYS 67 0.0007

CYS 67 THR 68 -0.0000

THR 68 LYS 69 0.0002

LYS 69 ALA 70 0.0013

ALA 70 VAL 71 0.0001

VAL 71 GLU 72 -0.0001

GLU 72 LEU 73 0.0003

LEU 73 ASN 74 -0.0002

ASN 74 PRO 75 0.0002

PRO 75 LYS 76 -0.0064

LYS 76 TYR 77 0.0002

TYR 77 VAL 78 -0.0003

VAL 78 LYS 79 0.0127

LYS 79 ALA 80 -0.0003

ALA 80 LEU 81 -0.0003

LEU 81 PHE 82 -0.0071

PHE 82 ARG 83 -0.0002

ARG 83 ARG 84 -0.0002

ARG 84 ALA 85 -0.0117

ALA 85 LYS 86 0.0001

LYS 86 ALA 87 0.0000

ALA 87 HIS 88 -0.0065

HIS 88 GLU 89 -0.0001

GLU 89 LYS 90 -0.0003

LYS 90 LEU 91 0.0076

LEU 91 ASP 92 0.0002

ASP 92 ASN 93 0.0003

ASN 93 LYS 94 -0.0134

LYS 94 LYS 95 0.0001

LYS 95 GLU 96 0.0002

GLU 96 CYS 97 0.0144

CYS 97 LEU 98 0.0002

LEU 98 GLU 99 -0.0001

GLU 99 ASP 100 -0.0060

ASP 100 VAL 101 0.0001

VAL 101 THR 102 -0.0001

THR 102 ALA 103 -0.0017

ALA 103 VAL 104 0.0002

VAL 104 CYS 105 -0.0001

CYS 105 ILE 106 -0.0006

ILE 106 LEU 107 -0.0001

LEU 107 GLU 108 -0.0000

GLU 108 GLY 109 0.0208

GLY 109 PHE 110 -0.0001

PHE 110 GLN 111 0.0002

GLN 111 ASN 112 0.0138

ASN 112 GLN 113 -0.0001

GLN 113 GLN 114 0.0000

GLN 114 SER 115 -0.0006

SER 115 MET 116 -0.0001

MET 116 LEU 117 -0.0000

LEU 117 LEU 118 0.0066

LEU 118 ALA 119 -0.0001

ALA 119 ASP 120 -0.0000

ASP 120 LYS 121 0.0002

LYS 121 VAL 122 -0.0002

VAL 122 LEU 123 -0.0001

LEU 123 LYS 124 -0.0038

LYS 124 LEU 125 -0.0003

LEU 125 LEU 126 0.0002

LEU 126 GLY 127 -0.0309

GLY 127 LYS 128 -0.0003

LYS 128 GLU 129 0.0001

GLU 129 LYS 130 -0.0368

LYS 130 ALA 131 -0.0005

ALA 131 LYS 132 0.0002

LYS 132 GLU 133 0.0155

GLU 133 LYS 134 -0.0001

LYS 134 TYR 135 0.0001

TYR 135 LYS 136 0.0239

LYS 136 ASN 137 -0.0002

ASN 137 ARG 138 0.0001

ARG 138 GLU 139 -0.0070

GLU 139 PRO 140 -0.0001

PRO 140 LEU 141 0.0001

LEU 141 MET 142 -0.0155

MET 142 PRO 143 0.0003

PRO 143 SER 144 -0.0001

SER 144 PRO 145 0.0202

PRO 145 GLN 146 0.0004

GLN 146 PHE 147 0.0000

PHE 147 ILE 148 0.0140

ILE 148 LYS 149 -0.0003

LYS 149 SER 150 0.0001

SER 150 TYR 151 0.0015

TYR 151 PHE 152 0.0001

PHE 152 SER 153 0.0003

SER 153 SER 154 -0.0005

SER 154 PHE 155 0.0003

PHE 155 THR 156 -0.0000

THR 156 ASP 157 0.0078

ASP 157 ASP 158 -0.0003

ASP 158 ILE 159 0.0001

ILE 159 ILE 160 -0.0168

ILE 160 SER 161 0.0003

SER 161 GLN 162 -0.0000

GLN 162 PRO 163 0.0470

PRO 163 MET 164 -0.0002

MET 164 LEU 165 -0.0001

LEU 165 LYS 166 -0.0212

LYS 166 GLY 167 0.0003

GLY 167 GLU 168 -0.0000

GLU 168 LYS 169 0.0085

LYS 169 SER 170 -0.0000

SER 170 ASP 171 -0.0004

ASP 171 GLU 172 -0.0035

GLU 172 ASP 173 0.0001

ASP 173 LYS 174 -0.0002

LYS 174 ASP 175 -0.0117

ASP 175 LYS 176 -0.0002

LYS 176 GLU 177 -0.0001

GLU 177 GLY 178 0.0558

