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 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
ARG 1 LEU 2 -0.0002

LEU 2 GLU 3 -0.0002

GLU 3 GLU 4 0.0087

GLU 4 ALA 5 0.0002

ALA 5 GLN 6 0.0001

GLN 6 GLN 7 0.0106

GLN 7 ALA 8 0.0002

ALA 8 LYS 9 0.0003

LYS 9 ASP 10 0.0047

ASP 10 LYS 11 0.0001

LYS 11 GLY 12 0.0001

GLY 12 ASN 13 0.0003

ASN 13 LYS 14 -0.0001

LYS 14 ALA 15 0.0004

ALA 15 PHE 16 -0.0134

PHE 16 LYS 17 0.0002

LYS 17 GLY 18 0.0001

GLY 18 GLY 19 -0.0006

GLY 19 LYS 20 -0.0001

LYS 20 TYR 21 -0.0001

TYR 21 GLU 22 -0.0027

GLU 22 GLU 23 0.0002

GLU 23 ALA 24 -0.0001

ALA 24 ILE 25 0.0222

ILE 25 GLU 26 0.0004

GLU 26 CYS 27 -0.0001

CYS 27 TYR 28 -0.0060

TYR 28 SER 29 0.0003

SER 29 LYS 30 0.0001

LYS 30 ALA 31 0.0025

ALA 31 ILE 32 0.0000

ILE 32 GLU 33 0.0001

GLU 33 LEU 34 0.0135

LEU 34 CYS 35 -0.0003

CYS 35 PRO 36 -0.0001

PRO 36 GLU 37 0.0264

GLU 37 GLU 38 -0.0001

GLU 38 ASN 39 0.0003

ASN 39 LYS 40 0.0149

LYS 40 LYS 41 0.0003

LYS 41 ASN 42 0.0002

ASN 42 LEU 43 0.0134

LEU 43 ALA 44 -0.0001

ALA 44 VAL 45 -0.0003

VAL 45 PHE 46 -0.0045

PHE 46 TYR 47 -0.0001

TYR 47 SER 48 0.0002

SER 48 ASN 49 -0.0020

ASN 49 ARG 50 -0.0002

ARG 50 ALA 51 0.0004

ALA 51 ALA 52 0.0086

ALA 52 CYS 53 0.0001

CYS 53 TYR 54 0.0000

TYR 54 ALA 55 -0.0206

ALA 55 LYS 56 -0.0004

LYS 56 LEU 57 -0.0002

LEU 57 ASN 58 -0.0487

ASN 58 GLU 59 -0.0002

GLU 59 TYR 60 0.0000

TYR 60 GLU 61 -0.0083

GLU 61 LYS 62 -0.0001

LYS 62 VAL 63 -0.0002

VAL 63 VAL 64 -0.0009

VAL 64 GLU 65 0.0002

GLU 65 ASP 66 -0.0002

ASP 66 CYS 67 0.0090

CYS 67 THR 68 -0.0000

THR 68 LYS 69 -0.0000

LYS 69 ALA 70 -0.0115

ALA 70 LEU 71 -0.0004

LEU 71 GLU 72 -0.0002

GLU 72 LEU 73 -0.0023

LEU 73 ASP 74 -0.0002

ASP 74 PRO 75 0.0000

PRO 75 LYS 76 0.0285

LYS 76 TYR 77 -0.0000

TYR 77 VAL 78 -0.0001

VAL 78 LYS 79 -0.0045

LYS 79 ALA 80 -0.0002

ALA 80 LEU 81 0.0000

LEU 81 ASN 82 0.0129

ASN 82 ARG 83 0.0000

ARG 83 ARG 84 0.0002

ARG 84 ALA 85 -0.0255

ALA 85 THR 86 0.0001

THR 86 ALA 87 0.0000

ALA 87 TYR 88 -0.0166

TYR 88 GLU 89 -0.0001

GLU 89 LYS 90 -0.0000

LYS 90 LEU 91 0.0098

LEU 91 GLY 92 0.0000

GLY 92 GLU 93 0.0001

GLU 93 TYR 94 0.0314

TYR 94 GLU 95 0.0001

GLU 95 GLU 96 0.0002

GLU 96 ALA 97 -0.0157

ALA 97 LEU 98 -0.0002

LEU 98 GLN 99 -0.0001

GLN 99 ASP 100 0.0243

ASP 100 PHE 101 -0.0004

PHE 101 THR 102 0.0002

THR 102 ALA 103 -0.0205

ALA 103 VAL 104 0.0004

VAL 104 CYS 105 -0.0000

