Should you encounter any unexpected behaviour,
please let us know.

* *

CA strain for 2405291050273995722

--- 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
PRO 5 PRO 6 -0.0001

PRO 6 LEU 7 -0.0001

LEU 7 THR 8 0.0951

THR 8 ALA 9 0.0001

ALA 9 HIS 10 0.0001

HIS 10 ALA 11 0.0491

ALA 11 THR 12 0.0002

THR 12 ALA 13 -0.0002

ALA 13 ALA 14 0.1120

ALA 14 ALA 15 -0.0001

ALA 15 ILE 16 0.0002

ILE 16 ARG 17 -0.0068

ARG 17 ALA 18 0.0001

ALA 18 GLY 19 -0.0002

GLY 19 THR 20 -0.0251

THR 20 THR 21 -0.0000

THR 21 THR 22 0.0001

THR 22 ALA 23 0.0710

ALA 23 ARG 24 0.0004

ARG 24 GLU 25 0.0002

GLU 25 GLN 26 -0.0130

GLN 26 ALA 27 0.0001

ALA 27 LEU 28 -0.0000

LEU 28 ALA 29 -0.0140

ALA 29 ALA 30 0.0001

ALA 30 ILE 31 -0.0002

ILE 31 ALA 32 0.0124

ALA 32 ARG 33 0.0002

ARG 33 ILE 34 -0.0002

ILE 34 GLU 35 -0.0065

GLU 35 THR 36 -0.0000

THR 36 LEU 37 -0.0002

LEU 37 ASP 38 -0.0610

ASP 38 PRO 39 -0.0002

PRO 39 GLU 40 -0.0001

GLU 40 ILE 41 0.0309

ILE 41 ASN 42 0.0001

ASN 42 ALA 43 0.0002

ALA 43 VAL 44 0.0176

VAL 44 PRO 45 -0.0003

PRO 45 VAL 46 0.0001

VAL 46 ARG 47 0.0658

ARG 47 ASP 48 -0.0001

ASP 48 PHE 49 -0.0004

PHE 49 ASP 50 0.0671

ASP 50 ARG 51 0.0003

ARG 51 ALA 52 -0.0003

ALA 52 LEU 53 0.0649

LEU 53 ALA 54 0.0001

ALA 54 ALA 55 0.0002

ALA 55 ALA 56 0.0108

ALA 56 ASP 57 0.0005

ASP 57 ALA 58 0.0002

ALA 58 ALA 59 -0.0480

ALA 59 ASP 60 0.0001

ASP 60 ALA 61 -0.0002

ALA 61 ARG 62 -0.0223

ARG 62 LEU 63 0.0002

LEU 63 ALA 64 -0.0001

ALA 64 ALA 65 -0.1279

ALA 65 GLY 66 -0.0000

GLY 66 ASP 67 -0.0003

ASP 67 THR 68 -0.1221

THR 68 ALA 69 -0.0002

ALA 69 PRO 70 0.0004

PRO 70 LEU 71 -0.0581

LEU 71 LEU 72 -0.0000

LEU 72 GLY 73 -0.0000

GLY 73 VAL 74 -0.0986

VAL 74 PRO 75 -0.0002

PRO 75 MET 76 0.0001

MET 76 THR 77 0.0079

THR 77 VAL 78 -0.0000

VAL 78 LYS 79 -0.0001

LYS 79 GLU 80 0.0034

GLU 80 ALA 81 0.0000

ALA 81 PHE 82 -0.0002

PHE 82 ASP 83 -0.0382

ASP 83 ILE 84 -0.0001

ILE 84 ALA 85 -0.0002

ALA 85 GLY 86 -0.0340

GLY 86 LEU 87 0.0001

LEU 87 PRO 88 -0.0001

PRO 88 THR 89 0.0227

THR 89 HIS 90 -0.0002

HIS 90 TRP 91 0.0002

TRP 91 GLY 92 0.0065

GLY 92 PHE 93 -0.0003

PHE 93 ALA 94 0.0001

ALA 94 GLU 95 0.0148

GLU 95 HIS 96 -0.0002

HIS 96 ARG 97 -0.0003

ARG 97 ASN 98 -0.0028

ASN 98 ASN 99 0.0004

ASN 99 VAL 100 -0.0003

VAL 100 ALA 101 0.0377

ALA 101 THR 102 0.0000

THR 102 THR 103 -0.0003

THR 103 ASP 104 0.0211

ASP 104 ALA 105 -0.0004

ALA 105 HIS 106 0.0001

HIS 106 ALA 107 -0.0419

ALA 107 VAL 108 0.0000

VAL 108 ALA 109 0.0004

ALA 109 ARG 110 -0.0074

ARG 110 LEU 111 -0.0000

LEU 111 LYS 112 -0.0002

LYS 112 ALA 113 0.0344

ALA 113 ALA 114 -0.0000

ALA 114 GLY 115 -0.0000

GLY 115 ALA 116 0.0042

ALA 116 ILE 117 0.0001

