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

* EHB *

CA strain for 260611084001679973

--- 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
ASP 20 PRO 21 -0.0000

PRO 21 GLU 22 0.0254

GLU 22 LEU 23 -0.0000

LEU 23 LEU 24 -0.0312

LEU 24 ALA 25 -0.0001

ALA 25 SER 26 0.0074

SER 26 VAL 27 -0.0001

VAL 27 THR 28 0.0246

THR 28 PRO 29 -0.0001

PRO 29 PHE 30 -0.0757

PHE 30 THR 31 0.0002

THR 31 VAL 32 0.0003

VAL 32 GLU 33 0.0001

GLU 33 GLU 34 0.0144

GLU 34 VAL 35 0.0004

VAL 35 GLU 36 -0.0425

GLU 36 ALA 37 -0.0001

ALA 37 LEU 38 0.0121

LEU 38 TYR 39 0.0000

TYR 39 GLU 40 -0.0169

GLU 40 LEU 41 -0.0003

LEU 41 PHE 42 -0.0108

PHE 42 LYS 43 -0.0001

LYS 43 LYS 44 0.1429

LYS 44 LEU 45 -0.0001

LEU 45 SER 46 -0.0178

SER 46 SER 47 0.0002

SER 47 SER 48 0.0259

SER 48 ILE 49 -0.0003

ILE 49 ILE 50 -0.0731

ILE 50 ASP 51 0.0001

ASP 51 ASP 52 0.0145

ASP 52 GLY 53 -0.0002

GLY 53 LEU 54 -0.0157

LEU 54 ILE 55 0.0000

ILE 55 HIS 56 -0.0925

HIS 56 LYS 57 0.0003

LYS 57 GLU 58 -0.0273

GLU 58 GLU 59 -0.0000

GLU 59 PHE 60 0.0411

PHE 60 GLN 61 0.0003

GLN 61 LEU 62 0.0306

LEU 62 ALA 63 0.0001

ALA 63 LEU 64 0.0168

LEU 64 PHE 65 -0.0000

PHE 65 ARG 66 -0.0336

ARG 66 ASN 67 0.0001

ASN 67 ARG 68 -0.2182

ARG 68 ASN 69 0.0004

ASN 69 ARG 70 0.0110

ARG 70 ARG 71 -0.0001

ARG 71 ASN 72 0.1428

ASN 72 LEU 73 -0.0001

LEU 73 PHE 74 0.0464

PHE 74 ALA 75 0.0002

ALA 75 ASP 76 0.0378

ASP 76 ARG 77 -0.0001

ARG 77 ILE 78 0.0050

ILE 78 PHE 79 -0.0003

PHE 79 ASP 80 0.0981

ASP 80 VAL 81 0.0003

VAL 81 PHE 82 -0.0179

PHE 82 ASP 83 0.0000

ASP 83 VAL 84 -0.0014

VAL 84 LYS 85 -0.0004

LYS 85 ARG 86 -0.0580

ARG 86 ASN 87 -0.0003

ASN 87 GLY 88 -0.1392

GLY 88 VAL 89 -0.0001

VAL 89 ILE 90 -0.0306

ILE 90 GLU 91 -0.0002

GLU 91 PHE 92 -0.1207

PHE 92 GLY 93 0.0003

GLY 93 GLU 94 -0.1772

GLU 94 PHE 95 -0.0002

PHE 95 VAL 96 -0.0363

VAL 96 ARG 97 -0.0002

ARG 97 SER 98 -0.2035

SER 98 LEU 99 -0.0000

LEU 99 GLY 100 -0.0065

GLY 100 VAL 101 -0.0003

VAL 101 PHE 102 -0.0325

PHE 102 HIS 103 0.0002

HIS 103 PRO 104 0.0521

PRO 104 SER 105 -0.0002

SER 105 ALA 106 -0.1409

ALA 106 PRO 107 0.0001

PRO 107 VAL 108 0.0723

VAL 108 HIS 109 -0.0004

HIS 109 GLU 110 0.0075

GLU 110 LYS 111 0.0003

LYS 111 VAL 112 -0.1499

VAL 112 LYS 113 0.0001

LYS 113 PHE 114 0.0344

PHE 114 ALA 115 -0.0003

ALA 115 PHE 116 -0.0682

PHE 116 LYS 117 -0.0002

LYS 117 LEU 118 -0.0149

LEU 118 TYR 119 0.0002

TYR 119 ASP 120 -0.0348

ASP 120 LEU 121 -0.0003

LEU 121 ARG 122 -0.0018

ARG 122 GLN 123 0.0002

GLN 123 THR 124 0.0367

