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

* close cutoff 10 melek *

CA strain for 260522120726406031

--- normal mode 15 ---

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
ALA 1 SER 2 0.0573

SER 2 SER 3 -0.0171

SER 3 THR 4 0.0466

THR 4 ASN 5 0.0007

ASN 5 LEU 6 -0.1458

LEU 6 LYS 7 -0.0443

LYS 7 ASP 8 0.0772

ASP 8 VAL 9 -0.0535

VAL 9 LEU 10 0.0593

LEU 10 ALA 11 -0.0223

ALA 11 SER 12 0.1201

SER 12 LEU 13 0.0462

LEU 13 ILE 14 -0.1708

ILE 14 PRO 15 0.0861

PRO 15 LYS 16 0.0701

LYS 16 GLU 17 -0.0446

GLU 17 GLN 18 0.0028

GLN 18 ALA 19 -0.0287

ALA 19 ARG 20 0.1248

ARG 20 ILE 21 0.1686

ILE 21 LYS 22 -0.3969

LYS 22 THR 23 0.2694

THR 23 PHE 24 0.2268

PHE 24 ARG 25 0.1983

ARG 25 GLN 26 -0.0376

GLN 26 GLN 27 0.3060

GLN 27 HIS 28 0.2501

HIS 28 GLY 29 0.4999

GLY 29 ASN 30 0.7042

ASN 30 THR 31 0.7632

THR 31 ALA 32 -0.0609

ALA 32 VAL 33 0.9724

VAL 33 GLY 34 0.2095

GLY 34 GLN 35 0.0073

GLN 35 ILE 36 0.1789

ILE 36 THR 37 0.1924

THR 37 VAL 38 0.2659

VAL 38 ASP 39 0.5379

ASP 39 MET 40 0.2042

MET 40 SER 41 0.2215

SER 41 TYR 42 0.4256

TYR 42 GLY 43 -0.0316

GLY 43 GLY 44 0.3629

GLY 44 MET 45 0.3363

MET 45 ARG 46 0.0479

ARG 46 GLY 47 0.1174

GLY 47 MET 48 0.1602

MET 48 LYS 49 0.0506

LYS 49 GLY 50 0.2606

GLY 50 LEU 51 0.0861

LEU 51 ILE 52 0.0076

ILE 52 TYR 53 0.0112

TYR 53 GLU 54 0.0477

GLU 54 THR 55 0.0067

THR 55 SER 56 -0.0630

SER 56 VAL 57 -0.0361

VAL 57 LEU 58 -0.0939

LEU 58 ASP 59 0.0890

ASP 59 PRO 60 -0.0087

PRO 60 ASP 61 0.0239

ASP 61 GLU 62 -0.0380

GLU 62 GLY 63 0.0762

GLY 63 ILE 64 -0.0549

ILE 64 ARG 65 -0.0165

ARG 65 PHE 66 -0.1576

PHE 66 ARG 67 0.0336

ARG 67 GLY 68 0.0111

GLY 68 PHE 69 0.0294

PHE 69 SER 70 -0.1620

SER 70 ILE 71 0.0240

ILE 71 PRO 72 0.1527

PRO 72 GLU 73 -0.0251

GLU 73 CYS 74 0.0052

CYS 74 GLN 75 0.0118

GLN 75 LYS 76 0.0366

LYS 76 LEU 77 0.0096

LEU 77 LEU 78 0.0510

LEU 78 PRO 79 -0.0077

PRO 79 LYS 80 0.0214

LYS 80 ALA 81 -0.0501

ALA 81 GLY 82 0.0539

GLY 82 GLY 84 0.0491

GLY 84 GLU 85 0.0094

GLU 85 GLU 86 0.0016

GLU 86 PRO 87 0.0016

PRO 87 LEU 88 -0.0076

LEU 88 PRO 89 0.0292

PRO 89 GLU 90 0.0184

GLU 90 GLY 91 0.0126

GLY 91 LEU 92 0.0137

LEU 92 PHE 93 -0.0128

PHE 93 TRP 94 0.0211

TRP 94 LEU 95 -0.0419

LEU 95 LEU 96 0.0266

LEU 96 VAL 97 -0.0443

VAL 97 THR 98 0.0722

THR 98 GLY 99 -0.1080

GLY 99 GLN 100 0.0096

GLN 100 ILE 101 0.0088

ILE 101 PRO 102 -0.0343

PRO 102 THR 103 0.0328

THR 103 PRO 104 0.0409

PRO 104 GLU 105 0.0584

GLU 105 GLN 106 -0.0022

GLN 106 VAL 107 0.0463

VAL 107 SER 108 0.0288

SER 108 TRP 109 0.0770

TRP 109 VAL 110 -0.0239

VAL 110 SER 111 0.0682

SER 111 LYS 112 0.0039

