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

* closed_cutoff10 *

CA strain for 2604261326212470324

--- normal mode 14 ---

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 0.0002

SER 2 SER 3 -0.0004

SER 3 THR 4 0.0004

THR 4 ASN 5 0.0001

ASN 5 LEU 6 0.0000

LEU 6 LYS 7 -0.0386

LYS 7 ASP 8 0.0002

ASP 8 VAL 9 -0.0004

VAL 9 LEU 10 0.0214

LEU 10 ALA 11 0.0001

ALA 11 LEU 13 -0.0002

LEU 13 ILE 14 -0.0002

ILE 14 PRO 15 -0.0000

PRO 15 LYS 16 -0.1689

LYS 16 GLU 17 -0.0004

GLU 17 GLN 18 0.0003

GLN 18 ALA 19 -0.1116

ALA 19 ARG 20 0.0000

ARG 20 ILE 21 -0.0000

ILE 21 LYS 22 -0.0685

LYS 22 THR 23 0.0000

THR 23 PHE 24 -0.0001

PHE 24 ARG 25 0.0154

ARG 25 GLN 26 -0.0002

GLN 26 GLN 27 -0.0001

GLN 27 HIS 28 -0.0100

HIS 28 GLY 29 -0.0000

GLY 29 THR 31 -0.0001

THR 31 ALA 32 -0.0000

ALA 32 GLY 34 -0.1298

GLY 34 GLN 35 -0.0000

GLN 35 ILE 36 -0.0000

ILE 36 THR 37 0.0839

THR 37 VAL 38 0.0002

VAL 38 ASP 39 -0.0001

ASP 39 MET 40 0.0015

MET 40 SER 41 -0.0000

SER 41 TYR 42 -0.0004

TYR 42 GLY 43 -0.0967

GLY 43 GLY 44 0.0003

GLY 44 MET 45 0.0002

MET 45 ARG 46 -0.0294

ARG 46 GLY 47 -0.0005

GLY 47 MET 48 -0.0002

MET 48 LYS 49 -0.0331

LYS 49 GLY 50 0.0002

GLY 50 LEU 51 0.0002

LEU 51 TYR 53 0.0104

TYR 53 GLU 54 -0.0003

GLU 54 THR 55 0.0001

THR 55 SER 56 0.0021

SER 56 VAL 57 0.0001

VAL 57 LEU 58 0.0002

LEU 58 ASP 59 0.0182

ASP 59 PRO 60 0.0000

PRO 60 ASP 61 -0.0001

ASP 61 GLU 62 -0.0182

GLU 62 GLY 63 -0.0002

GLY 63 ILE 64 0.0002

ILE 64 ARG 65 0.0059

ARG 65 PHE 66 0.0003

PHE 66 ARG 67 0.0003

ARG 67 GLY 68 0.0013

GLY 68 PHE 69 -0.0002

PHE 69 SER 70 0.0004

SER 70 ILE 71 0.0019

ILE 71 PRO 72 -0.0003

PRO 72 GLU 73 -0.0005

GLU 73 CYS 74 0.0031

CYS 74 GLN 75 -0.0000

GLN 75 LYS 76 0.0001

LYS 76 LEU 77 0.0028

LEU 77 LEU 78 0.0003

LEU 78 PRO 79 0.0000

PRO 79 LYS 80 0.0097

LYS 80 GLY 82 -0.0001

GLY 82 GLY 84 -0.0002

GLY 84 GLU 86 -0.0040

GLU 86 PRO 87 -0.0002

PRO 87 LEU 88 -0.0001

LEU 88 PRO 89 -0.0072

PRO 89 GLU 90 0.0000

GLU 90 GLY 91 -0.0003

GLY 91 LEU 92 -0.0080

LEU 92 PHE 93 -0.0001

PHE 93 TRP 94 0.0001

TRP 94 LEU 95 -0.0139

LEU 95 LEU 96 0.0004

LEU 96 VAL 97 -0.0001

VAL 97 THR 98 0.0170

THR 98 GLY 99 -0.0001

GLY 99 GLN 100 0.0001

GLN 100 ILE 101 0.0220

ILE 101 PRO 102 0.0000

PRO 102 THR 103 -0.0004

THR 103 GLN 106 -0.0053

GLN 106 VAL 107 0.0003

VAL 107 SER 108 -0.0000

SER 108 TRP 109 -0.0025

TRP 109 SER 111 -0.0001

SER 111 LYS 112 -0.0002

LYS 112 GLU 113 -0.0001

