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

* aspartate open to closed cut off 8 *

CA strain for 2604241226251976617

--- 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
SER 3 SER 4 -0.0004

SER 4 TRP 5 0.0002

TRP 5 TRP 6 0.0034

TRP 6 SER 7 -0.0004

SER 7 HIS 8 -0.0005

HIS 8 VAL 9 0.0056

VAL 9 GLU 10 0.0002

GLU 10 MET 11 -0.0002

MET 11 GLY 12 -0.0033

GLY 12 PRO 13 -0.0000

PRO 13 PRO 14 -0.0004

PRO 14 ASP 15 0.0084

ASP 15 PRO 16 0.0000

PRO 16 ILE 17 -0.0002

ILE 17 LEU 18 -0.0102

LEU 18 GLY 19 0.0001

GLY 19 VAL 20 -0.0001

VAL 20 THR 21 0.0065

THR 21 GLU 22 -0.0000

GLU 22 ALA 23 0.0000

ALA 23 PHE 24 -0.0402

PHE 24 LYS 25 -0.0002

LYS 25 ARG 26 0.0001

ARG 26 ASP 27 -0.0196

ASP 27 THR 28 0.0000

THR 28 ASN 29 -0.0000

ASN 29 SER 30 -0.0048

SER 30 LYS 31 -0.0001

LYS 31 LYS 32 -0.0000

LYS 32 MET 33 -0.0305

MET 33 ASN 34 -0.0002

ASN 34 LEU 35 0.0002

LEU 35 GLY 36 0.0173

GLY 36 VAL 37 0.0001

VAL 37 GLY 38 0.0001

GLY 38 ALA 39 -0.0328

ALA 39 TYR 40 0.0004

TYR 40 ARG 41 -0.0003

ARG 41 ASP 42 0.0133

ASP 42 ASP 43 0.0001

ASP 43 ASN 44 0.0002

ASN 44 GLY 45 -0.0289

GLY 45 LYS 46 -0.0000

LYS 46 PRO 47 0.0002

PRO 47 TYR 48 -0.0239

TYR 48 VAL 49 0.0002

VAL 49 LEU 50 -0.0001

LEU 50 ASN 51 -0.0040

ASN 51 CYS 52 0.0001

CYS 52 VAL 53 0.0001

VAL 53 ARG 54 -0.0119

ARG 54 LYS 55 0.0004

LYS 55 ALA 56 -0.0001

ALA 56 GLU 57 0.0078

GLU 57 ALA 58 0.0004

ALA 58 MET 59 -0.0003

MET 59 ILE 60 -0.0018

ILE 60 ALA 61 0.0001

ALA 61 ALA 62 -0.0001

ALA 62 LYS 63 -0.0067

LYS 63 LYS 64 0.0002

LYS 64 MET 66 -0.0001

MET 66 ASP 67 -0.0000

ASP 67 LYS 68 0.0002

LYS 68 GLU 69 0.0053

GLU 69 TYR 70 -0.0002

TYR 70 LEU 71 0.0001

LEU 71 PRO 72 0.0104

PRO 72 ILE 73 -0.0003

ILE 73 ALA 74 -0.0002

ALA 74 GLY 75 -0.0011

GLY 75 LEU 76 0.0000

LEU 76 ALA 77 -0.0002

ALA 77 ASP 78 -0.0129

ASP 78 PHE 79 -0.0002

PHE 79 THR 80 0.0004

THR 80 ARG 81 0.0031

ARG 81 ALA 82 0.0001

ALA 82 SER 83 0.0002

SER 83 ALA 84 0.0097

ALA 84 GLU 85 0.0001

GLU 85 LEU 86 0.0000

LEU 86 ALA 87 0.0067

ALA 87 LEU 88 0.0000

LEU 88 GLY 89 0.0003

GLY 89 GLU 90 -0.0164

GLU 90 ASN 91 0.0002

ASN 91 SER 92 0.0001

SER 92 GLU 93 -0.0028

GLU 93 ALA 94 0.0004

ALA 94 PHE 95 -0.0003

PHE 95 LYS 96 0.0050

LYS 96 SER 97 0.0001

SER 97 GLY 98 -0.0001

GLY 98 ARG 99 0.0008

ARG 99 TYR 100 0.0004

TYR 100 VAL 101 -0.0003

VAL 101 THR 102 0.0102

THR 102 VAL 103 0.0002

VAL 103 GLN 104 -0.0002

GLN 104 GLY 105 -0.0050

GLY 105 ILE 106 0.0002

ILE 106 SER 107 0.0001

SER 107 GLY 108 -0.0009

GLY 108 THR 109 0.0004

THR 109 GLY 110 -0.0003

GLY 110 SER 111 0.0032

SER 111 LEU 112 -0.0002

LEU 112 ARG 113 0.0002

ARG 113 VAL 114 0.0046

VAL 114 GLY 115 0.0002

GLY 115 ALA 116 -0.0001

ALA 116 ASN 117 -0.0015

ASN 117 PHE 118 0.0002

PHE 118 LEU 119 0.0000

LEU 119 GLN 120 0.0032

GLN 120 ARG 121 -0.0004

ARG 121 PHE 122 0.0000

PHE 122 PHE 123 -0.0021

PHE 123 LYS 124 -0.0002

LYS 124 PHE 125 0.0001

