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

* vps4b *

CA strain for 2609092319512946827

--- normal mode 8 ---

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 123 ILE 124 0.0001

ILE 124 VAL 125 0.0168

VAL 125 ILE 126 0.0001

ILE 126 GLU 127 0.0139

GLU 127 ARG 128 0.0003

ARG 128 PRO 129 0.0091

PRO 129 ASN 130 0.0002

ASN 130 VAL 131 0.0084

VAL 131 LYS 132 0.0001

LYS 132 TRP 133 0.0139

TRP 133 SER 134 0.0000

SER 134 ASP 135 -0.0200

ASP 135 VAL 136 0.0000

VAL 136 ALA 137 0.0785

ALA 137 GLY 138 0.0001

GLY 138 LEU 139 -0.0142

LEU 139 GLU 140 0.0002

GLU 140 GLY 141 -0.0242

GLY 141 ALA 142 0.0005

ALA 142 LYS 143 0.0092

LYS 143 GLU 144 -0.0003

GLU 144 ALA 145 -0.0110

ALA 145 LEU 146 -0.0001

LEU 146 LYS 147 -0.0003

LYS 147 GLU 148 -0.0003

GLU 148 ALA 149 -0.0061

ALA 149 VAL 150 -0.0001

VAL 150 ILE 151 -0.0008

ILE 151 LEU 152 0.0002

LEU 152 PRO 153 -0.0042

PRO 153 ILE 154 0.0001

ILE 154 LYS 155 -0.0004

LYS 155 PHE 156 -0.0001

PHE 156 PRO 157 0.0012

PRO 157 HIS 158 0.0001

HIS 158 LEU 159 0.0000

LEU 159 PHE 160 -0.0003

PHE 160 THR 161 0.0005

THR 161 GLY 162 0.0001

GLY 162 LYS 163 -0.0066

LYS 163 ARG 164 0.0002

ARG 164 THR 165 -0.0050

THR 165 PRO 166 0.0001

PRO 166 TRP 167 0.0008

TRP 167 ARG 168 0.0001

ARG 168 GLY 169 -0.0025

GLY 169 ILE 170 0.0003

ILE 170 LEU 171 0.0019

LEU 171 LEU 172 -0.0004

LEU 172 PHE 173 -0.0111

PHE 173 GLY 174 0.0004

GLY 174 PRO 175 0.0128

PRO 175 PRO 176 0.0003

PRO 176 GLY 177 0.0233

GLY 177 THR 178 0.0000

THR 178 GLY 179 -0.0520

GLY 179 LYS 180 0.0001

LYS 180 SER 181 -0.0248

SER 181 TYR 182 -0.0001

TYR 182 LEU 183 0.0008

LEU 183 ALA 184 0.0000

ALA 184 LYS 185 0.0015

LYS 185 ALA 186 -0.0002

ALA 186 VAL 187 -0.0035

VAL 187 ALA 188 -0.0000

ALA 188 THR 189 0.0062

THR 189 GLU 190 -0.0001

GLU 190 ALA 191 -0.0048

ALA 191 ASN 192 0.0004

ASN 192 ASN 193 -0.0009

ASN 193 SER 194 -0.0000

SER 194 THR 195 0.0019

THR 195 PHE 196 -0.0004

PHE 196 PHE 197 0.0110

PHE 197 SER 198 0.0000

SER 198 ILE 199 0.0082

ILE 199 SER 200 -0.0000

SER 200 SER 201 -0.0007

SER 201 SER 202 -0.0002

SER 202 ASP 203 0.0094

ASP 203 LEU 204 -0.0001

LEU 204 VAL 205 -0.0032

VAL 205 SER 206 0.0002

SER 206 LYS 207 0.0005

LYS 207 TRP 208 0.0005

TRP 208 LEU 209 -0.0002

LEU 209 GLY 210 -0.0001

GLY 210 GLU 211 -0.0096

GLU 211 SER 212 -0.0001

SER 212 GLU 213 -0.0030

GLU 213 LYS 214 -0.0001

LYS 214 LEU 215 0.0064

LEU 215 VAL 216 0.0001

VAL 216 LYS 217 -0.0005

LYS 217 ASN 218 -0.0001

ASN 218 LEU 219 -0.0008

LEU 219 PHE 220 0.0001

PHE 220 GLN 221 -0.0010

GLN 221 LEU 222 0.0002

LEU 222 ALA 223 -0.0010

ALA 223 ARG 224 -0.0001

ARG 224 GLU 225 0.0014

GLU 225 ASN 226 -0.0003

ASN 226 LYS 227 0.0009

LYS 227 PRO 228 -0.0003

PRO 228 SER 229 -0.0016