GLY 178 GLU 179 -0.0001

GLU 179 ALA 180 0.0000

ALA 180 LEU 181 0.0160

LEU 181 GLU 182 -0.0003

GLU 182 VAL 183 -0.0001

VAL 183 LYS 184 0.0280

LYS 184 GLU 185 0.0000

GLU 185 ASN 186 0.0004

ASN 186 SER 187 0.0094

SER 187 GLY 188 0.0001

GLY 188 TYR 189 -0.0001

TYR 189 LEU 190 0.0084

LEU 190 LYS 191 0.0000

LYS 191 ALA 192 0.0002

ALA 192 LYS 193 0.0033

LYS 193 GLN 194 0.0000

GLN 194 TYR 195 -0.0005

TYR 195 MET 196 0.0065

MET 196 GLU 197 -0.0001

GLU 197 GLU 198 -0.0002

GLU 198 GLU 199 0.0303

GLU 199 ASN 200 0.0001

ASN 200 TYR 201 0.0002

TYR 201 ASP 202 -0.0063

ASP 202 LYS 203 -0.0002

LYS 203 ILE 204 0.0001

ILE 204 ILE 205 0.0063

ILE 205 SER 206 -0.0002

SER 206 GLU 207 0.0001

GLU 207 CYS 208 0.0047

CYS 208 SER 209 0.0000

SER 209 LYS 210 -0.0001

LYS 210 GLU 211 0.0047

GLU 211 ILE 212 0.0004

ILE 212 ASP 213 -0.0001

ASP 213 ALA 214 0.0007

ALA 214 GLU 215 -0.0002

GLU 215 GLY 216 -0.0001

GLY 216 LYS 217 0.0063

LYS 217 TYR 218 -0.0002

TYR 218 MET 219 0.0005

MET 219 ALA 220 0.0019

ALA 220 GLU 221 -0.0001

GLU 221 ALA 222 -0.0000

ALA 222 LEU 223 -0.0069

LEU 223 LEU 224 -0.0001

LEU 224 LEU 225 0.0000

LEU 225 ARG 226 0.0008

ARG 226 ALA 227 0.0001

ALA 227 THR 228 -0.0004

THR 228 PHE 229 0.0009

PHE 229 TYR 230 0.0000

TYR 230 LEU 231 0.0000

LEU 231 LEU 232 0.0076

LEU 232 ILE 233 -0.0001

ILE 233 GLY 234 -0.0003

GLY 234 ASN 235 -0.0207

ASN 235 ALA 236 -0.0001

ALA 236 ASN 237 -0.0003

ASN 237 ALA 238 -0.0154

ALA 238 ALA 239 0.0002

ALA 239 LYS 240 -0.0002

LYS 240 PRO 241 -0.0091

PRO 241 ASP 242 0.0002

ASP 242 LEU 243 -0.0003

LEU 243 ASP 244 0.0084

ASP 244 LYS 245 0.0001

LYS 245 VAL 246 -0.0004

VAL 246 ILE 247 -0.0027

ILE 247 SER 248 -0.0001

SER 248 LEU 249 -0.0001

LEU 249 LYS 250 0.0024

LYS 250 GLU 251 -0.0003

GLU 251 ALA 252 -0.0002

ALA 252 ASN 253 0.0060

ASN 253 VAL 254 -0.0002

VAL 254 LYS 255 0.0001

LYS 255 LEU 256 0.0027

LEU 256 ARG 257 -0.0002

ARG 257 ALA 258 0.0001

ALA 258 ASN 259 0.0036

ASN 259 ALA 260 -0.0000

ALA 260 LEU 261 0.0002

LEU 261 ILE 262 0.0014

ILE 262 LYS 263 -0.0003

LYS 263 ARG 264 -0.0000

ARG 264 GLY 265 -0.0079

GLY 265 SER 266 0.0001

SER 266 MET 267 0.0002

MET 267 TYR 268 0.0078

TYR 268 MET 269 0.0001

MET 269 GLN 270 0.0002

GLN 270 GLN 271 0.0133

GLN 271 GLN 272 -0.0002

GLN 272 GLN 273 -0.0000

GLN 273 PRO 274 0.0067

PRO 274 LEU 275 0.0003

LEU 275 LEU 276 -0.0000

LEU 276 SER 277 0.0035

SER 277 THR 278 -0.0002

THR 278 GLN 279 0.0003

GLN 279 ASP 280 0.0006

ASP 280 PHE 281 -0.0004

PHE 281 ASN 282 0.0000

ASN 282 MET 283 -0.0016

MET 283 ALA 284 0.0000

ALA 284 ALA 285 0.0001

ALA 285 ASP 286 -0.0008

ASP 286 ILE 287 -0.0003

