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 7 ---

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 -0.0001

PRO 21 GLU 22 -0.0029

GLU 22 LEU 23 0.0001

LEU 23 LEU 24 0.0029

LEU 24 ALA 25 -0.0001

ALA 25 SER 26 0.0049

SER 26 VAL 27 0.0002

VAL 27 THR 28 -0.0140

THR 28 PRO 29 -0.0000

PRO 29 PHE 30 0.0055

PHE 30 THR 31 -0.0002

THR 31 VAL 32 -0.0064

VAL 32 GLU 33 -0.0000

GLU 33 GLU 34 -0.0045

GLU 34 VAL 35 -0.0001

VAL 35 GLU 36 0.0040

GLU 36 ALA 37 -0.0001

ALA 37 LEU 38 0.0013

LEU 38 TYR 39 0.0001

TYR 39 GLU 40 0.0021

GLU 40 LEU 41 -0.0003

LEU 41 PHE 42 0.0005

PHE 42 LYS 43 0.0004

LYS 43 LYS 44 -0.0441

LYS 44 LEU 45 0.0000

LEU 45 SER 46 -0.0123

SER 46 SER 47 0.0001

SER 47 SER 48 -0.0157

SER 48 ILE 49 0.0001

ILE 49 ILE 50 -0.0009

ILE 50 ASP 51 0.0001

ASP 51 ASP 52 -0.0030

ASP 52 GLY 53 0.0003

GLY 53 LEU 54 0.0093

LEU 54 ILE 55 -0.0001

ILE 55 HIS 56 0.0355

HIS 56 LYS 57 -0.0000

LYS 57 GLU 58 -0.0194

GLU 58 GLU 59 0.0001

GLU 59 PHE 60 -0.0017

PHE 60 GLN 61 -0.0001

GLN 61 LEU 62 -0.0219

LEU 62 ALA 63 0.0000

ALA 63 LEU 64 -0.0154

LEU 64 PHE 65 -0.0001

PHE 65 ARG 66 0.0245

ARG 66 ASN 67 0.0001

ASN 67 ARG 68 -0.0116

ARG 68 ASN 69 0.0001

ASN 69 ARG 70 0.0398

ARG 70 ARG 71 -0.0002

ARG 71 ASN 72 -0.0268

ASN 72 LEU 73 -0.0000

LEU 73 PHE 74 -0.0046

PHE 74 ALA 75 -0.0002

ALA 75 ASP 76 -0.0317

ASP 76 ARG 77 0.0002

ARG 77 ILE 78 0.0132

ILE 78 PHE 79 0.0002

PHE 79 ASP 80 -0.0243

ASP 80 VAL 81 0.0001

VAL 81 PHE 82 0.0286

PHE 82 ASP 83 0.0000

ASP 83 VAL 84 -0.0090

VAL 84 LYS 85 0.0001

LYS 85 ARG 86 0.0251

ARG 86 ASN 87 -0.0002

ASN 87 GLY 88 0.0129

GLY 88 VAL 89 0.0002

VAL 89 ILE 90 0.0072

ILE 90 GLU 91 0.0001

GLU 91 PHE 92 0.0333

PHE 92 GLY 93 -0.0001

GLY 93 GLU 94 0.0494

GLU 94 PHE 95 0.0001

PHE 95 VAL 96 0.0133

VAL 96 ARG 97 -0.0003

ARG 97 SER 98 0.0392

SER 98 LEU 99 -0.0001

LEU 99 GLY 100 0.0014

GLY 100 VAL 101 -0.0000

VAL 101 PHE 102 0.0085

PHE 102 HIS 103 -0.0001

HIS 103 PRO 104 -0.0106

PRO 104 SER 105 0.0002

SER 105 ALA 106 0.0453

ALA 106 PRO 107 -0.0000

PRO 107 VAL 108 -0.0581

VAL 108 HIS 109 0.0001

HIS 109 GLU 110 -0.0053

GLU 110 LYS 111 -0.0005

LYS 111 VAL 112 0.0276

VAL 112 LYS 113 0.0000

LYS 113 PHE 114 -0.0170

PHE 114 ALA 115 -0.0001

ALA 115 PHE 116 0.0137

PHE 116 LYS 117 0.0002

LYS 117 LEU 118 -0.0044

LEU 118 TYR 119 -0.0000

TYR 119 ASP 120 -0.0292

ASP 120 LEU 121 0.0000

LEU 121 ARG 122 -0.0124

ARG 122 GLN 123 -0.0000

GLN 123 THR 124 0.0241

THR 124 GLY 125 -0.0002