ILE 117 ILE 118 -0.0003

ILE 118 LEU 119 0.0211

LEU 119 GLY 120 -0.0000

GLY 120 LYS 121 -0.0001

LYS 121 SER 122 0.0268

SER 122 ASN 123 -0.0004

ASN 123 VAL 124 0.0001

VAL 124 PRO 125 0.0587

PRO 125 LYS 126 -0.0001

LYS 126 GLY 127 0.0001

GLY 127 LEU 128 0.0156

LEU 128 GLY 129 0.0001

GLY 129 ASP 130 0.0002

ASP 130 TRP 131 -0.0050

TRP 131 GLN 132 0.0002

GLN 132 SER 133 -0.0002

SER 133 VAL 134 0.0226

VAL 134 ASN 135 0.0005

ASN 135 SER 136 -0.0003

SER 136 ILE 137 0.0594

ILE 137 HIS 138 0.0002

HIS 138 GLY 139 0.0002

GLY 139 ARG 140 0.0503

ARG 140 THR 141 0.0000

THR 141 ASN 142 -0.0003

ASN 142 HIS 143 0.0527

HIS 143 PRO 144 -0.0001

PRO 144 LEU 145 0.0002

LEU 145 ASP 146 -0.0645

ASP 146 PRO 147 0.0005

PRO 147 ALA 148 -0.0001

ALA 148 ARG 149 0.0225

ARG 149 THR 150 0.0001

THR 150 SER 151 0.0005

SER 151 GLY 152 -0.0125

GLY 152 GLY 153 -0.0004

GLY 153 SER 154 0.0001

SER 154 SER 155 -0.0284

SER 155 GLY 156 0.0001

GLY 156 GLY 157 0.0001

GLY 157 GLY 158 0.0178

GLY 158 ALA 159 0.0003

ALA 159 ALA 160 0.0001

ALA 160 ALA 161 -0.0464

ALA 161 VAL 162 -0.0000

VAL 162 ALA 163 -0.0002

ALA 163 ALA 164 0.0380

ALA 164 GLY 165 -0.0003

GLY 165 MET 166 0.0003

MET 166 VAL 167 0.0077

VAL 167 PRO 168 0.0003

PRO 168 ILE 169 0.0001

ILE 169 GLU 170 -0.0092

GLU 170 LEU 171 0.0000

LEU 171 GLY 172 0.0003

GLY 172 SER 173 -0.0481

SER 173 ASP 174 -0.0003

ASP 174 VAL 175 0.0004

VAL 175 GLY 176 0.0286

GLY 176 GLY 177 0.0001

GLY 177 SER 178 -0.0002

SER 178 ILE 179 -0.0020

ILE 179 ARG 180 0.0002

ARG 180 VAL 181 -0.0001

VAL 181 PRO 182 -0.0119

PRO 182 ALA 183 0.0002

ALA 183 HIS 184 -0.0002

HIS 184 PHE 185 0.0288

PHE 185 CYS 186 -0.0002

CYS 186 GLY 187 -0.0003

GLY 187 ILE 188 -0.0895

ILE 188 TRP 189 -0.0001

TRP 189 GLY 190 0.0001

GLY 190 HIS 191 -0.0185

HIS 191 LYS 192 0.0003

LYS 192 PRO 193 0.0000

PRO 193 SER 194 -0.0312

SER 194 TRP 195 -0.0002

TRP 195 ASN 196 -0.0002

ASN 196 ALA 197 -0.0581

ALA 197 ILE 198 0.0001

ILE 198 SER 199 -0.0000

SER 199 SER 200 0.0456

SER 200 ASP 201 -0.0002

ASP 201 GLY 202 -0.0001

GLY 202 HIS 203 0.0517

HIS 203 ARG 204 -0.0002

ARG 204 TYR 205 -0.0000

TYR 205 PRO 206 -0.0251

PRO 206 GLY 207 -0.0003

GLY 207 THR 208 -0.0004

THR 208 ASP 209 0.0997

ASP 209 GLY 210 0.0002

GLY 210 THR 211 -0.0002

THR 211 GLU 212 -0.0471

GLU 212 THR 213 -0.0002

THR 213 VAL 214 0.0002

VAL 214 LEU 215 -0.3199

LEU 215 GLY 216 -0.0001

GLY 216 VAL 217 -0.0000

VAL 217 ILE 218 -0.1509

ILE 218 GLY 219 -0.0002

GLY 219 PRO 220 0.0001

PRO 220 LEU 221 -0.0190

LEU 221 ALA 222 0.0000

ALA 222 ARG 223 0.0001

ARG 223 ASP 224 0.0902

ASP 224 PRO 225 0.0001

PRO 225 GLN 226 -0.0000

GLN 226 ASP 227 -0.0390

ASP 227 LEU 228 0.0000