ILE 287 ASP 288 -0.0000

ASP 288 PRO 289 0.0015

PRO 289 GLN 290 -0.0002

GLN 290 ASN 291 0.0001

ASN 291 ALA 292 0.0048

ALA 292 ASP 293 0.0001

ASP 293 VAL 294 -0.0000

VAL 294 TYR 295 -0.0007

TYR 295 HIS 296 -0.0004

HIS 296 HIS 297 0.0003

HIS 297 ARG 298 0.0025

ARG 298 GLY 299 0.0001

GLY 299 GLN 300 0.0002

GLN 300 LEU 301 -0.0018

LEU 301 LYS 302 0.0001

LYS 302 ILE 303 -0.0000

ILE 303 LEU 304 0.0020

LEU 304 LEU 305 -0.0000

LEU 305 ASP 306 -0.0001

ASP 306 GLN 307 0.0040

GLN 307 VAL 308 0.0005

VAL 308 GLU 309 -0.0000

GLU 309 GLU 310 -0.0080

GLU 310 ALA 311 0.0002

ALA 311 VAL 312 -0.0003

VAL 312 ALA 313 -0.0100

ALA 313 ASP 314 -0.0004

ASP 314 PHE 315 0.0003

PHE 315 ASP 316 0.0008

ASP 316 GLU 317 -0.0001

GLU 317 CYS 318 -0.0000

CYS 318 ILE 319 -0.0000

ILE 319 ARG 320 0.0003

ARG 320 LEU 321 0.0002

LEU 321 ARG 322 0.0037

ARG 322 PRO 323 -0.0003

PRO 323 GLU 324 -0.0003

GLU 324 SER 325 -0.0034

SER 325 ALA 326 -0.0001

ALA 326 LEU 327 -0.0001

LEU 327 ALA 328 0.0046

ALA 328 GLN 329 -0.0002

GLN 329 ALA 330 -0.0000

ALA 330 GLN 331 -0.0033

GLN 331 LYS 332 -0.0001

LYS 332 CYS 333 0.0002

CYS 333 PHE 334 -0.0023

PHE 334 ALA 335 0.0001

ALA 335 LEU 336 0.0002

LEU 336 TYR 337 -0.0078

TYR 337 ARG 338 -0.0000

ARG 338 GLN 339 -0.0002

GLN 339 ALA 340 0.0031

ALA 340 TYR 341 0.0002

TYR 341 THR 342 0.0004

THR 342 GLY 343 -0.0016

GLY 343 ASN 344 -0.0002

ASN 344 ASN 345 -0.0002

ASN 345 SER 346 -0.0003

SER 346 SER 347 0.0002

SER 347 GLN 348 0.0002

GLN 348 ILE 349 -0.0013

ILE 349 GLN 350 0.0001

GLN 350 ALA 351 0.0000

ALA 351 ALA 352 -0.0007

ALA 352 MET 353 -0.0004

MET 353 LYS 354 -0.0000

LYS 354 GLY 355 -0.0024

GLY 355 PHE 356 0.0001

PHE 356 GLU 357 -0.0003

GLU 357 GLU 358 0.0031

GLU 358 VAL 359 -0.0000

VAL 359 ILE 360 -0.0000

ILE 360 LYS 361 0.0008

LYS 361 LYS 362 0.0003

LYS 362 PHE 363 0.0002

PHE 363 PRO 364 0.0099

PRO 364 ARG 365 0.0001

ARG 365 CYS 366 0.0003

CYS 366 ALA 367 -0.0000

ALA 367 GLU 368 -0.0001

GLU 368 GLY 369 -0.0003

GLY 369 TYR 370 0.0022

TYR 370 ALA 371 0.0003

ALA 371 LEU 372 -0.0003

LEU 372 TYR 373 0.0015

TYR 373 ALA 374 0.0000

ALA 374 GLN 375 0.0004

GLN 375 ALA 376 0.0087

ALA 376 LEU 377 -0.0003

LEU 377 THR 378 -0.0001

THR 378 ASP 379 -0.0052

ASP 379 GLN 380 0.0002

GLN 380 GLN 381 0.0000

GLN 381 GLN 382 -0.0078

GLN 382 PHE 383 -0.0002

PHE 383 GLY 384 -0.0002

GLY 384 LYS 385 0.0069

LYS 385 ALA 386 0.0003

ALA 386 ASP 387 0.0001

ASP 387 GLU 388 0.0056

GLU 388 MET 389 -0.0001

MET 389 TYR 390 0.0005

TYR 390 ASP 391 -0.0019

ASP 391 LYS 392 -0.0001

LYS 392 CYS 393 -0.0002

CYS 393 ILE 394 -0.0010

ILE 394 ASP 395 0.0001

ASP 395 LEU 396 -0.0003