GLU 113 TRP 114 0.0009

TRP 114 ALA 115 -0.0001

ALA 115 LYS 116 -0.0003

LYS 116 ARG 117 -0.0028

ARG 117 ALA 118 -0.0002

ALA 118 ALA 119 0.0003

ALA 119 LEU 120 -0.0032

LEU 120 PRO 121 -0.0000

PRO 121 SER 122 -0.0002

SER 122 HIS 123 0.0031

HIS 123 VAL 124 0.0000

VAL 124 VAL 125 0.0003

VAL 125 THR 126 0.0006

THR 126 MET 127 -0.0000

MET 127 LEU 128 0.0000

LEU 128 ASP 129 0.0023

ASP 129 ASN 130 0.0000

ASN 130 PHE 131 -0.0000

PHE 131 PRO 132 0.0010

PRO 132 THR 133 0.0000

THR 133 ASN 134 -0.0001

ASN 134 LEU 135 0.0011

LEU 135 HIS 136 -0.0001

HIS 136 PRO 137 0.0000

PRO 137 MET 138 0.0040

MET 138 SER 139 -0.0003

SER 139 GLN 140 0.0001

GLN 140 LEU 141 0.0014

LEU 141 SER 142 0.0001

SER 142 ALA 143 -0.0000

ALA 143 ALA 144 0.0013

ALA 144 ILE 145 -0.0001

ILE 145 THR 146 0.0004

THR 146 ALA 147 0.0025

ALA 147 LEU 148 0.0004

LEU 148 ASN 149 0.0001

ASN 149 SER 150 0.0020

SER 150 GLU 151 0.0002

GLU 151 SER 152 -0.0005

SER 152 ASN 153 -0.0023

ASN 153 PHE 154 -0.0001

PHE 154 ALA 155 0.0001

ALA 155 ARG 156 0.0066

ARG 156 ALA 157 -0.0000

ALA 157 TYR 158 -0.0000

TYR 158 ALA 159 0.0003

ALA 159 GLU 160 0.0001

GLU 160 GLY 161 -0.0002

GLY 161 ILE 162 -0.0016

ILE 162 ARG 164 -0.0003

ARG 164 THR 165 0.0001

THR 165 LYS 166 0.0002

LYS 166 TYR 167 0.0039

TYR 167 TRP 168 0.0003

TRP 168 GLU 169 0.0005

GLU 169 VAL 171 -0.0003

VAL 171 TYR 172 0.0001

TYR 172 GLU 173 -0.0000

GLU 173 ALA 175 0.0033

ALA 175 MET 176 0.0001

MET 176 ASP 177 0.0002

ASP 177 LEU 178 -0.0019

LEU 178 ILE 179 -0.0002

ILE 179 ALA 180 -0.0003

ALA 180 LYS 181 0.0009

LYS 181 LEU 182 -0.0000

LEU 182 PRO 183 -0.0002

PRO 183 CYS 184 0.0013

CYS 184 VAL 185 -0.0002

VAL 185 ALA 186 -0.0001

ALA 186 ALA 187 0.0004

ALA 187 LYS 188 -0.0004

LYS 188 ILE 189 -0.0001

ILE 189 TYR 190 -0.0010

TYR 190 ARG 191 -0.0001

ARG 191 ASN 192 0.0003

ASN 192 LEU 193 -0.0035

LEU 193 TYR 194 0.0002

TYR 194 ARG 195 0.0000

ARG 195 ALA 196 -0.0012

ALA 196 GLY 197 0.0001

GLY 197 SER 198 -0.0000

SER 198 SER 199 0.0023

SER 199 ILE 200 0.0002

ILE 200 GLY 201 0.0002

GLY 201 ALA 202 -0.0011

ALA 202 ILE 203 0.0002

ILE 203 ASP 204 0.0002

ASP 204 SER 205 0.0020

SER 205 LYS 206 -0.0005

LYS 206 LEU 207 -0.0002

LEU 207 ASP 208 -0.0026

ASP 208 TRP 209 -0.0000

TRP 209 SER 210 -0.0002

SER 210 HIS 211 -0.0011

HIS 211 ASN 212 0.0001

ASN 212 PHE 213 -0.0002

PHE 213 THR 214 -0.0003

THR 214 ASN 215 -0.0002

ASN 215 MET 216 -0.0002

MET 216 LEU 217 -0.0024

LEU 217 GLY 218 0.0001

