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

* open cutoff8 melek *

CA strain for 260522120615405517

--- 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 0.0001

SER 2 SER 3 0.0011

SER 3 THR 4 0.0014

THR 4 ASN 5 -0.0014

ASN 5 LEU 6 0.0067

LEU 6 LYS 7 0.0001

LYS 7 ASP 8 0.0038

ASP 8 VAL 9 -0.0185

VAL 9 LEU 10 0.0079

LEU 10 ALA 11 -0.0035

ALA 11 ALA 12 -0.0034

ALA 12 LEU 13 -0.0214

LEU 13 ILE 14 0.0248

ILE 14 PRO 15 0.0249

PRO 15 LYS 16 -0.0009

LYS 16 GLU 17 0.0199

GLU 17 GLN 18 0.0162

GLN 18 ALA 19 0.0122

ALA 19 ARG 20 0.0235

ARG 20 ILE 21 0.0125

ILE 21 LYS 22 0.0281

LYS 22 THR 23 0.0164

THR 23 PHE 24 0.0245

PHE 24 ARG 25 0.0421

ARG 25 GLN 26 0.0397

GLN 26 GLN 27 0.0442

GLN 27 HIS 28 0.0494

HIS 28 GLY 29 0.0126

GLY 29 GLY 30 1.1450

GLY 30 THR 31 0.9157

THR 31 ALA 32 0.6590

ALA 32 LEU 33 0.3889

LEU 33 GLY 34 0.1893

GLY 34 GLN 35 0.3163

GLN 35 ILE 36 0.8503

ILE 36 THR 37 0.6349

THR 37 VAL 38 0.7876

VAL 38 ASP 39 0.8212

ASP 39 MET 40 0.1808

MET 40 SER 41 0.8481

SER 41 TYR 42 0.8232

TYR 42 GLY 43 0.7053

GLY 43 GLY 44 0.4085

GLY 44 MET 45 0.8492

MET 45 ARG 46 0.8500

ARG 46 GLY 47 0.8350

GLY 47 MET 48 0.8520

MET 48 LYS 49 0.6014

LYS 49 GLY 50 1.1507

GLY 50 LEU 51 0.9092

LEU 51 VAL 52 0.2144

VAL 52 TYR 53 0.0083

TYR 53 GLU 54 -0.0004

GLU 54 THR 55 0.0018

THR 55 SER 56 0.0006

SER 56 VAL 57 0.0010

VAL 57 LEU 58 -0.0000

LEU 58 ASP 59 0.0014

ASP 59 PRO 60 0.0009

PRO 60 ASP 61 -0.0003

ASP 61 GLU 62 0.0014

GLU 62 GLY 63 0.0001

GLY 63 ILE 64 -0.0003

ILE 64 ARG 65 0.0012

ARG 65 PHE 66 -0.0002

PHE 66 ARG 67 0.0008

ARG 67 GLY 68 0.0006

GLY 68 PHE 69 0.0011

PHE 69 SER 70 0.0011

SER 70 ILE 71 0.0007

ILE 71 PRO 72 0.0000

PRO 72 GLU 73 0.0011

GLU 73 CYS 74 -0.0005

CYS 74 GLN 75 0.0013

GLN 75 LYS 76 0.0011

LYS 76 LEU 77 -0.0005

LEU 77 LEU 78 -0.0002

LEU 78 PRO 79 0.0024

PRO 79 LYS 80 0.0015

LYS 80 GLY 81 0.0011

GLY 81 GLY 82 0.0007

GLY 82 GLY 84 0.0013

GLY 84 GLY 85 0.0011

GLY 85 GLU 86 0.0003

GLU 86 PRO 87 0.0003

PRO 87 LEU 88 -0.0005

LEU 88 PRO 89 0.0011

PRO 89 GLU 90 0.0017

GLU 90 GLY 91 -0.0004

GLY 91 LEU 92 0.0002

LEU 92 PHE 93 0.0009

PHE 93 TRP 94 0.0033

TRP 94 LEU 95 0.0034

LEU 95 LEU 96 0.0014

LEU 96 VAL 97 0.0032

VAL 97 THR 98 -0.0029

THR 98 GLY 99 -0.0050

GLY 99 GLN 100 -0.0006

GLN 100 ILE 101 -0.0011

ILE 101 PRO 102 -0.0003

PRO 102 THR 103 -0.0001

THR 103 GLY 104 0.0004

GLY 104 ALA 105 0.0058

ALA 105 GLN 106 -0.0022

GLN 106 VAL 107 0.0005

VAL 107 SER 108 -0.0001

SER 108 TRP 109 0.0033

TRP 109 LEU 110 -0.0008

LEU 110 SER 111 0.0007

SER 111 LYS 112 0.0000

