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 9 ---

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 -0.0003

PRO 21 GLU 22 -0.0370

GLU 22 LEU 23 0.0001

LEU 23 LEU 24 -0.0202

LEU 24 ALA 25 0.0001

ALA 25 SER 26 -0.0403

SER 26 VAL 27 -0.0000

VAL 27 THR 28 0.0457

THR 28 PRO 29 0.0002

PRO 29 PHE 30 0.0397

PHE 30 THR 31 0.0001

THR 31 VAL 32 0.0234

VAL 32 GLU 33 0.0003

GLU 33 GLU 34 -0.0055

GLU 34 VAL 35 0.0003

VAL 35 GLU 36 0.0352

GLU 36 ALA 37 -0.0001

ALA 37 LEU 38 0.0101

LEU 38 TYR 39 0.0002

TYR 39 GLU 40 0.0214

GLU 40 LEU 41 0.0001

LEU 41 PHE 42 0.0185

PHE 42 LYS 43 -0.0001

LYS 43 LYS 44 -0.1635

LYS 44 LEU 45 0.0000

LEU 45 SER 46 -0.0001

SER 46 SER 47 -0.0002

SER 47 SER 48 -0.0908

SER 48 ILE 49 0.0001

ILE 49 ILE 50 -0.0730

ILE 50 ASP 51 -0.0001

ASP 51 ASP 52 -0.0029

ASP 52 GLY 53 0.0000

GLY 53 LEU 54 0.0243

LEU 54 ILE 55 0.0000

ILE 55 HIS 56 0.0159

HIS 56 LYS 57 -0.0000

LYS 57 GLU 58 -0.0437

GLU 58 GLU 59 -0.0002

GLU 59 PHE 60 0.0466

PHE 60 GLN 61 0.0000

GLN 61 LEU 62 -0.0376

LEU 62 ALA 63 -0.0002

ALA 63 LEU 64 -0.0660

LEU 64 PHE 65 -0.0001

PHE 65 ARG 66 0.0308

ARG 66 ASN 67 -0.0003

ASN 67 ARG 68 -0.1672

ARG 68 ASN 69 -0.0004

ASN 69 ARG 70 -0.0854

ARG 70 ARG 71 0.0002

ARG 71 ASN 72 0.0192

ASN 72 LEU 73 -0.0001

LEU 73 PHE 74 0.0088

PHE 74 ALA 75 -0.0002

ALA 75 ASP 76 0.0083

ASP 76 ARG 77 -0.0001

ARG 77 ILE 78 0.0069

ILE 78 PHE 79 -0.0001

PHE 79 ASP 80 0.0398

ASP 80 VAL 81 0.0001

VAL 81 PHE 82 0.1176

PHE 82 ASP 83 -0.0002

ASP 83 VAL 84 -0.0412

VAL 84 LYS 85 -0.0001

LYS 85 ARG 86 0.0459

ARG 86 ASN 87 -0.0001

ASN 87 GLY 88 -0.0673

GLY 88 VAL 89 -0.0002

VAL 89 ILE 90 0.0015

ILE 90 GLU 91 -0.0001

GLU 91 PHE 92 0.0395

PHE 92 GLY 93 -0.0002

GLY 93 GLU 94 0.1219

GLU 94 PHE 95 0.0001

PHE 95 VAL 96 -0.0190

VAL 96 ARG 97 -0.0004

ARG 97 SER 98 0.1305

SER 98 LEU 99 -0.0004

LEU 99 GLY 100 0.0070

GLY 100 VAL 101 0.0001

VAL 101 PHE 102 0.0089

PHE 102 HIS 103 -0.0001

HIS 103 PRO 104 -0.0057

PRO 104 SER 105 0.0000

SER 105 ALA 106 0.0080

ALA 106 PRO 107 -0.0002

PRO 107 VAL 108 0.0681

VAL 108 HIS 109 -0.0001

HIS 109 GLU 110 0.0357

GLU 110 LYS 111 0.0000

LYS 111 VAL 112 -0.0226

VAL 112 LYS 113 -0.0003

LYS 113 PHE 114 0.0449

PHE 114 ALA 115 0.0000

ALA 115 PHE 116 -0.0072

PHE 116 LYS 117 -0.0002

LYS 117 LEU 118 -0.0137

LEU 118 TYR 119 -0.0004

TYR 119 ASP 120 0.0173

ASP 120 LEU 121 0.0002

LEU 121 ARG 122 -0.0124

ARG 122 GLN 123 -0.0003

GLN 123 THR 124 0.1352

THR 124 GLY 125 0.0000

GLY 125 PHE 126 0.0264