SER 229 ILE 230 0.0001

ILE 230 ILE 231 -0.0005

ILE 231 PHE 232 -0.0001

PHE 232 ILE 233 0.0035

ILE 233 ASP 234 -0.0003

ASP 234 GLU 235 0.0018

GLU 235 ILE 236 -0.0001

ILE 236 ASP 237 -0.0024

ASP 237 SER 238 -0.0000

SER 238 LEU 239 -0.0077

LEU 239 CYS 240 0.0002

CYS 240 GLY 241 -0.0033

GLY 241 SER 242 0.0002

SER 242 ARG 243 0.0044

ARG 243 SER 244 -0.0000

SER 244 GLU 245 -0.0097

GLU 245 ASN 246 0.0003

ASN 246 GLU 247 -0.0013

GLU 247 SER 248 0.0002

SER 248 GLU 249 0.0006

GLU 249 ALA 250 0.0003

ALA 250 ALA 251 -0.0012

ALA 251 ARG 252 0.0001

ARG 252 ARG 253 0.0022

ARG 253 ILE 254 0.0001

ILE 254 LYS 255 -0.0033

LYS 255 THR 256 0.0001

THR 256 GLU 257 0.0047

GLU 257 PHE 258 -0.0001

PHE 258 LEU 259 0.0016

LEU 259 VAL 260 -0.0000

VAL 260 GLN 261 -0.0002

GLN 261 MET 262 0.0000

MET 262 GLN 263 -0.0013

GLN 263 GLY 264 0.0001

GLY 264 VAL 265 0.0021

VAL 265 GLY 266 -0.0004

GLY 266 VAL 267 -0.0002

VAL 267 ASP 268 0.0002

ASP 268 ASN 269 -0.0009

ASN 269 ASP 270 -0.0004

ASP 270 GLY 271 -0.0034

GLY 271 ILE 272 -0.0000

ILE 272 LEU 273 0.0010

LEU 273 VAL 274 -0.0000

VAL 274 LEU 275 -0.0092

LEU 275 GLY 276 -0.0002

GLY 276 ALA 277 -0.0156

ALA 277 THR 278 0.0000

THR 278 ASN 279 -0.0159

ASN 279 ILE 280 -0.0002

ILE 280 PRO 281 0.0097

PRO 281 TRP 282 -0.0001

TRP 282 VAL 283 -0.0126

VAL 283 LEU 284 0.0001

LEU 284 ASP 285 0.0021

ASP 285 SER 286 0.0003

SER 286 ALA 287 0.0060

ALA 287 ILE 288 -0.0001

ILE 288 ARG 289 -0.0006

ARG 289 ARG 290 -0.0004

ARG 290 ARG 291 0.0165

ARG 291 PHE 292 -0.0001

PHE 292 GLU 293 -0.0021

GLU 293 LYS 294 -0.0001

LYS 294 ARG 295 0.0205

ARG 295 ILE 296 -0.0001

ILE 296 TYR 297 0.0204

TYR 297 ILE 298 0.0000

ILE 298 PRO 299 0.0069

PRO 299 LEU 300 0.0000

LEU 300 PRO 301 -0.0553

PRO 301 GLU 302 -0.0001

GLU 302 PRO 303 0.0121

PRO 303 HIS 304 -0.0000

HIS 304 ALA 305 0.0357

ALA 305 ARG 306 0.0000

ARG 306 ALA 307 -0.0133

ALA 307 ALA 308 -0.0001

ALA 308 MET 309 0.0259

MET 309 PHE 310 -0.0001

PHE 310 LYS 311 0.0021

LYS 311 LEU 312 0.0000

LEU 312 HIS 313 -0.0345

HIS 313 LEU 314 0.0002

LEU 314 GLY 315 0.0257

GLY 315 THR 316 0.0003

THR 316 THR 317 -0.0400

THR 317 GLN 318 0.0001

GLN 318 ASN 319 -0.0838

ASN 319 SER 320 -0.0002

SER 320 LEU 321 -0.0392

LEU 321 THR 322 -0.0004

THR 322 GLU 323 -0.0106

GLU 323 ALA 324 0.0001

ALA 324 ASP 325 0.0155

ASP 325 PHE 326 0.0002

PHE 326 ARG 327 -0.0082

ARG 327 GLU 328 -0.0000

GLU 328 LEU 329 0.0025

LEU 329 GLY 330 -0.0002

GLY 330 ARG 331 0.0189

ARG 331 LYS 332 -0.0002

LYS 332 THR 333 -0.0333

THR 333 ASP 334 0.0002

ASP 334 GLY 335 -0.0676

GLY 335 TYR 336 -0.0000

TYR 336 SER 337 -0.0255

SER 337 GLY 338 0.0001

GLY 338 ALA 339 0.0076

ALA 339 ASP 340 0.0001

ASP 340 ILE 341 0.0368