THR 124 GLY 125 -0.0001

GLY 125 PHE 126 -0.0029

PHE 126 ILE 127 -0.0002

ILE 127 GLU 128 -0.0238

GLU 128 ARG 129 0.0003

ARG 129 GLU 130 0.0077

GLU 130 GLU 131 0.0002

GLU 131 LEU 132 -0.0437

LEU 132 LYS 133 0.0002

LYS 133 GLU 134 0.0338

GLU 134 MET 135 0.0000

MET 135 VAL 136 -0.0011

VAL 136 VAL 137 0.0002

VAL 137 ALA 138 0.0711

ALA 138 LEU 139 0.0000

LEU 139 LEU 140 0.0825

LEU 140 HIS 141 0.0001

HIS 141 GLU 142 0.0683

GLU 142 SER 143 0.0001

SER 143 GLU 144 0.0338

GLU 144 LEU 145 0.0003

LEU 145 VAL 146 -0.0480

VAL 146 LEU 147 -0.0000

LEU 147 SER 148 0.0122

SER 148 GLU 149 0.0000

GLU 149 ASP 150 -0.0070

ASP 150 MET 151 0.0004

MET 151 ILE 152 0.0642

ILE 152 GLU 153 0.0002

GLU 153 VAL 154 -0.0168

VAL 154 MET 155 0.0001

MET 155 VAL 156 -0.0283

VAL 156 ASP 157 0.0000

ASP 157 LYS 158 -0.0437

LYS 158 ALA 159 -0.0001

ALA 159 PHE 160 -0.0403

PHE 160 VAL 161 0.0001

VAL 161 GLN 162 0.0172

GLN 162 ALA 163 0.0002

ALA 163 ASP 164 -0.0160

ASP 164 ARG 165 -0.0000

ARG 165 LYS 166 -0.0067

LYS 166 ASN 167 -0.0000

ASN 167 ASP 168 0.0167

ASP 168 GLY 169 -0.0001

GLY 169 LYS 170 -0.0080

LYS 170 ILE 171 -0.0002

ILE 171 ASP 172 -0.0621

ASP 172 ILE 173 -0.0000

ILE 173 ASP 174 0.0396

ASP 174 GLU 175 0.0001

GLU 175 TRP 176 -0.0275

TRP 176 LYS 177 0.0000

LYS 177 ASP 178 -0.0078

ASP 178 PHE 179 -0.0000

PHE 179 VAL 180 -0.0172

VAL 180 SER 181 0.0000

SER 181 LEU 182 0.0123

LEU 182 ASN 183 0.0001

ASN 183 PRO 184 -0.0041

PRO 184 SER 185 0.0003

SER 185 LEU 186 -0.0050

LEU 186 ILE 187 -0.0003

ILE 187 LYS 188 0.0366

LYS 188 ASN 189 -0.0005

ASN 189 MET 190 0.0959

MET 190 THR 191 0.0004

THR 191 LEU 192 -0.0808

LEU 192 PRO 193 0.0001

PRO 193 TYR 194 -0.0007

TYR 194 LEU 195 0.0002

LEU 195 LYS 196 0.0549

LYS 196 ASP 197 -0.0002

ASP 197 ILE 198 -0.0861

ILE 198 ASN 199 -0.0002

ASN 199 ARG 200 -0.0428

ARG 200 THR 201 -0.0001

THR 201 GLU 305 0.0504

GLU 305 GLY 306 0.0001

GLY 306 PRO 307 0.0102

PRO 307 LEU 308 0.0001

LEU 308 MET 309 -0.1664

MET 309 MET 310 0.0000

MET 310 ASN 311 -0.2871

ASN 311 ALA 312 0.0000

ALA 312 PHE 313 0.0115

PHE 313 GLU 314 0.0002

GLU 314 MET 315 0.0139

MET 315 ILE 316 0.0003

ILE 316 THR 317 0.1600

THR 317 LEU 318 0.0001

LEU 318 SER 319 -0.1667

SER 319 GLN 320 -0.0004

GLN 320 GLY 321 -0.0158

GLY 321 LEU 322 -0.0001

LEU 322 ASN 323 0.0680

ASN 323 LEU 324 0.0003

LEU 324 SER 325 -0.0070

SER 325 ALA 326 -0.0002

ALA 326 LEU 327 0.0160

LEU 327 PHE 328 0.0001

PHE 328 ASP 329 0.1366

ASP 329 ARG 330 -0.0001

ARG 330 ARG 331 0.1705

ARG 331 GLN 332 -0.0000