CYS 105 ILE 106 -0.0033

ILE 106 LEU 107 -0.0003

LEU 107 GLU 108 -0.0001

GLU 108 GLY 109 -0.0208

GLY 109 PHE 110 0.0005

PHE 110 LYS 111 0.0004

LYS 111 ASN 112 -0.0106

ASN 112 GLN 113 -0.0004

GLN 113 GLN 114 -0.0001

GLN 114 ALA 115 0.0170

ALA 115 MET 116 0.0002

MET 116 GLN 117 -0.0004

GLN 117 ALA 118 0.0202

ALA 118 ALA 119 -0.0001

ALA 119 GLU 120 -0.0002

GLU 120 ARG 121 0.0182

ARG 121 VAL 122 0.0003

VAL 122 LEU 123 -0.0002

LEU 123 LYS 124 0.0197

LYS 124 GLU 125 0.0003

GLU 125 ILE 126 -0.0001

ILE 126 GLY 127 -0.0004

GLY 127 LYS 128 0.0005

LYS 128 GLU 129 0.0002

GLU 129 LYS 130 -0.0023

LYS 130 ALA 131 -0.0003

ALA 131 LYS 132 -0.0002

LYS 132 GLU 133 -0.0052

GLU 133 ILE 134 0.0002

ILE 134 LEU 135 -0.0003

LEU 135 LYS 136 0.0186

LYS 136 ASN 137 0.0002

ASN 137 ARG 138 -0.0003

ARG 138 LYS 139 -0.0384

LYS 139 PRO 140 -0.0002

PRO 140 ARG 141 0.0002

ARG 141 LEU 142 -0.1551

LEU 142 PRO 143 0.0000

PRO 143 SER 144 -0.0001

SER 144 PRO 145 -0.0066

PRO 145 THR 146 0.0000

THR 146 PHE 147 -0.0001

PHE 147 ILE 148 0.0159

ILE 148 SER 149 0.0002

SER 149 SER 150 0.0001

SER 150 TYR 151 -0.0081

TYR 151 LEU 152 -0.0000

LEU 152 ASP 153 0.0003

ASP 153 SER 154 0.0046

SER 154 PHE 155 -0.0003

PHE 155 ARG 156 -0.0003

ARG 156 SER 157 0.0493

SER 157 ASP 158 -0.0001

ASP 158 PRO 159 0.0004

PRO 159 LYS 160 -0.0032

LYS 160 HIS 161 -0.0002

HIS 161 GLU 162 -0.0002

GLU 162 ALA 163 -0.0187

ALA 163 PRO 164 -0.0003

PRO 164 THR 165 0.0002

THR 165 GLU 166 0.0148

GLU 166 SER 167 0.0000

SER 167 GLU 168 -0.0001

GLU 168 GLU 169 0.0161

GLU 169 VAL 170 -0.0000

VAL 170 ASP 171 -0.0000

ASP 171 GLU 172 0.0134

GLU 172 ASP 173 -0.0000

ASP 173 LYS 174 -0.0001

LYS 174 ASP 175 -0.0017

ASP 175 ASP 176 0.0000

ASP 176 GLU 177 -0.0003

GLU 177 GLU 178 0.0000

GLU 178 GLN 179 -0.0003

GLN 179 GLY 180 -0.0002

GLY 180 ASP 181 -0.0004

ASP 181 LEU 182 -0.0000

LEU 182 TYR 183 -0.0000

TYR 183 PHE 184 0.0117

PHE 184 LEU 185 -0.0003

LEU 185 LYS 186 0.0000

LYS 186 ALA 187 0.0000

ALA 187 LEU 188 -0.0001

LEU 188 GLN 189 0.0004

GLN 189 HIS 190 -0.0114

HIS 190 MET 191 0.0003

MET 191 LYS 192 0.0002

LYS 192 GLU 193 -0.0109

GLU 193 LYS 194 0.0001

LYS 194 LYS 195 0.0002

LYS 195 TYR 196 -0.0045

TYR 196 GLU 197 0.0001

GLU 197 GLU 198 0.0000

GLU 198 ALA 199 -0.0220

ALA 199 MET 200 -0.0002

MET 200 ASP 201 0.0003

ASP 201 ALA 202 -0.0191

ALA 202 PHE 203 -0.0004

PHE 203 ASN 204 -0.0001