GLY 125 PHE 126 -0.0110

PHE 126 ILE 127 -0.0002

ILE 127 GLU 128 0.0180

GLU 128 ARG 129 0.0002

ARG 129 GLU 130 0.0008

GLU 130 GLU 131 -0.0002

GLU 131 LEU 132 -0.0300

LEU 132 LYS 133 -0.0005

LYS 133 GLU 134 0.0337

GLU 134 MET 135 -0.0004

MET 135 VAL 136 0.0351

VAL 136 VAL 137 0.0001

VAL 137 ALA 138 0.0244

ALA 138 LEU 139 -0.0002

LEU 139 LEU 140 0.0313

LEU 140 HIS 141 -0.0003

HIS 141 GLU 142 -0.0097

GLU 142 SER 143 0.0000

SER 143 GLU 144 -0.0358

GLU 144 LEU 145 -0.0004

LEU 145 VAL 146 -0.0734

VAL 146 LEU 147 -0.0001

LEU 147 SER 148 -0.0191

SER 148 GLU 149 0.0002

GLU 149 ASP 150 0.0001

ASP 150 MET 151 -0.0003

MET 151 ILE 152 0.0805

ILE 152 GLU 153 0.0002

GLU 153 VAL 154 0.0348

VAL 154 MET 155 -0.0002

MET 155 VAL 156 0.0631

VAL 156 ASP 157 -0.0001

ASP 157 LYS 158 0.0136

LYS 158 ALA 159 0.0000

ALA 159 PHE 160 -0.0163

PHE 160 VAL 161 -0.0001

VAL 161 GLN 162 0.0069

GLN 162 ALA 163 0.0001

ALA 163 ASP 164 -0.0158

ASP 164 ARG 165 0.0002

ARG 165 LYS 166 -0.0017

LYS 166 ASN 167 0.0002

ASN 167 ASP 168 -0.0029

ASP 168 GLY 169 -0.0001

GLY 169 LYS 170 0.0045

LYS 170 ILE 171 -0.0001

ILE 171 ASP 172 0.0287

ASP 172 ILE 173 0.0004

ILE 173 ASP 174 -0.0070

ASP 174 GLU 175 -0.0001

GLU 175 TRP 176 -0.0018

TRP 176 LYS 177 0.0001

LYS 177 ASP 178 0.0046

ASP 178 PHE 179 -0.0003

PHE 179 VAL 180 -0.0022

VAL 180 SER 181 -0.0001

SER 181 LEU 182 -0.0105

LEU 182 ASN 183 0.0000

ASN 183 PRO 184 -0.0149

PRO 184 SER 185 0.0004

SER 185 LEU 186 0.0318

LEU 186 ILE 187 -0.0001

ILE 187 LYS 188 -0.0203

LYS 188 ASN 189 -0.0003

ASN 189 MET 190 -0.0717

MET 190 THR 191 0.0003

THR 191 LEU 192 0.0207

LEU 192 PRO 193 -0.0003

PRO 193 TYR 194 -0.0063

TYR 194 LEU 195 0.0002

LEU 195 LYS 196 -0.0052

LYS 196 ASP 197 -0.0002

ASP 197 ILE 198 0.0200

ILE 198 ASN 199 -0.0002

ASN 199 ARG 200 0.0107

ARG 200 THR 201 -0.0001

THR 201 GLU 305 -0.1752

GLU 305 GLY 306 -0.0001

GLY 306 PRO 307 -0.0060

PRO 307 LEU 308 0.0001

LEU 308 MET 309 -0.0434

MET 309 MET 310 0.0000

MET 310 ASN 311 -0.0677

ASN 311 ALA 312 -0.0001

ALA 312 PHE 313 -0.0170

PHE 313 GLU 314 -0.0003

GLU 314 MET 315 -0.0062

MET 315 ILE 316 -0.0003

ILE 316 THR 317 -0.0549

THR 317 LEU 318 0.0000

LEU 318 SER 319 -0.0071

SER 319 GLN 320 0.0001

GLN 320 GLY 321 -0.0213

GLY 321 LEU 322 -0.0001

LEU 322 ASN 323 0.0006

ASN 323 LEU 324 0.0001

LEU 324 SER 325 0.0164

SER 325 ALA 326 0.0001

ALA 326 LEU 327 -0.0255

LEU 327 PHE 328 -0.0001

PHE 328 ASP 329 -0.0193

ASP 329 ARG 330 0.0001

ARG 330 ARG 331 -0.0266