LEU 228 ALA 229 0.0003

ALA 229 LEU 230 -0.1977

LEU 230 MET 231 -0.0002

MET 231 ILE 232 0.0000

ILE 232 ASP 233 -0.0043

ASP 233 LEU 234 0.0001

LEU 234 LEU 235 -0.0002

LEU 235 ALA 236 0.0256

ALA 236 THR 237 -0.0001

THR 237 LEU 238 -0.0000

LEU 238 PRO 239 -0.0448

PRO 239 LEU 240 0.0002

LEU 240 PRO 241 0.0000

PRO 241 ARG 242 -0.0445

ARG 242 PRO 243 0.0000

PRO 243 ALA 244 -0.0000

ALA 244 ALA 245 -0.0236

ALA 245 ARG 246 -0.0002

ARG 246 THR 247 0.0001

THR 247 ARG 248 -0.0095

ARG 248 ARG 249 -0.0003

ARG 249 VAL 250 -0.0000

VAL 250 LEU 251 -0.0120

LEU 251 VAL 252 -0.0002

VAL 252 LEU 253 0.0003

LEU 253 ALA 254 -0.0421

ALA 254 GLN 255 0.0005

GLN 255 HIS 256 -0.0002

HIS 256 PRO 257 0.0472

PRO 257 GLU 258 -0.0002

GLU 258 THR 259 -0.0002

THR 259 ARG 260 0.2111

ARG 260 THR 261 -0.0001

THR 261 ALA 262 0.0005

ALA 262 HIS 263 0.0517

HIS 263 ALA 264 0.0000

ALA 264 VAL 265 -0.0001

VAL 265 VAL 266 0.0031

VAL 266 GLU 267 -0.0003

GLU 267 GLY 268 -0.0002

GLY 268 VAL 269 -0.0135

VAL 269 GLU 270 0.0001

GLU 270 ARG 271 0.0004

ARG 271 ALA 272 -0.0306

ALA 272 ALA 273 0.0001

ALA 273 ALA 274 -0.0001

ALA 274 ALA 275 -0.0203

ALA 275 LEU 276 0.0000

LEU 276 ALA 277 0.0002

ALA 277 ARG 278 0.0089

ARG 278 ALA 279 -0.0001

ALA 279 GLY 280 0.0001

GLY 280 VAL 281 0.0155

VAL 281 GLU 282 0.0001

GLU 282 VAL 283 -0.0001

VAL 283 VAL 284 0.0330

VAL 284 ARG 285 0.0001

ARG 285 HIS 286 -0.0001

HIS 286 SER 287 0.0178

SER 287 ASP 288 0.0003

ASP 288 LEU 289 0.0001

LEU 289 LEU 290 -0.0504

LEU 290 PRO 291 -0.0001

PRO 291 ASP 292 0.0001

ASP 292 LEU 293 0.0098

LEU 293 SER 294 0.0001

SER 294 ARG 295 -0.0001

ARG 295 GLN 296 -0.1134

GLN 296 HIS 297 -0.0002

HIS 297 SER 298 -0.0002

SER 298 ALA 299 0.3020

ALA 299 TYR 300 0.0002

TYR 300 GLY 301 -0.0003

GLY 301 ASP 302 0.3008

ASP 302 LEU 303 -0.0001

LEU 303 LEU 304 -0.0006

LEU 304 ASN 305 -0.1049

ASN 305 VAL 306 -0.0002

VAL 306 THR 307 -0.0000

THR 307 PHE 308 -0.0631

PHE 308 ALA 309 -0.0001

ALA 309 ARG 310 -0.0001

ARG 310 SER 311 0.2068

SER 311 ASN 312 0.0000

ASN 312 PRO 313 -0.0001

PRO 313 ALA 314 0.0186

ALA 314 LEU 315 0.0002

LEU 315 HIS 316 -0.0002

HIS 316 HIS 317 -0.0921

HIS 317 THR 318 -0.0001

THR 318 LEU 319 0.0002

LEU 319 PRO 320 -0.1157

PRO 320 SER 321 -0.0003

SER 321 LEU 322 -0.0000

LEU 322 LEU 323 0.1264

LEU 323 LYS 324 -0.0002

LYS 324 TRP 325 -0.0002

TRP 325 LEU 326 -0.1223

LEU 326 SER 327 0.0000

SER 327 MET 328 -0.0002

MET 328 LEU 329 -0.0323

LEU 329 ASP 330 -0.0003

ASP 330 ALA 331 -0.0000

ALA 331 GLN 332 -0.0048

GLN 332 ALA 333 0.0001

ALA 333 ARG 334 0.0001

ARG 334 SER 335 0.0845

SER 335 THR 336 0.0000

THR 336 ARG 337 -0.0001

ARG 337 ALA 338 0.0179

ALA 338 TRP 339 0.0001