ASN 204 LYS 205 -0.0209

LYS 205 ALA 206 0.0000

ALA 206 ILE 207 -0.0005

ILE 207 ASP 208 -0.0019

ASP 208 GLU 209 -0.0003

GLU 209 ASP 210 -0.0002

ASP 210 GLY 211 0.0097

GLY 211 PRO 212 -0.0002

PRO 212 HIS 213 -0.0003

HIS 213 GLN 214 -0.0147

GLN 214 ALA 215 -0.0001

ALA 215 GLN 216 0.0005

GLN 216 ALA 217 -0.0076

ALA 217 PHE 218 -0.0000

PHE 218 ASN 219 0.0003

ASN 219 MET 220 -0.0077

MET 220 ARG 221 -0.0001

ARG 221 GLY 222 0.0000

GLY 222 THR 223 0.0013

THR 223 PHE 224 -0.0002

PHE 224 TYR 225 -0.0001

TYR 225 PHE 226 -0.0234

PHE 226 LEU 227 -0.0003

LEU 227 MET 228 -0.0000

MET 228 GLY 229 -0.0058

GLY 229 ASP 230 0.0003

ASP 230 VAL 231 -0.0001

VAL 231 ASP 232 0.0015

ASP 232 GLU 233 0.0003

GLU 233 ALA 234 -0.0001

ALA 234 LEU 235 0.0028

LEU 235 GLU 236 0.0000

GLU 236 ASP 237 0.0001

ASP 237 PHE 238 -0.0037

PHE 238 ASP 239 -0.0000

ASP 239 ARG 240 -0.0002

ARG 240 ALA 241 0.0033

ALA 241 LEU 242 -0.0000

LEU 242 GLU 243 0.0003

GLU 243 LEU 244 -0.0028

LEU 244 ASP 245 -0.0001

ASP 245 PRO 246 0.0001

PRO 246 SER 247 0.0082

SER 247 GLY 248 -0.0001

GLY 248 VAL 249 0.0002

VAL 249 LYS 250 -0.0073

LYS 250 LEU 251 -0.0000

LEU 251 ASN 252 -0.0001

ASN 252 VAL 253 0.0047

VAL 253 ASN 254 0.0002

ASN 254 ALA 255 0.0001

ALA 255 LEU 256 -0.0092

LEU 256 ILE 257 -0.0003

ILE 257 LYS 258 0.0003

LYS 258 ARG 259 -0.0010

ARG 259 ALA 260 -0.0002

ALA 260 SER 261 0.0005

SER 261 ILE 262 -0.0035

ILE 262 TYR 263 0.0002

TYR 263 MET 264 -0.0004

MET 264 GLU 265 0.0755

GLU 265 GLN 266 0.0002

GLN 266 GLY 267 -0.0000

GLY 267 ASP 268 0.0261

ASP 268 VAL 269 0.0003

VAL 269 ASP 270 -0.0002

ASP 270 GLU 271 -0.0133

GLU 271 ALA 272 -0.0002

ALA 272 LEU 273 -0.0000

LEU 273 GLU 274 -0.0179

GLU 274 ASP 275 0.0001

ASP 275 PHE 276 0.0001

PHE 276 GLU 277 0.0037

GLU 277 LYS 278 -0.0000

LYS 278 ALA 279 -0.0001

ALA 279 ILE 280 0.0039

ILE 280 LYS 281 0.0000

LYS 281 LEU 282 0.0002

LEU 282 ASP 283 0.0115

ASP 283 PRO 284 -0.0002

PRO 284 ASP 285 -0.0002

ASP 285 ASN 286 -0.0093

ASN 286 PRO 287 -0.0002

PRO 287 ASP 288 -0.0003

ASP 288 ILE 289 0.0066

ILE 289 TYR 290 -0.0001

TYR 290 TYR 291 -0.0002

TYR 291 HIS 292 -0.0043

HIS 292 ARG 293 0.0003

ARG 293 GLY 294 0.0002

GLY 294 GLN 295 -0.0066

GLN 295 LEU 296 0.0000

LEU 296 HIS 297 0.0001

HIS 297 PHE 298 -0.0270

PHE 298 LEU 299 0.0003

LEU 299 GLN 300 0.0001

GLN 300 GLY 301 -0.0409

GLY 301 ASP 302 0.0000

ASP 302 PHE 303 0.0002