LYS 112 GLU 113 0.0008

GLU 113 TRP 114 0.0007

TRP 114 ALA 115 0.0002

ALA 115 LYS 116 0.0003

LYS 116 ARG 117 -0.0001

ARG 117 ALA 118 0.0008

ALA 118 ALA 119 -0.0003

ALA 119 LEU 120 0.0006

LEU 120 PRO 121 0.0003

PRO 121 SER 122 0.0011

SER 122 HIS 123 0.0010

HIS 123 VAL 124 0.0005

VAL 124 VAL 125 0.0010

VAL 125 THR 126 0.0005

THR 126 MET 127 0.0012

MET 127 LEU 128 -0.0001

LEU 128 ASP 129 0.0011

ASP 129 ASN 130 0.0004

ASN 130 PHE 131 0.0012

PHE 131 PRO 132 0.0010

PRO 132 THR 133 0.0004

THR 133 ASN 134 0.0009

ASN 134 LEU 135 0.0013

LEU 135 HIS 136 0.0004

HIS 136 PRO 137 0.0012

PRO 137 MET 138 0.0017

MET 138 SER 139 -0.0003

SER 139 GLN 140 0.0012

GLN 140 LEU 141 0.0006

LEU 141 SER 142 0.0006

SER 142 ALA 143 0.0008

ALA 143 ALA 144 0.0004

ALA 144 ILE 145 0.0005

ILE 145 THR 146 0.0004

THR 146 ALA 147 0.0009

ALA 147 LEU 148 0.0006

LEU 148 ASN 149 0.0005

ASN 149 SER 150 0.0004

SER 150 GLU 151 0.0007

GLU 151 SER 152 0.0006

SER 152 ASN 153 0.0014

ASN 153 PHE 154 0.0012

PHE 154 ALA 155 0.0008

ALA 155 ARG 156 0.0006

ARG 156 ALA 157 0.0010

ALA 157 TYR 158 0.0013

TYR 158 ALA 159 -0.0001

ALA 159 GLU 160 0.0008

GLU 160 GLY 161 0.0009

GLY 161 ILE 162 -0.0000

ILE 162 LEU 163 0.0013

LEU 163 ARG 164 0.0006

ARG 164 THR 165 0.0004

THR 165 LYS 166 0.0009

LYS 166 TYR 167 0.0012

TYR 167 TRP 168 0.0006

TRP 168 GLU 169 0.0021

GLU 169 MET 170 -0.0012

MET 170 VAL 171 -0.0002

VAL 171 TYR 172 0.0005

TYR 172 GLU 173 0.0006

GLU 173 SER 174 0.0008

SER 174 ALA 175 0.0004

ALA 175 MET 176 0.0001

MET 176 ASP 177 0.0011

ASP 177 LEU 178 0.0007

LEU 178 ILE 179 -0.0004

ILE 179 ALA 180 0.0012

ALA 180 LYS 181 0.0012

LYS 181 LEU 182 0.0016

LEU 182 PRO 183 0.0011

PRO 183 CYS 184 0.0003

CYS 184 VAL 185 0.0003

VAL 185 ALA 186 0.0007

ALA 186 ALA 187 0.0012

ALA 187 LYS 188 0.0004

LYS 188 ILE 189 0.0010

ILE 189 TYR 190 0.0002

TYR 190 ARG 191 0.0016

ARG 191 ASN 192 -0.0001

ASN 192 LEU 193 0.0010

LEU 193 TYR 194 0.0004

TYR 194 ARG 195 0.0009

ARG 195 ALA 196 0.0007

ALA 196 GLY 197 0.0007

GLY 197 SER 198 0.0009

SER 198 SER 199 0.0012

SER 199 ILE 200 0.0004

ILE 200 GLY 201 0.0004

GLY 201 ALA 202 0.0013

ALA 202 ILE 203 0.0007

ILE 203 ASP 204 0.0001

ASP 204 SER 205 0.0013

SER 205 LYS 206 -0.0008

LYS 206 LEU 207 0.0013

LEU 207 ASP 208 0.0014

ASP 208 TRP 209 0.0001

TRP 209 SER 210 0.0022

SER 210 HIS 211 0.0001

HIS 211 ASN 212 0.0004

ASN 212 PHE 213 0.0014

PHE 213 THR 214 0.0008

THR 214 ASN 215 0.0003

ASN 215 MET 216 0.0003

MET 216 LEU 217 0.0013

LEU 217 GLY 218 0.0011

GLY 218 TYR 219 -0.0005

TYR 219 THR 220 0.0001