LYS 112 GLU 113 0.0308

GLU 113 TRP 114 0.0385

TRP 114 ALA 115 0.0026

ALA 115 LYS 116 -0.0226

LYS 116 ARG 117 -0.0009

ARG 117 ALA 118 0.0199

ALA 118 ALA 119 0.0142

ALA 119 LEU 120 -0.0387

LEU 120 PRO 121 0.0349

PRO 121 SER 122 0.0085

SER 122 HIS 123 0.0070

HIS 123 VAL 124 0.0361

VAL 124 VAL 125 -0.0030

VAL 125 THR 126 0.0164

THR 126 MET 127 0.0567

MET 127 LEU 128 -0.0079

LEU 128 ASP 129 0.0271

ASP 129 ASN 130 0.0155

ASN 130 PHE 131 0.0815

PHE 131 PRO 132 0.0378

PRO 132 THR 133 0.0321

THR 133 ASN 134 0.0263

ASN 134 LEU 135 0.0141

LEU 135 HIS 136 0.0586

HIS 136 PRO 137 0.0712

PRO 137 MET 138 0.0701

MET 138 SER 139 0.0210

SER 139 GLN 140 0.0812

GLN 140 LEU 141 -0.0032

LEU 141 SER 142 -0.0082

SER 142 ALA 143 0.0437

ALA 143 ALA 144 -0.0165

ALA 144 ILE 145 0.0169

ILE 145 THR 146 0.0038

THR 146 ALA 147 0.0220

ALA 147 LEU 148 -0.0039

LEU 148 ASN 149 -0.0098

ASN 149 SER 150 0.0097

SER 150 GLU 151 0.0091

GLU 151 SER 152 0.0038

SER 152 ASN 153 0.0314

ASN 153 PHE 154 0.0401

PHE 154 ALA 155 0.0269

ALA 155 ARG 156 0.0776

ARG 156 ALA 157 0.0290

ALA 157 TYR 158 0.1234

TYR 158 ALA 159 0.1461

ALA 159 GLU 160 0.0823

GLU 160 GLY 161 0.0151

GLY 161 ILE 162 0.0527

ILE 162 ASN 163 0.0412

ASN 163 ARG 164 0.0884

ARG 164 THR 165 0.0599

THR 165 LYS 166 0.0407

LYS 166 TYR 167 0.0640

TYR 167 TRP 168 0.0256

TRP 168 GLU 169 0.0283

GLU 169 PHE 170 0.0179

PHE 170 VAL 171 0.0194

VAL 171 TYR 172 0.0500

TYR 172 GLU 173 0.0066

GLU 173 ASP 174 0.0662

ASP 174 ALA 175 0.0143

ALA 175 MET 176 0.0079

MET 176 ASP 177 -0.0055

ASP 177 LEU 178 -0.0050

LEU 178 ILE 179 0.0289

ILE 179 ALA 180 0.0359

ALA 180 LYS 181 0.0012

LYS 181 LEU 182 0.0702

LEU 182 PRO 183 -0.0234

PRO 183 CYS 184 0.0613

CYS 184 VAL 185 -0.0122

VAL 185 ALA 186 0.1026

ALA 186 ALA 187 0.0259

ALA 187 LYS 188 0.0008

LYS 188 ILE 189 0.0378

ILE 189 TYR 190 0.0419

TYR 190 ARG 191 0.0846

ARG 191 ASN 192 -0.0211

ASN 192 LEU 193 0.0079

LEU 193 TYR 194 0.0337

TYR 194 ARG 195 0.0889

ARG 195 ALA 196 -0.0366

ALA 196 GLY 197 -0.0225

GLY 197 SER 198 -0.0492

SER 198 SER 199 0.0315

SER 199 ILE 200 -0.0033

ILE 200 GLY 201 0.0199

GLY 201 ALA 202 -0.0045

ALA 202 ILE 203 0.0183

ILE 203 ASP 204 0.0006

ASP 204 SER 205 0.0181

SER 205 LYS 206 0.0176

LYS 206 LEU 207 0.0107

LEU 207 ASP 208 0.0226

ASP 208 TRP 209 -0.0253

TRP 209 SER 210 -0.0191

SER 210 HIS 211 0.0359

HIS 211 ASN 212 0.0169

ASN 212 PHE 213 0.0025

PHE 213 THR 214 -0.0049

THR 214 ASN 215 -0.0377

ASN 215 MET 216 0.0333

MET 216 LEU 217 0.0282

LEU 217 GLY 218 0.0196

GLY 218 TYR 219 -0.0263

TYR 219 THR 220 0.1154

THR 220 ASP 221 0.0855