PHE 303 ASP 304 -0.0033

ASP 304 GLU 305 -0.0001

GLU 305 ALA 306 0.0002

ALA 306 ILE 307 0.0026

ILE 307 LYS 308 -0.0001

LYS 308 ASP 309 0.0002

ASP 309 PHE 310 -0.0079

PHE 310 GLN 311 -0.0001

GLN 311 LYS 312 -0.0003

LYS 312 CYS 313 0.0014

CYS 313 ILE 314 -0.0000

ILE 314 GLU 315 -0.0000

GLU 315 LEU 316 0.0023

LEU 316 ASP 317 0.0001

ASP 317 PRO 318 0.0003

PRO 318 ASP 319 -0.0075

ASP 319 PHE 320 -0.0004

PHE 320 VAL 321 0.0001

VAL 321 LEU 322 -0.0117

LEU 322 ALA 323 0.0001

ALA 323 HIS 324 0.0001

HIS 324 ILE 325 0.0006

ILE 325 GLN 326 0.0002

GLN 326 LEU 327 -0.0001

LEU 327 ALA 328 0.0104

ALA 328 MET 329 -0.0002

MET 329 ALA 330 -0.0001

ALA 330 GLN 331 0.0012

GLN 331 TYR 332 -0.0002

TYR 332 LYS 333 -0.0003

LYS 333 MET 334 0.0015

MET 334 GLY 335 0.0002

GLY 335 SER 336 0.0000

SER 336 THR 337 0.0040

THR 337 GLN 338 0.0003

GLN 338 GLN 339 0.0003

GLN 339 SER 340 -0.0179

SER 340 PRO 341 0.0002

PRO 341 SER 342 -0.0003

SER 342 LEU 343 0.0054

LEU 343 ILE 344 0.0001

ILE 344 GLN 345 0.0001

GLN 345 GLU 346 0.0113

GLU 346 ALA 347 -0.0004

ALA 347 MET 348 -0.0001

MET 348 LYS 349 0.0238

LYS 349 THR 350 -0.0000

THR 350 PHE 351 -0.0004

PHE 351 GLU 352 -0.0085

GLU 352 LYS 353 0.0002

LYS 353 ALA 354 -0.0002

ALA 354 VAL 355 -0.0075

VAL 355 GLU 356 0.0001

GLU 356 LYS 357 0.0001

LYS 357 PHE 358 -0.0274

PHE 358 PRO 359 0.0003

PRO 359 ASP 360 -0.0002

ASP 360 SER 361 0.0100

SER 361 PRO 362 -0.0001

PRO 362 GLU 363 0.0002

GLU 363 VAL 364 -0.0138

VAL 364 TYR 365 0.0003

TYR 365 ASN 366 -0.0000

ASN 366 TYR 367 0.0138

TYR 367 TYR 368 -0.0000

TYR 368 GLY 369 -0.0002

GLY 369 GLU 370 0.0027

GLU 370 LEU 371 0.0003

LEU 371 LEU 372 0.0002

LEU 372 MET 373 0.0386

MET 373 ASP 374 -0.0001

ASP 374 GLN 375 0.0007

GLN 375 GLY 376 -0.0117

GLY 376 GLN 377 0.0001

GLN 377 PHE 378 0.0001

PHE 378 ASP 379 0.0067

ASP 379 GLU 380 -0.0003

GLU 380 ALA 381 -0.0000

ALA 381 MET 382 -0.0169

MET 382 GLU 383 0.0000

GLU 383 GLN 384 0.0002

GLN 384 PHE 385 0.0001

PHE 385 ASP 386 -0.0002

ASP 386 LYS 387 -0.0004

LYS 387 ALA 388 -0.0012

ALA 388 ILE 389 -0.0004

ILE 389 GLU 390 -0.0003

GLU 390 LEU 391 0.0028

LEU 391 GLU 392 0.0002

GLU 392 PRO 393 -0.0001

PRO 393 ASP 394 -0.0166

ASP 394 ASN 395 -0.0002

ASN 395 PRO 396 0.0003

PRO 396 MET 397 0.0095

MET 397 PRO 398 -0.0000

PRO 398 TYR 399 0.0002

TYR 399 VAL 400 0.0289

VAL 400 ASN 401 -0.0001

ASN 401 LYS 402 0.0001