THR 220 ASP 221 0.0008

ASP 221 ALA 222 0.0005

ALA 222 GLN 223 0.0015

GLN 223 PHE 224 0.0000

PHE 224 THR 225 0.0020

THR 225 GLU 226 -0.0002

GLU 226 LEU 227 0.0007

LEU 227 MET 228 0.0004

MET 228 ARG 229 0.0004

ARG 229 LEU 230 0.0007

LEU 230 TYR 231 0.0007

TYR 231 LEU 232 0.0008

LEU 232 THR 233 0.0009

THR 233 ILE 234 0.0016

ILE 234 HIS 235 -0.0001

HIS 235 SER 236 0.0012

SER 236 ASP 237 0.0009

ASP 237 HIS 238 0.0023

HIS 238 GLU 239 0.0024

GLU 239 GLY 240 0.0001

GLY 240 GLY 241 0.0019

GLY 241 ASN 242 0.0117

ASN 242 VAL 243 -0.0001

VAL 243 SER 244 0.0005

SER 244 ALA 245 -0.0016

ALA 245 HIS 246 0.0022

HIS 246 THR 247 -0.0008

THR 247 SER 248 0.0014

SER 248 HIS 249 0.0017

HIS 249 LEU 250 0.0017

LEU 250 VAL 251 0.0002

VAL 251 GLY 252 0.0023

GLY 252 SER 253 0.0010

SER 253 ALA 254 -0.0006

ALA 254 LEU 255 0.0008

LEU 255 SER 256 0.0010

SER 256 ASP 257 0.0003

ASP 257 PRO 258 0.0009

PRO 258 TYR 259 0.0012

TYR 259 LEU 260 0.0004

LEU 260 SER 261 -0.0004

SER 261 PHE 262 0.0014

PHE 262 ALA 263 0.0010

ALA 263 ALA 264 0.0007

ALA 264 ALA 265 -0.0002

ALA 265 MET 266 0.0004

MET 266 ASN 267 0.0007

ASN 267 GLY 268 0.0023

GLY 268 LEU 269 0.0002

LEU 269 ALA 270 0.0014

ALA 270 GLY 271 0.0012

GLY 271 PRO 272 0.0010

PRO 272 LEU 273 0.0009

LEU 273 HIS 274 0.0010

HIS 274 GLY 275 0.0017

GLY 275 LEU 276 0.0006

LEU 276 ALA 277 0.0003

ALA 277 ASN 278 0.0005

ASN 278 GLN 279 0.0011

GLN 279 GLU 280 0.0016

GLU 280 VAL 281 -0.0006

VAL 281 LEU 282 0.0011

LEU 282 GLY 283 0.0009

GLY 283 TRP 284 0.0010

TRP 284 LEU 285 0.0003

LEU 285 ALA 286 0.0008

ALA 286 GLN 287 0.0009

GLN 287 LEU 288 0.0003

LEU 288 GLN 289 0.0013

GLN 289 LYS 290 0.0014

LYS 290 ALA 291 0.0012

ALA 291 ALA 295 -0.0056

ALA 295 GLY 296 0.0008

GLY 296 ALA 297 0.0009

ALA 297 ASP 298 0.0014

ASP 298 ALA 299 0.0014

ALA 299 SER 300 0.0004

SER 300 LEU 301 0.0012

LEU 301 ARG 302 0.0008

ARG 302 ASP 303 0.0012

ASP 303 TYR 304 -0.0001

TYR 304 ILE 305 0.0012

ILE 305 TRP 306 0.0008

TRP 306 ASN 307 0.0009

ASN 307 THR 308 0.0006

THR 308 LEU 309 0.0010

LEU 309 ASN 310 0.0010

ASN 310 SER 311 0.0006

SER 311 GLY 312 0.0009

GLY 312 ARG 313 0.0014

ARG 313 VAL 314 0.0008

VAL 314 VAL 315 0.0012

VAL 315 PRO 316 0.0005

PRO 316 GLY 317 0.0009

GLY 317 TYR 318 0.0008

TYR 318 GLY 319 0.0015

GLY 319 HIS 320 0.0010

HIS 320 ALA 321 0.0012

ALA 321 VAL 322 0.0009

VAL 322 LEU 323 0.0010

LEU 323 ARG 324 -0.0000

ARG 324 LYS 325 0.0009

LYS 325 THR 326 0.0018

THR 326 ASP 327 0.0004

ASP 327 PRO 328 0.0005

PRO 328 ARG 329 0.0013

ARG 329 TYR 330 0.0012

TYR 330 THR 331 0.0004

THR 331 CYS 332 0.0011

