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 11 ---

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 -0.0001

LEU 2 ASP 3 -0.0002

ASP 3 ARG 4 -0.0085

ARG 4 ALA 5 -0.0000

ALA 5 GLN 6 -0.0004

GLN 6 ALA 7 -0.0149

ALA 7 ALA 8 -0.0002

ALA 8 LYS 9 0.0002

LYS 9 ASN 10 -0.0048

ASN 10 LYS 11 -0.0000

LYS 11 GLY 12 0.0001

GLY 12 ASN 13 -0.0012

ASN 13 LYS 14 -0.0002

LYS 14 TYR 15 0.0002

TYR 15 PHE 16 0.0275

PHE 16 LYS 17 -0.0004

LYS 17 ALA 18 0.0001

ALA 18 GLY 19 0.0044

GLY 19 LYS 20 0.0003

LYS 20 TYR 21 0.0000

TYR 21 GLU 22 0.0022

GLU 22 GLN 23 -0.0000

GLN 23 ALA 24 0.0001

ALA 24 ILE 25 -0.0181

ILE 25 GLN 26 0.0004

GLN 26 CYS 27 0.0002

CYS 27 TYR 28 0.0112

TYR 28 THR 29 -0.0001

THR 29 GLU 30 -0.0001

GLU 30 ALA 31 0.0034

ALA 31 ILE 32 0.0000

ILE 32 SER 33 0.0000

SER 33 LEU 34 -0.0265

LEU 34 CYS 35 -0.0003

CYS 35 PRO 36 -0.0001

PRO 36 THR 37 -0.0212

THR 37 GLU 38 -0.0002

GLU 38 LYS 39 0.0001

LYS 39 LYS 40 -0.0102

LYS 40 VAL 41 0.0001

VAL 41 ASP 42 -0.0000

ASP 42 LEU 43 -0.0141

LEU 43 SER 44 0.0001

SER 44 THR 45 -0.0000

THR 45 PHE 46 0.0065

PHE 46 TYR 47 0.0002

TYR 47 GLN 48 0.0003

GLN 48 ASN 49 0.0175

ASN 49 ARG 50 -0.0002

ARG 50 ALA 51 0.0003

ALA 51 ALA 52 -0.0170

ALA 52 ALA 53 -0.0002

ALA 53 PHE 54 0.0002

PHE 54 GLU 55 0.0141

GLU 55 GLN 56 0.0000

GLN 56 LEU 57 -0.0002

LEU 57 GLN 58 0.0349

GLN 58 LYS 59 0.0004

LYS 59 TRP 60 0.0000

TRP 60 LYS 61 0.0133

LYS 61 GLU 62 -0.0001

GLU 62 VAL 63 -0.0003

VAL 63 ALA 64 0.0061

ALA 64 GLN 65 0.0000

GLN 65 ASP 66 0.0003

ASP 66 CYS 67 -0.0062

CYS 67 THR 68 -0.0002

THR 68 LYS 69 0.0002

LYS 69 ALA 70 0.0182

ALA 70 VAL 71 -0.0003

VAL 71 GLU 72 -0.0001

GLU 72 LEU 73 -0.0146

LEU 73 ASN 74 0.0004

ASN 74 PRO 75 0.0001

PRO 75 ARG 76 -0.0232

ARG 76 TYR 77 0.0000

TYR 77 VAL 78 -0.0001

VAL 78 LYS 79 -0.0115

LYS 79 ALA 80 -0.0003

ALA 80 LEU 81 0.0000

LEU 81 PHE 82 -0.0008

PHE 82 ARG 83 -0.0002

ARG 83 ARG 84 -0.0001

ARG 84 ALA 85 0.0251

ALA 85 LYS 86 0.0002

LYS 86 ALA 87 0.0002

ALA 87 HIS 88 -0.0002

HIS 88 GLU 89 -0.0004

GLU 89 LYS 90 -0.0002

LYS 90 LEU 91 -0.0005

LEU 91 ASP 92 -0.0001

ASP 92 ASN 93 0.0005

ASN 93 LYS 94 -0.0586

LYS 94 LYS 95 -0.0003

LYS 95 GLU 96 0.0004

GLU 96 CYS 97 -0.0034

CYS 97 LEU 98 0.0000

LEU 98 GLU 99 0.0001

GLU 99 ASP 100 -0.0108

ASP 100 VAL 101 -0.0001

VAL 101 THR 102 0.0003

THR 102 ALA 103 0.0226

ALA 103 VAL 104 0.0001

VAL 104 CYS 105 -0.0003