ASP 221 PRO 222 0.0457

PRO 222 GLN 223 -0.0615

GLN 223 PHE 224 0.0457

PHE 224 THR 225 0.1132

THR 225 GLU 226 0.0108

GLU 226 LEU 227 0.0444

LEU 227 MET 228 -0.0898

MET 228 ARG 229 0.0345

ARG 229 LEU 230 -0.0513

LEU 230 TYR 231 0.0234

TYR 231 LEU 232 -0.0001

LEU 232 THR 233 0.0295

THR 233 ILE 234 -0.0698

ILE 234 HIS 235 -0.0138

HIS 235 SER 236 -0.0008

SER 236 ASP 237 0.0176

ASP 237 HIS 238 0.0056

HIS 238 GLU 239 0.0062

GLU 239 GLY 240 0.0122

GLY 240 GLY 241 0.1810

GLY 241 ASN 242 -0.2002

ASN 242 VAL 243 0.1296

VAL 243 SER 244 0.0433

SER 244 ALA 245 -0.0101

ALA 245 HIS 246 -0.0112

HIS 246 THR 247 -0.0063

THR 247 SER 248 0.0007

SER 248 HIS 249 -0.0011

HIS 249 LEU 250 -0.0115

LEU 250 VAL 251 0.0295

VAL 251 GLY 252 -0.0112

GLY 252 SER 253 -0.0212

SER 253 ALA 254 0.0276

ALA 254 LEU 255 0.1403

LEU 255 SER 256 -0.0610

SER 256 ASP 257 -0.0055

ASP 257 PRO 258 0.0143

PRO 258 TYR 259 -0.0064

TYR 259 LEU 260 -0.0051

LEU 260 SER 261 0.0090

SER 261 PHE 262 -0.0161

PHE 262 ALA 263 0.0004

ALA 263 ALA 264 -0.0251

ALA 264 ALA 265 0.0061

ALA 265 MET 266 -0.0042

MET 266 ASN 267 -0.0586

ASN 267 GLY 268 0.0553

GLY 268 LEU 269 -0.0741

LEU 269 ALA 270 0.0202

ALA 270 GLY 271 0.0447

GLY 271 PRO 272 0.0527

PRO 272 LEU 273 0.0021

LEU 273 HIS 274 0.0847

HIS 274 GLY 275 0.0337

GLY 275 LEU 276 -0.0621

LEU 276 ALA 277 0.1506

ALA 277 ASN 278 0.0283

ASN 278 GLN 279 -0.0164

GLN 279 GLU 280 0.1123

GLU 280 VAL 281 -0.0631

VAL 281 LEU 282 0.1583

LEU 282 LEU 283 -0.0885

LEU 283 TRP 284 0.0381

TRP 284 LEU 285 0.1778

LEU 285 SER 286 0.1642

SER 286 GLN 287 0.2976

GLN 287 LEU 288 0.2933

LEU 288 GLN 289 0.4247

GLN 289 LYS 290 0.3987

LYS 290 ASP 291 0.0671

ASP 291 ASP 295 0.3499

ASP 295 ALA 296 0.3076

ALA 296 SER 297 0.4487

SER 297 ASP 298 0.1762

ASP 298 GLU 299 0.3037

GLU 299 LYS 300 0.3458

LYS 300 LEU 301 0.1744

LEU 301 ARG 302 0.3922

ARG 302 ASP 303 0.2426

ASP 303 TYR 304 0.3568

TYR 304 ILE 305 -0.0854

ILE 305 TRP 306 0.3847

TRP 306 ASN 307 0.3346

ASN 307 THR 308 0.2508

THR 308 LEU 309 0.3257

LEU 309 ASN 310 0.6920

ASN 310 SER 311 0.6864

SER 311 GLY 312 0.3981

GLY 312 ARG 313 0.8031

ARG 313 VAL 314 0.7485

VAL 314 VAL 315 0.4137

VAL 315 PRO 316 0.7794

PRO 316 GLY 317 0.1883

GLY 317 TYR 318 0.3635

TYR 318 GLY 319 0.1216

GLY 319 HIS 320 0.1135

HIS 320 ALA 321 0.0335

ALA 321 VAL 322 -0.0103

VAL 322 LEU 323 0.0139

LEU 323 ARG 324 0.0666

ARG 324 LYS 325 0.0802

LYS 325 THR 326 0.0202

THR 326 ASP 327 -0.0240

ASP 327 PRO 328 -0.0939

PRO 328 ARG 329 0.0086

ARG 329 TYR 330 -0.0549

TYR 330 THR 331 0.0195

THR 331 CYS 332 -0.1772