GLN 332 ASP 333 0.0511

ASP 333 PHE 334 -0.0002

PHE 334 VAL 335 0.0820

VAL 335 LYS 336 -0.0001

LYS 336 ARG 337 0.1820

ARG 337 GLN 338 0.0003

GLN 338 THR 339 -0.0850

THR 339 ARG 340 -0.0001

ARG 340 PHE 341 -0.0560

PHE 341 VAL 342 -0.0002

VAL 342 SER 343 0.0352

SER 343 ARG 344 -0.0001

ARG 344 ARG 345 0.1644

ARG 345 GLU 346 -0.0001

GLU 346 PRO 347 -0.0114

PRO 347 SER 348 0.0003

SER 348 GLU 349 -0.0339

GLU 349 ILE 350 0.0003

ILE 350 ILE 351 0.0950

ILE 351 ALA 352 -0.0001

ALA 352 ASN 353 0.0025

ASN 353 ILE 354 0.0001

ILE 354 GLU 355 0.0249

GLU 355 ALA 356 0.0002

ALA 356 VAL 357 -0.0230

VAL 357 ALA 358 -0.0005

ALA 358 ASN 359 -0.0173

ASN 359 SER 360 0.0003

SER 360 MET 361 -0.0361

MET 361 GLY 362 -0.0001

GLY 362 PHE 363 -0.0292

PHE 363 LYS 364 0.0003

LYS 364 SER 365 -0.0171

SER 365 HIS 366 -0.0002

HIS 366 THR 367 -0.0509

THR 367 ARG 368 0.0002

ARG 368 ASN 369 -0.0691

ASN 369 PHE 370 -0.0001

PHE 370 LYS 371 0.0447

LYS 371 THR 372 0.0000

THR 372 ARG 373 0.0047

ARG 373 LEU 374 -0.0001

LEU 374 GLU 375 -0.0446

GLU 375 GLY 376 0.0000

GLY 376 LEU 377 -0.0331

LEU 377 SER 378 0.0002

SER 378 SER 379 0.1643

SER 379 ILE 380 -0.0001

ILE 380 LYS 381 -0.0292

LYS 381 ALA 382 -0.0002

ALA 382 GLY 383 -0.0734

GLY 383 GLN 384 -0.0000

GLN 384 LEU 385 -0.1029

LEU 385 ALA 386 -0.0001

ALA 386 VAL 387 -0.0476

VAL 387 VAL 388 -0.0002

VAL 388 ILE 389 0.0020

ILE 389 GLU 390 0.0005

GLU 390 ILE 391 -0.0099

ILE 391 TYR 392 -0.0003

TYR 392 GLU 393 -0.0395

GLU 393 VAL 394 0.0000

VAL 394 ALA 395 -0.0085

ALA 395 PRO 396 0.0001

PRO 396 SER 397 0.0197

SER 397 LEU 398 -0.0002

LEU 398 PHE 399 -0.0227

PHE 399 MET 400 -0.0001

MET 400 VAL 401 -0.0305

VAL 401 ASP 402 -0.0000

ASP 402 VAL 403 -0.0387

VAL 403 ARG 404 -0.0000

ARG 404 LYS 405 -0.0580

LYS 405 ALA 406 0.0000

ALA 406 ALA 407 -0.0469

ALA 407 GLY 408 -0.0001

GLY 408 GLU 409 -0.1484

GLU 409 THR 410 0.0000

THR 410 LEU 411 0.0422

LEU 411 GLU 412 -0.0004

GLU 412 TYR 413 0.0414

TYR 413 HIS 414 -0.0001

HIS 414 LYS 415 -0.0470

LYS 415 PHE 416 -0.0001

PHE 416 TYR 417 0.0500

TYR 417 LYS 418 0.0002

LYS 418 LYS 419 0.0186

LYS 419 LEU 420 -0.0003

LEU 420 CYS 421 0.0249

CYS 421 SER 422 0.0000

SER 422 LYS 423 -0.0118

LYS 423 LEU 424 -0.0001

LEU 424 GLU 425 0.0512

GLU 425 ASN 426 0.0000

ASN 426 ILE 427 -0.0108

ILE 427 ILE 428 -0.0004

ILE 428 TRP 429 0.1971

TRP 429 ARG 430 -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.

*** EHB ***

CA strain for 260611084001679973

--- 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.

* EHB *