CYS 105 ILE 106 0.0005

ILE 106 LEU 107 0.0002

LEU 107 GLU 108 -0.0002

GLU 108 GLY 109 0.0362

GLY 109 PHE 110 0.0003

PHE 110 GLN 111 -0.0001

GLN 111 ASN 112 0.0119

ASN 112 GLN 113 -0.0002

GLN 113 GLN 114 -0.0001

GLN 114 SER 115 -0.0106

SER 115 MET 116 0.0001

MET 116 LEU 117 0.0000

LEU 117 LEU 118 -0.0509

LEU 118 ALA 119 0.0003

ALA 119 ASP 120 -0.0003

ASP 120 LYS 121 -0.0481

LYS 121 VAL 122 -0.0002

VAL 122 LEU 123 0.0002

LEU 123 LYS 124 -0.0433

LYS 124 LEU 125 -0.0000

LEU 125 LEU 126 0.0002

LEU 126 GLY 127 -0.0347

GLY 127 LYS 128 0.0003

LYS 128 GLU 129 0.0002

GLU 129 LYS 130 0.0033

LYS 130 ALA 131 -0.0001

ALA 131 LYS 132 -0.0002

LYS 132 GLU 133 -0.0194

GLU 133 LYS 134 0.0000

LYS 134 TYR 135 0.0000

TYR 135 LYS 136 -0.0312

LYS 136 ASN 137 0.0001

ASN 137 ARG 138 0.0000

ARG 138 GLU 139 0.0671

GLU 139 PRO 140 0.0001

PRO 140 LEU 141 -0.0000

LEU 141 MET 142 0.1610

MET 142 PRO 143 -0.0003

PRO 143 SER 144 -0.0001

SER 144 PRO 145 0.0048

PRO 145 GLN 146 -0.0003

GLN 146 PHE 147 0.0002

PHE 147 ILE 148 -0.0262

ILE 148 LYS 149 0.0003

LYS 149 SER 150 0.0004

SER 150 TYR 151 -0.0075

TYR 151 PHE 152 -0.0003

PHE 152 SER 153 -0.0004

SER 153 SER 154 -0.0086

SER 154 PHE 155 -0.0000

PHE 155 THR 156 -0.0001

THR 156 ASP 157 0.0220

ASP 157 ASP 158 0.0000

ASP 158 ILE 159 0.0001

ILE 159 ILE 160 -0.0037

ILE 160 SER 161 -0.0002

SER 161 GLN 162 -0.0003

GLN 162 PRO 163 -0.0550

PRO 163 MET 164 0.0001

MET 164 LEU 165 0.0001

LEU 165 LYS 166 -0.0969

LYS 166 GLY 167 -0.0001

GLY 167 GLU 168 -0.0003

GLU 168 LYS 169 -0.0356

LYS 169 SER 170 0.0002

SER 170 ASP 171 -0.0002

ASP 171 GLU 172 0.0352

GLU 172 ASP 173 0.0003

ASP 173 LYS 174 -0.0000

LYS 174 ALA 175 -0.0658

ALA 175 LEU 176 -0.0002

LEU 176 GLU 177 -0.0001

GLU 177 VAL 178 -0.0608

VAL 178 LYS 179 0.0000

LYS 179 GLU 180 -0.0001

GLU 180 ASN 181 0.0286

ASN 181 SER 182 0.0002

SER 182 GLY 183 0.0001

GLY 183 TYR 184 0.0648

TYR 184 LEU 185 -0.0003

LEU 185 LYS 186 -0.0002

LYS 186 ALA 187 0.0438

ALA 187 LYS 188 -0.0001

LYS 188 GLN 189 0.0001

GLN 189 TYR 190 0.0155

TYR 190 MET 191 -0.0000

MET 191 GLU 192 -0.0001

GLU 192 GLU 193 0.0104

GLU 193 GLU 194 -0.0001

GLU 194 ASN 195 -0.0002

ASN 195 TYR 196 0.0110

TYR 196 ASP 197 -0.0005

ASP 197 LYS 198 -0.0003

LYS 198 ILE 199 0.0025

ILE 199 ILE 200 0.0001

ILE 200 SER 201 -0.0003

SER 201 GLU 202 0.0692

GLU 202 CYS 203 0.0000

CYS 203 THR 204 0.0002