CYS 332 GLN 333 0.0467

GLN 333 ARG 334 -0.1150

ARG 334 GLU 335 -0.1037

GLU 335 PHE 336 -0.0782

PHE 336 ALA 337 -0.0307

ALA 337 LEU 338 0.0273

LEU 338 LYS 339 -0.1125

LYS 339 HIS 340 -0.0900

HIS 340 LEU 341 -0.0123

LEU 341 PRO 342 -0.0438

PRO 342 SER 343 0.0612

SER 343 ASP 344 -0.0381

ASP 344 PRO 345 0.0925

PRO 345 MET 346 -0.0341

MET 346 PHE 347 0.0786

PHE 347 LYS 348 0.0326

LYS 348 LEU 349 -0.0240

LEU 349 VAL 350 -0.0786

VAL 350 ALA 351 0.1736

ALA 351 GLN 352 -0.1557

GLN 352 LEU 353 0.1364

LEU 353 TYR 354 0.1398

TYR 354 LYS 355 0.2901

LYS 355 ILE 356 0.3144

ILE 356 VAL 357 0.1862

VAL 357 PRO 358 -0.0629

PRO 358 ASN 359 0.4650

ASN 359 VAL 360 0.4033

VAL 360 LEU 361 0.3815

LEU 361 LEU 362 0.4636

LEU 362 GLU 363 0.4525

GLU 363 GLN 364 0.4942

GLN 364 GLY 365 0.1335

GLY 365 LYS 366 0.5265

LYS 366 ALA 367 0.7732

ALA 367 LYS 368 0.2898

LYS 368 ASN 369 0.0916

ASN 369 PRO 370 0.1122

PRO 370 TRP 371 0.1108

TRP 371 PRO 372 0.0295

PRO 372 ASN 373 -0.0144

ASN 373 VAL 374 0.0006

VAL 374 ASP 375 0.0125

ASP 375 ALA 376 0.0193

ALA 376 HIS 377 0.0312

HIS 377 SER 378 -0.0283

SER 378 GLY 379 0.0344

GLY 379 VAL 380 -0.0654

VAL 380 LEU 381 0.0375

LEU 381 LEU 382 -0.0121

LEU 382 GLN 383 0.0773

GLN 383 TYR 384 -0.0505

TYR 384 TYR 385 0.0836

TYR 385 GLY 386 0.0272

GLY 386 MET 387 -0.0740

MET 387 THR 388 0.2080

THR 388 GLU 389 0.0082

GLU 389 MET 390 0.1032

MET 390 ASN 391 0.0227

ASN 391 TYR 392 0.2323

TYR 392 TYR 393 0.0715

TYR 393 THR 394 -0.1295

THR 394 VAL 395 0.1069

VAL 395 LEU 396 -0.0589

LEU 396 PHE 397 0.0098

PHE 397 GLY 398 -0.0030

GLY 398 VAL 399 -0.0006

VAL 399 SER 400 -0.0266

SER 400 ARG 401 -0.0185

ARG 401 ALA 402 0.0088

ALA 402 LEU 403 0.0269

LEU 403 GLY 404 -0.0330

GLY 404 VAL 405 -0.0007

VAL 405 LEU 406 0.0109

LEU 406 ALA 407 0.0131

ALA 407 GLN 408 -0.0067

GLN 408 LEU 409 -0.0085

LEU 409 ILE 410 0.0218

ILE 410 TRP 411 0.0241

TRP 411 SER 412 0.0110

SER 412 ARG 413 0.0603

ARG 413 ALA 414 -0.0141

ALA 414 LEU 415 0.0971

LEU 415 GLY 416 0.0627

GLY 416 PHE 417 0.0323

PHE 417 PRO 418 0.1912

PRO 418 LEU 419 0.0199

LEU 419 GLU 420 0.0898

GLU 420 ARG 421 0.0129

ARG 421 PRO 422 0.9398

PRO 422 LYS 423 0.5661

LYS 423 SER 424 0.6050

SER 424 MET 425 0.3329

MET 425 SER 426 0.2048

SER 426 THR 427 0.1932

THR 427 ALA 428 0.2207

ALA 428 GLY 429 0.0308

GLY 429 LEU 430 0.4351

LEU 430 GLU 431 0.1015

GLU 431 LYS 432 0.3583

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.

*** close cutoff 10 melek ***

CA strain for 260522120726406031

--- normal mode 15 ---

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

* close cutoff 10 melek *