ARG 331 GLN 332 0.0001

GLN 332 ASP 333 0.0824

ASP 333 PHE 334 -0.0001

PHE 334 VAL 335 0.0272

VAL 335 LYS 336 -0.0005

LYS 336 ARG 337 -0.1296

ARG 337 GLN 338 -0.0002

GLN 338 THR 339 0.0057

THR 339 ARG 340 0.0002

ARG 340 PHE 341 -0.0714

PHE 341 VAL 342 -0.0003

VAL 342 SER 343 0.0313

SER 343 ARG 344 -0.0000

ARG 344 ARG 345 0.1115

ARG 345 GLU 346 0.0001

GLU 346 PRO 347 -0.0115

PRO 347 SER 348 0.0003

SER 348 GLU 349 -0.0200

GLU 349 ILE 350 0.0001

ILE 350 ILE 351 0.0566

ILE 351 ALA 352 -0.0003

ALA 352 ASN 353 0.0016

ASN 353 ILE 354 0.0002

ILE 354 GLU 355 0.0161

GLU 355 ALA 356 -0.0003

ALA 356 VAL 357 -0.0123

VAL 357 ALA 358 0.0002

ALA 358 ASN 359 -0.0042

ASN 359 SER 360 -0.0002

SER 360 MET 361 -0.0149

MET 361 GLY 362 -0.0001

GLY 362 PHE 363 -0.0114

PHE 363 LYS 364 -0.0002

LYS 364 SER 365 -0.0088

SER 365 HIS 366 -0.0001

HIS 366 THR 367 -0.0176

THR 367 ARG 368 0.0003

ARG 368 ASN 369 -0.0178

ASN 369 PHE 370 -0.0002

PHE 370 LYS 371 0.0348

LYS 371 THR 372 0.0001

THR 372 ARG 373 0.0214

ARG 373 LEU 374 -0.0001

LEU 374 GLU 375 -0.0091

GLU 375 GLY 376 0.0002

GLY 376 LEU 377 -0.0074

LEU 377 SER 378 0.0003

SER 378 SER 379 0.0424

SER 379 ILE 380 -0.0001

ILE 380 LYS 381 -0.0061

LYS 381 ALA 382 -0.0001

ALA 382 GLY 383 -0.0181

GLY 383 GLN 384 -0.0000

GLN 384 LEU 385 -0.0184

LEU 385 ALA 386 -0.0000

ALA 386 VAL 387 -0.0088

VAL 387 VAL 388 0.0005

VAL 388 ILE 389 0.0168

ILE 389 GLU 390 0.0002

GLU 390 ILE 391 0.0205

ILE 391 TYR 392 0.0002

TYR 392 GLU 393 0.0341

GLU 393 VAL 394 -0.0000

VAL 394 ALA 395 -0.0203

ALA 395 PRO 396 -0.0001

PRO 396 SER 397 0.0187

SER 397 LEU 398 -0.0000

LEU 398 PHE 399 0.0118

PHE 399 MET 400 0.0000

MET 400 VAL 401 0.0008

VAL 401 ASP 402 0.0000

ASP 402 VAL 403 -0.0194

VAL 403 ARG 404 0.0002

ARG 404 LYS 405 -0.0046

LYS 405 ALA 406 0.0002

ALA 406 ALA 407 -0.0088

ALA 407 GLY 408 -0.0001

GLY 408 GLU 409 0.0075

GLU 409 THR 410 -0.0000

THR 410 LEU 411 0.0205

LEU 411 GLU 412 0.0001

GLU 412 TYR 413 0.0141

TYR 413 HIS 414 0.0000

HIS 414 LYS 415 -0.0029

LYS 415 PHE 416 -0.0000

PHE 416 TYR 417 0.0220

TYR 417 LYS 418 0.0001

LYS 418 LYS 419 0.0090

LYS 419 LEU 420 0.0001

LEU 420 CYS 421 0.0104

CYS 421 SER 422 0.0003

SER 422 LYS 423 -0.0133

LYS 423 LEU 424 0.0002

LEU 424 GLU 425 0.0316

GLU 425 ASN 426 0.0002

ASN 426 ILE 427 -0.0070

ILE 427 ILE 428 -0.0003

ILE 428 TRP 429 0.1129

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 7 ---

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 *