PHE 126 ILE 127 -0.0001

ILE 127 GLU 128 -0.0187

GLU 128 ARG 129 -0.0000

ARG 129 GLU 130 -0.0217

GLU 130 GLU 131 0.0000

GLU 131 LEU 132 0.0723

LEU 132 LYS 133 -0.0000

LYS 133 GLU 134 0.0187

GLU 134 MET 135 0.0002

MET 135 VAL 136 -0.0037

VAL 136 VAL 137 -0.0003

VAL 137 ALA 138 0.0095

ALA 138 LEU 139 -0.0005

LEU 139 LEU 140 -0.0547

LEU 140 HIS 141 -0.0003

HIS 141 GLU 142 -0.0184

GLU 142 SER 143 -0.0002

SER 143 GLU 144 -0.0015

GLU 144 LEU 145 0.0001

LEU 145 VAL 146 0.0839

VAL 146 LEU 147 -0.0002

LEU 147 SER 148 0.0187

SER 148 GLU 149 -0.0005

GLU 149 ASP 150 0.0149

ASP 150 MET 151 -0.0002

MET 151 ILE 152 -0.0282

ILE 152 GLU 153 0.0000

GLU 153 VAL 154 0.0029

VAL 154 MET 155 0.0003

MET 155 VAL 156 0.0602

VAL 156 ASP 157 -0.0001

ASP 157 LYS 158 -0.0073

LYS 158 ALA 159 0.0001

ALA 159 PHE 160 0.0826

PHE 160 VAL 161 -0.0000

VAL 161 GLN 162 -0.0454

GLN 162 ALA 163 0.0002

ALA 163 ASP 164 0.0123

ASP 164 ARG 165 0.0003

ARG 165 LYS 166 0.0033

LYS 166 ASN 167 -0.0003

ASN 167 ASP 168 0.0027

ASP 168 GLY 169 -0.0003

GLY 169 LYS 170 0.0031

LYS 170 ILE 171 -0.0000

ILE 171 ASP 172 -0.0057

ASP 172 ILE 173 -0.0004

ILE 173 ASP 174 -0.0055

ASP 174 GLU 175 0.0002

GLU 175 TRP 176 -0.0014

TRP 176 LYS 177 -0.0001

LYS 177 ASP 178 0.0127

ASP 178 PHE 179 0.0004

PHE 179 VAL 180 -0.0388

VAL 180 SER 181 0.0002

SER 181 LEU 182 0.0246

LEU 182 ASN 183 -0.0004

ASN 183 PRO 184 0.0098

PRO 184 SER 185 -0.0001

SER 185 LEU 186 -0.0447

LEU 186 ILE 187 -0.0000

ILE 187 LYS 188 -0.0384

LYS 188 ASN 189 0.0002

ASN 189 MET 190 0.0813

MET 190 THR 191 -0.0000

THR 191 LEU 192 -0.0732

LEU 192 PRO 193 -0.0002

PRO 193 TYR 194 -0.0623

TYR 194 LEU 195 0.0000

LEU 195 LYS 196 0.0401

LYS 196 ASP 197 0.0000

ASP 197 ILE 198 0.0376

ILE 198 ASN 199 0.0001

ASN 199 ARG 200 0.0303

ARG 200 THR 201 0.0003

THR 201 GLU 305 -0.0681

GLU 305 GLY 306 -0.0001

GLY 306 PRO 307 0.0211

PRO 307 LEU 308 -0.0002

LEU 308 MET 309 0.1064

MET 309 MET 310 0.0000

MET 310 ASN 311 0.2338

ASN 311 ALA 312 -0.0003

ALA 312 PHE 313 0.0531

PHE 313 GLU 314 0.0001

GLU 314 MET 315 0.0720

MET 315 ILE 316 0.0002

ILE 316 THR 317 -0.0405

THR 317 LEU 318 0.0001

LEU 318 SER 319 -0.0005

SER 319 GLN 320 0.0000

GLN 320 GLY 321 0.0079

GLY 321 LEU 322 -0.0003

LEU 322 ASN 323 -0.0524

ASN 323 LEU 324 0.0003

LEU 324 SER 325 0.0231

SER 325 ALA 326 -0.0002

ALA 326 LEU 327 -0.0952

LEU 327 PHE 328 0.0000

PHE 328 ASP 329 -0.0348

ASP 329 ARG 330 0.0002

ARG 330 ARG 331 -0.1258

ARG 331 GLN 332 0.0003

GLN 332 ASP 333 0.0641