CYS 332 GLN 333 0.0006

GLN 333 ARG 334 0.0002

ARG 334 GLU 335 0.0012

GLU 335 PHE 336 0.0014

PHE 336 ALA 337 0.0011

ALA 337 LEU 338 0.0002

LEU 338 LYS 339 0.0010

LYS 339 HIS 340 0.0011

HIS 340 LEU 341 0.0013

LEU 341 PRO 342 0.0002

PRO 342 GLY 343 0.0013

GLY 343 ASP 344 0.0001

ASP 344 PRO 345 0.0008

PRO 345 MET 346 0.0005

MET 346 PHE 347 0.0013

PHE 347 LYS 348 0.0003

LYS 348 LEU 349 0.0012

LEU 349 VAL 350 0.0008

VAL 350 ALA 351 0.0002

ALA 351 GLN 352 0.0014

GLN 352 LEU 353 0.0006

LEU 353 TYR 354 0.0009

TYR 354 LYS 355 0.0004

LYS 355 ILE 356 0.0011

ILE 356 VAL 357 -0.0002

VAL 357 PRO 358 0.0010

PRO 358 ASN 359 0.0004

ASN 359 VAL 360 0.0009

VAL 360 LEU 361 0.0004

LEU 361 LEU 362 0.0007

LEU 362 GLU 363 0.0008

GLU 363 GLN 364 0.0004

GLN 364 GLY 365 0.0008

GLY 365 ALA 366 0.0008

ALA 366 ALA 367 0.0010

ALA 367 ALA 368 0.0008

ALA 368 ASN 369 0.0014

ASN 369 PRO 370 0.0005

PRO 370 TRP 371 0.0013

TRP 371 PRO 372 0.0005

PRO 372 ASN 373 0.0007

ASN 373 VAL 374 0.0013

VAL 374 ASP 375 0.0004

ASP 375 ALA 376 0.0004

ALA 376 HIS 377 0.0015

HIS 377 SER 378 0.0003

SER 378 GLY 379 0.0010

GLY 379 VAL 380 -0.0001

VAL 380 LEU 381 0.0011

LEU 381 LEU 382 0.0004

LEU 382 GLN 383 0.0008

GLN 383 TYR 384 -0.0000

TYR 384 TYR 385 0.0015

TYR 385 GLY 386 0.0007

GLY 386 MET 387 0.0004

MET 387 THR 388 0.0014

THR 388 GLU 389 -0.0004

GLU 389 MET 390 0.0021

MET 390 ASN 391 -0.0001

ASN 391 TYR 392 0.0018

TYR 392 TYR 393 0.0013

TYR 393 THR 394 0.0005

THR 394 VAL 395 0.0017

VAL 395 LEU 396 -0.0001

LEU 396 PHE 397 0.0005

PHE 397 GLY 398 0.0004

GLY 398 VAL 399 0.0015

VAL 399 SER 400 0.0001

SER 400 ARG 401 0.0012

ARG 401 ALA 402 0.0011

ALA 402 LEU 403 0.0009

LEU 403 GLY 404 0.0013

GLY 404 VAL 405 0.0008

VAL 405 LEU 406 0.0010

LEU 406 ALA 407 0.0011

ALA 407 GLN 408 0.0009

GLN 408 LEU 409 0.0019

LEU 409 ILE 410 0.0008

ILE 410 TRP 411 0.0007

TRP 411 SER 412 0.0023

SER 412 ARG 413 -0.0014

ARG 413 ALA 414 0.0051

ALA 414 LEU 415 0.0025

LEU 415 GLY 416 -0.0018

GLY 416 PHE 417 0.0010

PHE 417 PRO 418 0.0007

PRO 418 LEU 419 0.0014

LEU 419 GLU 420 0.0010

GLU 420 ARG 421 0.0648

ARG 421 PRO 422 0.1937

PRO 422 LYS 423 0.3749

LYS 423 SER 424 0.4866

SER 424 MET 425 0.1968

MET 425 SER 426 0.0838

SER 426 THR 427 0.2124

THR 427 ASP 428 0.2689

ASP 428 GLY 429 0.0078

GLY 429 LEU 430 0.2535

LEU 430 ILE 431 0.1668

ILE 431 ALA 432 0.1985

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.

*** open cutoff8 melek ***

CA strain for 260522120615405517

--- 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.

* open cutoff8 melek *