ILE 341 SER 342 -0.0001

SER 342 ILE 343 -0.0009

ILE 343 ILE 344 0.0003

ILE 344 VAL 345 0.0063

VAL 345 ARG 346 -0.0000

ARG 346 ASP 347 -0.0305

ASP 347 ALA 348 -0.0002

ALA 348 LEU 349 0.0153

LEU 349 MET 350 -0.0003

MET 350 GLN 351 0.0061

GLN 351 PRO 352 -0.0000

PRO 352 VAL 353 -0.0132

VAL 353 ARG 354 -0.0000

ARG 354 LYS 355 -0.0387

LYS 355 VAL 356 0.0002

VAL 356 GLN 357 0.0253

GLN 357 SER 358 0.0001

SER 358 ALA 359 -0.0540

ALA 359 THR 360 0.0002

THR 360 HIS 361 -0.0065

HIS 361 PHE 362 -0.0000

PHE 362 LYS 363 -0.0087

LYS 363 LYS 364 0.0002

LYS 364 VAL 365 -0.0017

VAL 365 ARG 366 0.0001

ARG 366 GLY 367 0.0030

GLY 367 PRO 368 0.0002

PRO 368 SER 369 -0.0006

SER 369 ARG 370 0.0000

ARG 370 ALA 371 -0.0048

ALA 371 ASP 372 0.0002

ASP 372 PRO 373 -0.0063

PRO 373 ASN 374 0.0002

ASN 374 HIS 375 0.0059

HIS 375 LEU 376 0.0001

LEU 376 VAL 377 0.0195

VAL 377 ASP 378 0.0000

ASP 378 ASP 379 -0.0019

ASP 379 LEU 380 -0.0004

LEU 380 LEU 381 0.0096

LEU 381 THR 382 -0.0001

THR 382 PRO 383 -0.0032

PRO 383 CYS 384 0.0000

CYS 384 SER 385 0.0098

SER 385 PRO 386 -0.0001

PRO 386 GLY 387 -0.0057

GLY 387 ASP 388 0.0002

ASP 388 PRO 389 -0.0013

PRO 389 GLY 390 -0.0000

GLY 390 ALA 391 -0.0025

ALA 391 ILE 392 0.0000

ILE 392 GLU 393 -0.0006

GLU 393 MET 394 -0.0003

MET 394 THR 395 -0.0021

THR 395 TRP 396 -0.0002

TRP 396 MET 397 0.0002

MET 397 ASP 398 -0.0000

ASP 398 VAL 399 -0.0152

VAL 399 PRO 400 -0.0003

PRO 400 GLY 401 -0.0175

GLY 401 ASP 402 0.0001

ASP 402 LYS 403 -0.0011

LYS 403 LEU 404 -0.0002

LEU 404 LEU 405 -0.0414

LEU 405 GLU 406 -0.0002

GLU 406 PRO 407 -0.0111

PRO 407 VAL 408 -0.0000

VAL 408 VAL 409 -0.0073

VAL 409 SER 410 -0.0001

SER 410 MET 411 -0.0025

MET 411 SER 412 0.0000

SER 412 ASP 413 0.0061

ASP 413 MET 414 -0.0002

MET 414 LEU 415 -0.0005

LEU 415 ARG 416 -0.0001

ARG 416 SER 417 -0.0199

SER 417 LEU 418 0.0001

LEU 418 SER 419 0.0154

SER 419 ASN 420 0.0001

ASN 420 THR 421 0.0078

THR 421 LYS 422 -0.0004

LYS 422 PRO 423 0.0189

PRO 423 THR 424 0.0001

THR 424 VAL 425 0.0686

VAL 425 ASN 426 0.0002

ASN 426 GLU 427 0.0299

GLU 427 HIS 428 -0.0001

HIS 428 ASP 429 -0.0068

ASP 429 LEU 430 0.0001

LEU 430 LEU 431 -0.0141

LEU 431 LYS 432 0.0000

LYS 432 LEU 433 -0.0021

LEU 433 LYS 434 -0.0000

LYS 434 LYS 435 -0.0198

LYS 435 PHE 436 0.0004

PHE 436 THR 437 -0.0029

THR 437 GLU 438 -0.0001

GLU 438 ASP 439 -0.0083

ASP 439 PHE 440 -0.0001

PHE 440 GLY 441 -0.0015

GLY 441 GLN 442 0.0001

GLN 442 GLU 443 -0.0007

GLU 443 GLY 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).
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.

*** vps4b ***

CA strain for 2609092319512946827

--- normal mode 8 ---

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

* vps4b *