THR 204 LYS 205 0.0476

LYS 205 GLU 206 -0.0002

GLU 206 ILE 207 0.0002

ILE 207 ASP 208 -0.0006

ASP 208 ALA 209 0.0000

ALA 209 GLN 210 0.0004

GLN 210 GLY 211 0.0351

GLY 211 LYS 212 -0.0000

LYS 212 TYR 213 0.0002

TYR 213 MET 214 0.0043

MET 214 ALA 215 -0.0003

ALA 215 GLU 216 0.0002

GLU 216 ALA 217 -0.0081

ALA 217 LEU 218 0.0001

LEU 218 LEU 219 0.0003

LEU 219 LEU 220 0.0124

LEU 220 ARG 221 -0.0002

ARG 221 ALA 222 0.0000

ALA 222 THR 223 0.0108

THR 223 PHE 224 0.0003

PHE 224 TYR 225 0.0001

TYR 225 LEU 226 0.0606

LEU 226 LEU 227 -0.0002

LEU 227 ILE 228 -0.0001

ILE 228 GLY 229 0.0390

GLY 229 ASN 230 -0.0000

ASN 230 ALA 231 -0.0000

ALA 231 ASN 232 -0.0109

ASN 232 ALA 233 -0.0000

ALA 233 ALA 234 0.0005

ALA 234 LYS 235 -0.0118

LYS 235 PRO 236 -0.0003

PRO 236 ASP 237 0.0001

ASP 237 LEU 238 0.0194

LEU 238 ASP 239 -0.0001

ASP 239 GLN 240 0.0000

GLN 240 VAL 241 -0.0128

VAL 241 ILE 242 -0.0004

ILE 242 SER 243 0.0001

SER 243 MET 244 -0.0011

MET 244 GLU 245 0.0001

GLU 245 GLU 246 0.0002

GLU 246 ALA 247 -0.0016

ALA 247 ASN 248 -0.0001

ASN 248 VAL 249 -0.0002

VAL 249 LYS 250 0.0037

LYS 250 LEU 251 -0.0004

LEU 251 ARG 252 0.0000

ARG 252 ALA 253 -0.0149

ALA 253 ASN 254 0.0003

ASN 254 ALA 255 0.0000

ALA 255 LEU 256 0.0003

LEU 256 ILE 257 0.0003

ILE 257 LYS 258 -0.0001

LYS 258 ARG 259 -0.0127

ARG 259 GLY 260 0.0001

GLY 260 SER 261 -0.0000

SER 261 MET 262 -0.0024

MET 262 TYR 263 -0.0001

TYR 263 MET 264 0.0000

MET 264 GLN 265 -0.0985

GLN 265 GLN 266 -0.0000

GLN 266 GLN 267 -0.0001

GLN 267 GLN 268 -0.1110

GLN 268 PRO 269 0.0002

PRO 269 LEU 270 -0.0002

LEU 270 LEU 271 0.0059

LEU 271 SER 272 -0.0001

SER 272 THR 273 -0.0001

THR 273 GLN 274 0.0266

GLN 274 ASP 275 0.0001

ASP 275 PHE 276 0.0001

PHE 276 ASN 277 -0.0009

ASN 277 MET 278 0.0001

MET 278 ALA 279 -0.0000

ALA 279 ALA 280 0.0004

ALA 280 ASP 281 -0.0000

ASP 281 ILE 282 -0.0000

ILE 282 ASP 283 -0.0100

ASP 283 PRO 284 -0.0004

PRO 284 GLN 285 -0.0004

GLN 285 ASN 286 0.0235

ASN 286 ALA 287 -0.0000

ALA 287 ASP 288 0.0000

ASP 288 VAL 289 -0.0204

VAL 289 TYR 290 -0.0003

TYR 290 HIS 291 0.0002

HIS 291 HIS 292 0.0047

HIS 292 ARG 293 0.0002

ARG 293 GLY 294 0.0002

GLY 294 GLN 295 0.0195

GLN 295 LEU 296 -0.0002

LEU 296 LYS 297 0.0000

LYS 297 ILE 298 0.0513

ILE 298 LEU 299 0.0001

LEU 299 LEU 300 0.0004

LEU 300 ASP 301 0.0494

ASP 301 GLN 302 0.0004

GLN 302 VAL 303 0.0000

VAL 303 GLU 304 0.0011