TRP 339 GLY 340 -0.0001

GLY 340 ALA 341 0.0021

ALA 341 LEU 342 0.0001

LEU 342 PHE 343 0.0002

PHE 343 GLY 344 -0.0084

GLY 344 GLU 345 -0.0003

GLU 345 PHE 346 -0.0001

PHE 346 ASP 347 -0.0035

ASP 347 ALA 348 -0.0000

ALA 348 VAL 349 -0.0002

VAL 349 ILE 350 0.0320

ILE 350 ALA 351 0.0000

ALA 351 PRO 352 0.0001

PRO 352 PRO 353 -0.0058

PRO 353 ALA 354 0.0000

ALA 354 ALA 355 0.0002

ALA 355 THR 356 0.0375

THR 356 GLN 357 0.0001

GLN 357 ALA 358 -0.0001

ALA 358 PHE 359 -0.0221

PHE 359 ALA 360 -0.0001

ALA 360 HIS 361 -0.0002

HIS 361 ASP 362 -0.0509

ASP 362 HIS 363 -0.0002

HIS 363 SER 364 0.0001

SER 364 PRO 365 -0.0273

PRO 365 LEU 366 0.0001

LEU 366 ALA 367 -0.0002

ALA 367 ASP 368 0.0383

ASP 368 ARG 369 -0.0000

ARG 369 THR 370 -0.0003

THR 370 LEU 371 -0.0272

LEU 371 ALA 372 0.0002

ALA 372 ILE 373 -0.0001

ILE 373 ASP 374 0.0310

ASP 374 GLY 375 0.0002

GLY 375 THR 376 0.0001

THR 376 PRO 377 0.0327

PRO 377 GLY 378 0.0003

GLY 378 PRO 379 -0.0002

PRO 379 TYR 380 0.0369

TYR 380 ASP 381 -0.0003

ASP 381 ALA 382 -0.0004

ALA 382 HIS 383 -0.0162

HIS 383 LEU 384 0.0001

LEU 384 ALA 385 -0.0003

ALA 385 TRP 386 0.0118

TRP 386 ALA 387 -0.0003

ALA 387 GLY 388 -0.0003

GLY 388 LEU 389 -0.0242

LEU 389 ALA 390 0.0001

ALA 390 THR 391 -0.0000

THR 391 TYR 392 0.0350

TYR 392 PRO 393 0.0003

PRO 393 GLY 394 -0.0003

GLY 394 LEU 395 -0.1317

LEU 395 PRO 396 0.0000

PRO 396 ALA 397 -0.0001

ALA 397 THR 398 -0.0563

THR 398 CYS 399 -0.0001

CYS 399 MET 400 -0.0002

MET 400 PRO 401 -0.0166

PRO 401 VAL 402 0.0000

VAL 402 GLY 403 0.0000

GLY 403 LEU 404 -0.0372

LEU 404 ILE 405 -0.0001

ILE 405 ASP 406 0.0000

ASP 406 GLY 407 -0.0020

GLY 407 LEU 408 0.0004

LEU 408 PRO 409 0.0000

PRO 409 THR 410 0.0218

THR 410 GLY 411 -0.0002

GLY 411 VAL 412 0.0000

VAL 412 GLN 413 0.0349

GLN 413 VAL 414 -0.0001

VAL 414 ILE 415 -0.0001

ILE 415 THR 416 0.0070

THR 416 GLU 417 0.0000

GLU 417 LEU 418 0.0001

LEU 418 HIS 419 -0.0041

HIS 419 GLN 420 0.0000

GLN 420 ASP 421 0.0002

ASP 421 HIS 422 -0.0058

HIS 422 ARG 423 0.0000

ARG 423 ALA 424 -0.0005

ALA 424 ILE 425 0.0244

ILE 425 GLU 426 -0.0002

GLU 426 ILE 427 -0.0000

ILE 427 ALA 428 0.0413

ALA 428 ALA 429 -0.0003

ALA 429 LEU 430 0.0002

LEU 430 ILE 431 -0.0126

ILE 431 ALA 432 0.0001

ALA 432 GLN 433 -0.0001

GLN 433 HIS 434 -0.0533

HIS 434 LEU 435 0.0001

LEU 435 SER 436 0.0001

SER 436 PRO 437 0.0909

PRO 437 SER 438 -0.0002

SER 438 PRO 439 -0.0000

PRO 439 GLN 440 -0.0217

GLN 440 GLY 441 -0.0001

GLY 441 ALA 442 -0.0003

ALA 442 ILE 443 -0.0857

ILE 443 ALA 444 0.0002

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** ***

CA strain for 2405291050273995722

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.

* *