GLY 218 TYR 219 0.0003

TYR 219 THR 220 -0.0056

THR 220 ASP 221 0.0002

ASP 221 GLN 223 -0.0003

GLN 223 PHE 224 -0.0002

PHE 224 THR 225 -0.0001

THR 225 GLU 226 0.0040

GLU 226 LEU 227 0.0004

LEU 227 MET 228 0.0000

MET 228 ARG 229 0.0028

ARG 229 LEU 230 -0.0001

LEU 230 TYR 231 -0.0001

TYR 231 LEU 232 0.0088

LEU 232 THR 233 0.0003

THR 233 ILE 234 0.0000

ILE 234 HIS 235 0.0041

HIS 235 SER 236 0.0003

SER 236 ASP 237 -0.0003

ASP 237 HIS 238 -0.0005

HIS 238 GLU 239 -0.0002

GLU 239 GLY 240 -0.0004

GLY 240 GLY 241 -0.0145

GLY 241 ASN 242 -0.0000

ASN 242 VAL 243 -0.0002

VAL 243 SER 244 -0.0049

SER 244 ALA 245 -0.0001

ALA 245 HIS 246 -0.0002

HIS 246 THR 247 -0.0047

THR 247 SER 248 0.0001

SER 248 HIS 249 0.0005

HIS 249 LEU 250 0.0075

LEU 250 VAL 251 -0.0001

VAL 251 GLY 252 -0.0002

GLY 252 SER 253 -0.0071

SER 253 ALA 254 0.0000

ALA 254 LEU 255 0.0001

LEU 255 SER 256 -0.0135

SER 256 ASP 257 -0.0000

ASP 257 PRO 258 0.0002

PRO 258 TYR 259 -0.0002

TYR 259 LEU 260 0.0000

LEU 260 SER 261 0.0002

SER 261 PHE 262 -0.0042

PHE 262 ALA 263 0.0001

ALA 263 ALA 264 0.0003

ALA 264 ALA 265 -0.0024

ALA 265 MET 266 -0.0002

MET 266 ASN 267 -0.0000

ASN 267 GLY 268 -0.0032

GLY 268 LEU 269 0.0005

LEU 269 ALA 270 0.0004

ALA 270 GLY 271 0.0076

GLY 271 PRO 272 -0.0003

PRO 272 LEU 273 -0.0001

LEU 273 HIS 274 -0.0182

HIS 274 GLY 275 -0.0001

GLY 275 LEU 276 -0.0004

LEU 276 ALA 277 0.0106

ALA 277 ASN 278 0.0002

ASN 278 GLN 279 -0.0001

GLN 279 GLU 280 0.0022

GLU 280 VAL 281 0.0005

VAL 281 LEU 282 0.0002

LEU 282 TRP 284 0.0117

TRP 284 LEU 285 0.0001

LEU 285 GLN 287 -0.0001

GLN 287 LEU 288 -0.0005

LEU 288 GLN 289 -0.0003

GLN 289 LYS 290 0.0359

LYS 290 ASP 298 0.0001

ASP 298 LEU 301 0.0001

LEU 301 ARG 302 0.0003

ARG 302 ASP 303 -0.0003

ASP 303 TYR 304 -0.0007

TYR 304 ILE 305 -0.0001

ILE 305 TRP 306 -0.0001

TRP 306 ASN 307 -0.0182

ASN 307 THR 308 0.0000

THR 308 LEU 309 -0.0000

LEU 309 ASN 310 -0.0201

ASN 310 SER 311 -0.0001

SER 311 GLY 312 -0.0003

GLY 312 ARG 313 0.0249

ARG 313 VAL 314 0.0001

VAL 314 VAL 315 -0.0002

VAL 315 PRO 316 0.0062

PRO 316 GLY 317 -0.0001

GLY 317 TYR 318 0.0002

TYR 318 GLY 319 -0.0034

GLY 319 HIS 320 -0.0002

HIS 320 ALA 321 0.0001

ALA 321 VAL 322 -0.0653

VAL 322 LEU 323 -0.0003

LEU 323 ARG 324 0.0000

ARG 324 LYS 325 0.0141

LYS 325 THR 326 -0.0005

THR 326 ASP 327 0.0001

ASP 327 PRO 328 -0.0135

PRO 328 ARG 329 -0.0002

ARG 329 TYR 330 -0.0001

TYR 330 THR 331 0.0121