GLU 304 GLU 305 -0.0002

GLU 305 ALA 306 -0.0004

ALA 306 VAL 307 0.0020

VAL 307 ALA 308 -0.0001

ALA 308 ASP 309 0.0004

ASP 309 PHE 310 0.0142

PHE 310 ASP 311 0.0000

ASP 311 GLU 312 -0.0004

GLU 312 CYS 313 -0.0140

CYS 313 ILE 314 -0.0000

ILE 314 ARG 315 -0.0001

ARG 315 LEU 316 -0.0046

LEU 316 ARG 317 0.0004

ARG 317 PRO 318 -0.0002

PRO 318 ASP 319 0.0431

ASP 319 SER 320 -0.0001

SER 320 ALA 321 -0.0002

ALA 321 LEU 322 0.0048

LEU 322 ALA 323 0.0000

ALA 323 GLN 324 0.0001

GLN 324 ALA 325 -0.0026

ALA 325 GLN 326 -0.0001

GLN 326 LYS 327 -0.0005

LYS 327 CYS 328 -0.0262

CYS 328 PHE 329 -0.0001

PHE 329 ALA 330 0.0002

ALA 330 LEU 331 0.0063

LEU 331 TYR 332 0.0001

TYR 332 ARG 333 -0.0003

ARG 333 GLN 334 -0.0086

GLN 334 ALA 335 -0.0000

ALA 335 TYR 336 -0.0001

TYR 336 THR 337 0.0125

THR 337 GLY 338 0.0003

GLY 338 ASN 339 -0.0003

ASN 339 ASN 340 0.0122

ASN 340 SER 341 -0.0003

SER 341 THR 342 0.0001

THR 342 GLN 343 -0.0044

GLN 343 VAL 344 0.0001

VAL 344 GLN 345 -0.0000

GLN 345 ALA 346 -0.0128

ALA 346 ALA 347 0.0001

ALA 347 MET 348 0.0000

MET 348 LYS 349 -0.0087

LYS 349 GLY 350 0.0003

GLY 350 PHE 351 -0.0001

PHE 351 GLU 352 0.0192

GLU 352 ASP 353 0.0001

ASP 353 VAL 354 -0.0000

VAL 354 ILE 355 0.0000

ILE 355 LYS 356 -0.0003

LYS 356 LYS 357 0.0001

LYS 357 PHE 358 0.0206

PHE 358 PRO 359 -0.0001

PRO 359 ARG 360 -0.0000

ARG 360 CYS 361 -0.0252

CYS 361 ALA 362 0.0001

ALA 362 GLU 363 -0.0002

GLU 363 GLY 364 -0.0003

GLY 364 TYR 365 -0.0002

TYR 365 ALA 366 -0.0002

ALA 366 LEU 367 -0.0077

LEU 367 TYR 368 -0.0003

TYR 368 ALA 369 0.0001

ALA 369 GLN 370 -0.0024

GLN 370 ALA 371 -0.0003

ALA 371 LEU 372 0.0000

LEU 372 THR 373 -0.0295

THR 373 ASP 374 0.0002

ASP 374 GLN 375 -0.0001

GLN 375 GLN 376 -0.0028

GLN 376 GLN 377 -0.0001

GLN 377 PHE 378 -0.0001

PHE 378 GLY 379 -0.0060

GLY 379 LYS 380 0.0000

LYS 380 ALA 381 0.0000

ALA 381 ASP 382 0.0065

ASP 382 GLU 383 -0.0003

GLU 383 MET 384 -0.0004

MET 384 TYR 385 -0.0072

TYR 385 ASP 386 0.0000

ASP 386 LYS 387 -0.0002

LYS 387 CYS 388 -0.0066

CYS 388 ILE 389 -0.0001

ILE 389 ASP 390 0.0003

ASP 390 LEU 391 0.0064

LEU 391 GLU 392 -0.0001

GLU 392 PRO 393 -0.0001

PRO 393 ASP 394 0.0036

ASP 394 ASN 395 -0.0003

ASN 395 ALA 396 0.0000

ALA 396 THR 397 -0.0090

THR 397 THR 398 -0.0001

THR 398 TYR 399 -0.0003

TYR 399 VAL 400 -0.0103

VAL 400 HIS 401 -0.0001

HIS 401 LYS 402 -0.0002

LYS 402 GLY 403 0.0063