LYS 402 ALA 403 0.0246

ALA 403 MET 404 0.0000

MET 404 LEU 405 0.0001

LEU 405 LEU 406 0.0117

LEU 406 LEU 407 -0.0001

LEU 407 GLN 408 0.0003

GLN 408 VAL 409 0.0039

VAL 409 LYS 410 0.0001

LYS 410 GLN 411 -0.0000

GLN 411 ASP 412 0.0311

ASP 412 ALA 413 -0.0001

ALA 413 ASP 414 0.0001

ASP 414 GLU 415 -0.0080

GLU 415 ALA 416 0.0001

ALA 416 VAL 417 -0.0002

VAL 417 LYS 418 -0.0217

LYS 418 LEU 419 -0.0001

LEU 419 LEU 420 0.0002

LEU 420 LYS 421 0.0272

LYS 421 LYS 422 0.0002

LYS 422 ALA 423 -0.0000

ALA 423 ILE 424 0.0014

ILE 424 GLU 425 0.0001

GLU 425 ILE 426 0.0004

ILE 426 ASP 427 0.0097

ASP 427 PRO 428 -0.0001

PRO 428 ARG 429 0.0002

ARG 429 CYS 430 -0.0275

CYS 430 ASP 431 -0.0000

ASP 431 VAL 432 0.0003

VAL 432 ALA 433 -0.0257

ALA 433 TYR 434 0.0000

TYR 434 VAL 435 0.0003

VAL 435 THR 436 -0.0038

THR 436 LEU 437 -0.0004

LEU 437 ALA 438 -0.0001

ALA 438 GLN 439 -0.0150

GLN 439 LEU 440 -0.0002

LEU 440 TYR 441 0.0001

TYR 441 LEU 442 -0.0260

LEU 442 GLN 443 0.0001

GLN 443 GLN 444 -0.0000

GLN 444 GLY 445 0.0480

GLY 445 LYS 446 -0.0001

LYS 446 VAL 447 0.0000

VAL 447 ASP 448 -0.0497

ASP 448 GLU 449 0.0005

GLU 449 ALA 450 0.0001

ALA 450 ILE 451 0.0189

ILE 451 GLU 452 -0.0001

GLU 452 LEU 453 -0.0003

LEU 453 PHE 454 -0.0171

PHE 454 ASP 455 0.0000

ASP 455 LYS 456 0.0003

LYS 456 ALA 457 0.0119

ALA 457 ILE 458 0.0000

ILE 458 ASP 459 -0.0002

ASP 459 LEU 460 -0.0032

LEU 460 ALA 461 0.0001

ALA 461 ARG 462 0.0004

ARG 462 THR 463 0.0095

THR 463 GLU 464 -0.0000

GLU 464 ALA 465 -0.0000

ALA 465 GLU 466 0.0362

GLU 466 LEU 467 -0.0001

LEU 467 ALA 468 -0.0002

ALA 468 ASN 469 -0.0068

ASN 469 ALA 470 0.0002

ALA 470 PHE 471 0.0002

PHE 471 SER 472 -0.0354

SER 472 MET 473 0.0000

MET 473 ARG 474 0.0001

ARG 474 GLU 475 0.0132

GLU 475 ALA 476 0.0003

ALA 476 ALA 477 -0.0003

ALA 477 LYS 478 0.0104

LYS 478 ALA 479 -0.0002

ALA 479 GLN 480 -0.0000

GLN 480 LEU 481 -0.0602

LEU 481 LYS 482 -0.0001

LYS 482 VAL 483 0.0000

VAL 483 THR 484 -0.0195

THR 484 LYS 485 -0.0003

LYS 485 LYS 486 0.0002

LYS 486 LEU 487 -0.0051

LEU 487 GLY 488 0.0001

GLY 488 VAL 489 0.0001

VAL 489 THR 490 0.0661

THR 490 LEU 491 0.0004

LEU 491 ALA 492 0.0002

ALA 492 THR 493 0.0085

THR 493 MET 494 0.0002

MET 494 ALA 495 -0.0000

ALA 495 GLN 496 -0.0109

GLN 496 MET 497 -0.0002

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 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.

* *