THR 331 CYS 332 0.0002

CYS 332 GLN 333 -0.0001

GLN 333 ARG 334 0.0157

ARG 334 GLU 335 0.0001

GLU 335 PHE 336 -0.0000

PHE 336 ALA 337 0.0042

ALA 337 LEU 338 0.0000

LEU 338 LYS 339 -0.0002

LYS 339 HIS 340 -0.0032

HIS 340 LEU 341 -0.0004

LEU 341 PRO 342 -0.0001

PRO 342 ASP 344 0.0041

ASP 344 PRO 345 0.0004

PRO 345 MET 346 -0.0000

MET 346 PHE 347 0.0084

PHE 347 LYS 348 -0.0003

LYS 348 LEU 349 0.0004

LEU 349 VAL 350 0.0081

VAL 350 ALA 351 0.0001

ALA 351 GLN 352 -0.0000

GLN 352 LEU 353 -0.0007

LEU 353 TYR 354 0.0000

TYR 354 LYS 355 0.0002

LYS 355 ILE 356 0.0035

ILE 356 VAL 357 0.0003

VAL 357 PRO 358 -0.0001

PRO 358 ASN 359 0.0018

ASN 359 VAL 360 -0.0001

VAL 360 LEU 361 0.0001

LEU 361 LEU 362 0.0070

LEU 362 GLU 363 -0.0001

GLU 363 GLN 364 0.0003

GLN 364 GLY 365 -0.0151

GLY 365 ALA 367 0.0002

ALA 367 ASN 369 -0.0001

ASN 369 PRO 370 0.0002

PRO 370 TRP 371 0.0002

TRP 371 PRO 372 0.0044

PRO 372 ASN 373 -0.0002

ASN 373 VAL 374 0.0002

VAL 374 ASP 375 -0.0010

ASP 375 ALA 376 0.0001

ALA 376 HIS 377 -0.0003

HIS 377 SER 378 0.0035

SER 378 GLY 379 0.0001

GLY 379 VAL 380 0.0000

VAL 380 LEU 381 0.0060

LEU 381 LEU 382 -0.0000

LEU 382 GLN 383 -0.0001

GLN 383 TYR 384 -0.0054

TYR 384 TYR 385 -0.0003

TYR 385 GLY 386 -0.0000

GLY 386 MET 387 -0.0102

MET 387 THR 388 -0.0002

THR 388 GLU 389 0.0001

GLU 389 MET 390 -0.0020

MET 390 ASN 391 0.0001

ASN 391 TYR 392 0.0002

TYR 392 TYR 393 -0.0029

TYR 393 THR 394 0.0000

THR 394 VAL 395 -0.0000

VAL 395 LEU 396 0.0003

LEU 396 PHE 397 -0.0001

PHE 397 GLY 398 -0.0003

GLY 398 VAL 399 -0.0024

VAL 399 SER 400 -0.0001

SER 400 ARG 401 0.0002

ARG 401 ALA 402 -0.0016

ALA 402 LEU 403 0.0002

LEU 403 GLY 404 -0.0003

GLY 404 VAL 405 0.0007

VAL 405 LEU 406 -0.0002

LEU 406 ALA 407 -0.0000

ALA 407 GLN 408 0.0010

GLN 408 LEU 409 -0.0001

LEU 409 ILE 410 -0.0003

ILE 410 TRP 411 0.0410

TRP 411 SER 412 0.0002

SER 412 ARG 413 -0.0005

ARG 413 ALA 414 -0.0355

ALA 414 LEU 415 0.0000

LEU 415 GLY 416 -0.0002

GLY 416 PHE 417 0.0012

PHE 417 PRO 418 0.0002

PRO 418 LEU 419 -0.0003

LEU 419 GLU 420 0.0862

GLU 420 ARG 421 -0.0005

ARG 421 PRO 422 0.0001

PRO 422 LYS 423 -0.0155

LYS 423 SER 424 -0.0003

SER 424 MET 425 0.0000

MET 425 SER 426 0.1238

SER 426 THR 427 0.0000

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.

*** closed_cutoff10 ***

CA strain for 2604261326212470324

--- normal mode 14 ---

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

* closed_cutoff10 *