ASP 333 PHE 334 0.0001

PHE 334 VAL 335 0.1153

VAL 335 LYS 336 -0.0001

LYS 336 ARG 337 -0.1864

ARG 337 GLN 338 0.0001

GLN 338 THR 339 -0.0998

THR 339 ARG 340 0.0002

ARG 340 PHE 341 -0.0637

PHE 341 VAL 342 0.0002

VAL 342 SER 343 -0.1149

SER 343 ARG 344 -0.0004

ARG 344 ARG 345 -0.0746

ARG 345 GLU 346 0.0002

GLU 346 PRO 347 0.0032

PRO 347 SER 348 0.0001

SER 348 GLU 349 0.0294

GLU 349 ILE 350 -0.0001

ILE 350 ILE 351 -0.0372

ILE 351 ALA 352 -0.0002

ALA 352 ASN 353 -0.0421

ASN 353 ILE 354 -0.0000

ILE 354 GLU 355 0.0041

GLU 355 ALA 356 -0.0002

ALA 356 VAL 357 -0.0902

VAL 357 ALA 358 -0.0001

ALA 358 ASN 359 -0.0349

ASN 359 SER 360 -0.0003

SER 360 MET 361 -0.0475

MET 361 GLY 362 0.0003

GLY 362 PHE 363 -0.0139

PHE 363 LYS 364 0.0001

LYS 364 SER 365 0.0211

SER 365 HIS 366 0.0000

HIS 366 THR 367 0.0049

THR 367 ARG 368 0.0003

ARG 368 ASN 369 -0.0067

ASN 369 PHE 370 -0.0000

PHE 370 LYS 371 -0.0502

LYS 371 THR 372 0.0000

THR 372 ARG 373 -0.0294

ARG 373 LEU 374 0.0004

LEU 374 GLU 375 -0.0395

GLU 375 GLY 376 -0.0001

GLY 376 LEU 377 -0.0096

LEU 377 SER 378 0.0002

SER 378 SER 379 0.1703

SER 379 ILE 380 -0.0003

ILE 380 LYS 381 -0.0159

LYS 381 ALA 382 0.0002

ALA 382 GLY 383 -0.0536

GLY 383 GLN 384 -0.0002

GLN 384 LEU 385 -0.1070

LEU 385 ALA 386 -0.0001

ALA 386 VAL 387 -0.0665

VAL 387 VAL 388 -0.0001

VAL 388 ILE 389 -0.0326

ILE 389 GLU 390 -0.0002

GLU 390 ILE 391 -0.0317

ILE 391 TYR 392 0.0000

TYR 392 GLU 393 -0.0786

GLU 393 VAL 394 -0.0001

VAL 394 ALA 395 -0.0385

ALA 395 PRO 396 -0.0002

PRO 396 SER 397 0.1213

SER 397 LEU 398 0.0003

LEU 398 PHE 399 -0.0672

PHE 399 MET 400 -0.0005

MET 400 VAL 401 0.0350

VAL 401 ASP 402 -0.0003

ASP 402 VAL 403 0.0115

VAL 403 ARG 404 0.0002

ARG 404 LYS 405 -0.0811

LYS 405 ALA 406 -0.0002

ALA 406 ALA 407 -0.0976

ALA 407 GLY 408 0.0002

GLY 408 GLU 409 0.0110

GLU 409 THR 410 -0.0000

THR 410 LEU 411 0.1006

LEU 411 GLU 412 -0.0002

GLU 412 TYR 413 0.0622

TYR 413 HIS 414 0.0002

HIS 414 LYS 415 -0.0908

LYS 415 PHE 416 -0.0004

PHE 416 TYR 417 0.0749

TYR 417 LYS 418 0.0002

LYS 418 LYS 419 -0.0998

LYS 419 LEU 420 0.0003

LEU 420 CYS 421 0.0394

CYS 421 SER 422 -0.0003

SER 422 LYS 423 -0.0117

LYS 423 LEU 424 -0.0001

LEU 424 GLU 425 0.0230

GLU 425 ASN 426 0.0003

ASN 426 ILE 427 0.0378

ILE 427 ILE 428 0.0001

ILE 428 TRP 429 0.0766

TRP 429 ARG 430 -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.

*** EHB ***

CA strain for 260611084001679973

--- normal mode 9 ---

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 *