LEU 396 GLU 397 -0.0073

GLU 397 PRO 398 0.0001

PRO 398 ASP 399 0.0002

ASP 399 ASN 400 -0.0011

ASN 400 ALA 401 0.0002

ALA 401 THR 402 -0.0000

THR 402 THR 403 0.0004

THR 403 TYR 404 0.0004

TYR 404 VAL 405 -0.0004

VAL 405 HIS 406 0.0011

HIS 406 LYS 407 0.0002

LYS 407 GLY 408 0.0002

GLY 408 LEU 409 0.0008

LEU 409 LEU 410 -0.0000

LEU 410 GLN 411 0.0002

GLN 411 LEU 412 -0.0002

LEU 412 GLN 413 0.0000

GLN 413 TRP 414 0.0003

TRP 414 LYS 415 -0.0102

LYS 415 GLN 416 -0.0001

GLN 416 ASP 417 -0.0000

ASP 417 LEU 418 -0.0028

LEU 418 ASP 419 -0.0004

ASP 419 ARG 420 -0.0000

ARG 420 GLY 421 0.0015

GLY 421 LEU 422 0.0001

LEU 422 GLU 423 -0.0000

GLU 423 LEU 424 0.0140

LEU 424 ILE 425 -0.0002

ILE 425 SER 426 -0.0002

SER 426 LYS 427 0.0254

LYS 427 ALA 428 0.0002

ALA 428 ILE 429 -0.0000

ILE 429 GLU 430 -0.0014

GLU 430 ILE 431 -0.0001

ILE 431 ASP 432 -0.0001

ASP 432 ASN 433 0.0026

ASN 433 LYS 434 -0.0001

LYS 434 CYS 435 0.0000

CYS 435 ASP 436 0.0104

ASP 436 PHE 437 0.0001

PHE 437 ALA 438 0.0000

ALA 438 TYR 439 -0.0037

TYR 439 GLU 440 0.0003

GLU 440 THR 441 -0.0001

THR 441 MET 442 -0.0088

MET 442 GLY 443 0.0003

GLY 443 THR 444 -0.0002

THR 444 ILE 445 -0.0062

ILE 445 GLU 446 -0.0001

GLU 446 VAL 447 -0.0001

VAL 447 GLN 448 0.0070

GLN 448 ARG 449 0.0000

ARG 449 GLY 450 -0.0003

GLY 450 ASN 451 0.0281

ASN 451 MET 452 0.0001

MET 452 GLU 453 -0.0002

GLU 453 LYS 454 0.0076

LYS 454 ALA 455 -0.0001

ALA 455 ILE 456 -0.0005

ILE 456 ASP 457 0.0162

ASP 457 MET 458 -0.0000

MET 458 PHE 459 0.0001

PHE 459 ASN 460 -0.0014

ASN 460 LYS 461 0.0001

LYS 461 ALA 462 0.0003

ALA 462 ILE 463 -0.0053

ILE 463 ASN 464 -0.0000

ASN 464 LEU 465 -0.0004

LEU 465 ALA 466 -0.0058

ALA 466 LYS 467 -0.0002

LYS 467 SER 468 0.0004

SER 468 GLU 469 -0.0397

GLU 469 MET 470 0.0001

MET 470 GLU 471 -0.0002

GLU 471 MET 472 -0.0175

MET 472 ALA 473 -0.0003

ALA 473 HIS 474 0.0001

HIS 474 LEU 475 -0.0089

LEU 475 TYR 476 0.0001

TYR 476 SER 477 -0.0001

SER 477 LEU 478 0.0080

LEU 478 CYS 479 0.0000

CYS 479 ASP 480 0.0004

ASP 480 ALA 481 0.0089

ALA 481 ALA 482 -0.0003

ALA 482 HIS 483 0.0003

HIS 483 ALA 484 0.0113

ALA 484 GLN 485 -0.0002

GLN 485 THR 486 0.0000

THR 486 GLU 487 -0.0027

GLU 487 VAL 488 0.0003

VAL 488 ALA 489 0.0002

ALA 489 LYS 490 -0.0098

LYS 490 LYS 491 0.0003

LYS 491 TYR 492 0.0004

TYR 492 GLY 493 0.0145

GLY 493 LEU 494 -0.0001

LEU 494 LYS 495 -0.0002

LYS 495 PRO 496 0.0129

PRO 496 PRO 497 -0.0003

PRO 497 THR 498 0.0000

THR 498 LEU 499 -0.0138

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 260711055515516635

--- normal mode 8 ---

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

* *