GLY 403 LEU 404 0.0001

LEU 404 LEU 405 -0.0001

LEU 405 GLN 406 -0.0085

GLN 406 LEU 407 0.0003

LEU 407 GLN 408 -0.0001

GLN 408 TRP 409 0.0265

TRP 409 LYS 410 -0.0001

LYS 410 GLN 411 0.0002

GLN 411 ASP 412 -0.0290

ASP 412 LEU 413 -0.0003

LEU 413 ASP 414 -0.0002

ASP 414 LYS 415 0.0330

LYS 415 GLY 416 -0.0003

GLY 416 LEU 417 -0.0000

LEU 417 GLU 418 0.0218

GLU 418 LEU 419 -0.0002

LEU 419 ILE 420 0.0004

ILE 420 SER 421 -0.0046

SER 421 LYS 422 -0.0001

LYS 422 ALA 423 -0.0002

ALA 423 ILE 424 -0.0090

ILE 424 GLU 425 -0.0004

GLU 425 ILE 426 -0.0001

ILE 426 ASP 427 -0.0117

ASP 427 ASN 428 0.0000

ASN 428 LYS 429 -0.0002

LYS 429 CYS 430 0.0158

CYS 430 ASP 431 -0.0000

ASP 431 PHE 432 -0.0003

PHE 432 ALA 433 0.0046

ALA 433 TYR 434 0.0005

TYR 434 GLU 435 -0.0001

GLU 435 THR 436 0.0117

THR 436 MET 437 0.0002

MET 437 GLY 438 0.0002

GLY 438 THR 439 0.0085

THR 439 ILE 440 -0.0003

ILE 440 GLU 441 -0.0001

GLU 441 VAL 442 0.0269

VAL 442 GLN 443 -0.0001

GLN 443 ARG 444 0.0000

ARG 444 GLY 445 -0.0217

GLY 445 ASN 446 -0.0003

ASN 446 MET 447 0.0001

MET 447 ASP 448 0.0318

ASP 448 LYS 449 0.0001

LYS 449 ALA 450 -0.0001

ALA 450 ILE 451 -0.0121

ILE 451 ASP 452 -0.0001

ASP 452 MET 453 0.0004

MET 453 PHE 454 0.0087

PHE 454 ASN 455 -0.0002

ASN 455 LYS 456 -0.0001

LYS 456 ALA 457 -0.0034

ALA 457 ILE 458 -0.0001

ILE 458 ASN 459 -0.0001

ASN 459 LEU 460 0.0027

LEU 460 ALA 461 -0.0000

ALA 461 LYS 462 0.0003

LYS 462 SER 463 -0.0193

SER 463 GLU 464 0.0004

GLU 464 MET 465 0.0004

MET 465 GLU 466 -0.0342

GLU 466 MET 467 0.0001

MET 467 ALA 468 -0.0003

ALA 468 HIS 469 0.0102

HIS 469 LEU 470 -0.0003

LEU 470 TYR 471 0.0001

TYR 471 SER 472 0.0622

SER 472 LEU 473 0.0000

LEU 473 CYS 474 -0.0003

CYS 474 ASP 475 0.0093

ASP 475 ALA 476 0.0001

ALA 476 ALA 477 0.0002

ALA 477 TYR 478 0.0100

TYR 478 ALA 479 0.0002

ALA 479 GLN 480 0.0000

GLN 480 THR 481 0.0348

THR 481 GLU 482 -0.0004

GLU 482 VAL 483 0.0003

VAL 483 ALA 484 0.0169

ALA 484 LYS 485 0.0004

LYS 485 LYS 486 0.0000

LYS 486 TYR 487 -0.0439

TYR 487 GLY 488 -0.0000

GLY 488 LEU 489 -0.0002

LEU 489 LYS 490 0.0107

LYS 490 PRO 491 0.0000

PRO 491 PRO 492 -0.0002

PRO 492 THR 493 0.1116

THR 493 LEU 494 0.0000

LEU 494 ASN 495 -0.0004

ASN 495 VAL 496 0.0057

VAL 496 MET 497 -0.0001

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 11 ---

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

* *