PHE 125 SER 126 -0.0007

SER 126 ARG 129 0.0001

ARG 129 ASP 130 0.0000

ASP 130 VAL 133 -0.0009

VAL 133 TYR 134 0.0001

TYR 134 LEU 135 -0.0001

LEU 135 PRO 136 0.0080

PRO 136 LYS 137 -0.0001

LYS 137 PRO 138 -0.0001

PRO 138 SER 139 -0.0115

SER 139 TRP 140 -0.0003

TRP 140 GLY 141 0.0001

GLY 141 ASN 142 -0.0063

ASN 142 HIS 143 -0.0001

HIS 143 THR 144 0.0002

THR 144 PRO 145 -0.0050

PRO 145 ILE 146 -0.0001

ILE 146 PHE 147 -0.0001

PHE 147 ARG 148 -0.0003

ARG 148 ASP 149 0.0000

ASP 149 ALA 150 -0.0001

ALA 150 GLY 151 -0.0050

GLY 151 LEU 152 -0.0002

LEU 152 GLN 154 -0.0001

GLN 154 LEU 155 0.0005

LEU 155 GLN 156 -0.0003

GLN 156 ALA 157 0.0088

ALA 157 TYR 158 0.0002

TYR 158 ARG 159 0.0000

ARG 159 TYR 160 -0.0085

TYR 160 TYR 161 0.0002

TYR 161 ASP 162 0.0000

ASP 162 PRO 163 0.0173

PRO 163 LYS 164 0.0001

LYS 164 THR 165 -0.0002

THR 165 CYS 166 -0.0043

CYS 166 SER 167 0.0002

SER 167 LEU 168 -0.0002

LEU 168 ASP 169 -0.0046

ASP 169 PHE 170 -0.0001

PHE 170 THR 171 -0.0002

THR 171 GLY 172 0.0029

GLY 172 ALA 173 -0.0002

ALA 173 MET 174 0.0001

MET 174 GLU 175 0.0047

GLU 175 ASP 176 0.0005

ASP 176 ILE 177 -0.0002

ILE 177 SER 178 0.0068

SER 178 LYS 179 0.0001

LYS 179 ILE 180 0.0001

ILE 180 PRO 181 -0.0017

PRO 181 GLU 182 -0.0002

GLU 182 LYS 183 -0.0003

LYS 183 SER 184 0.0031

SER 184 ILE 185 -0.0001

ILE 185 ILE 186 0.0000

ILE 186 LEU 187 -0.0018

LEU 187 LEU 188 -0.0002

LEU 188 HIS 189 0.0003

HIS 189 ALA 190 0.0345

ALA 190 CYS 191 0.0000

CYS 191 ALA 192 -0.0002

ALA 192 HIS 193 -0.0086

HIS 193 ASN 194 -0.0001

ASN 194 PRO 195 0.0003

PRO 195 THR 196 -0.0191

THR 196 GLY 197 -0.0000

GLY 197 VAL 198 -0.0003

VAL 198 ASP 199 -0.0087

ASP 199 PRO 200 0.0000

PRO 200 ARG 201 0.0002

ARG 201 GLN 202 0.0041

GLN 202 GLU 203 -0.0001

GLU 203 GLN 204 -0.0002

GLN 204 TRP 205 0.0096

TRP 205 LYS 206 -0.0004

LYS 206 GLU 207 -0.0004

GLU 207 LEU 208 0.0050

LEU 208 ALA 209 0.0000

ALA 209 SER 210 -0.0001

SER 210 VAL 211 0.0076

VAL 211 VAL 212 -0.0002

VAL 212 LYS 213 0.0002

LYS 213 LYS 214 -0.0035

LYS 214 ARG 215 0.0001

ARG 215 ASN 216 -0.0001

ASN 216 LEU 217 0.0049

LEU 217 LEU 218 0.0004

LEU 218 ALA 219 0.0000

ALA 219 TYR 220 0.0054

TYR 220 PHE 221 0.0001

PHE 221 ASP 222 -0.0003

ASP 222 MET 223 -0.0072

MET 223 ALA 224 0.0000

ALA 224 TYR 225 -0.0001

TYR 225 GLN 226 0.0044

GLN 226 GLY 227 0.0002

GLY 227 PHE 228 -0.0001

PHE 228 ALA 229 0.0071

ALA 229 SER 230 0.0000

SER 230 GLY 231 0.0002

GLY 231 ASP 232 -0.0379

ASP 232 ILE 233 0.0002

ILE 233 ASN 234 -0.0002

ASN 234 ARG 235 -0.0133

ARG 235 ASP 236 -0.0004

ASP 236 ALA 237 0.0001

ALA 237 TRP 238 0.0132

TRP 238 ALA 239 0.0004

ALA 239 LEU 240 0.0000

LEU 240 ARG 241 -0.0022

ARG 241 HIS 242 -0.0005

HIS 242 PHE 243 0.0002

PHE 243 ILE 244 0.0128

ILE 244 GLU 245 0.0002

GLU 245 GLN 246 -0.0003

GLN 246 GLY 247 0.0029

GLY 247 ILE 248 -0.0004

ILE 248 ASP 249 0.0000

ASP 249 VAL 250 0.0033

VAL 250 VAL 251 -0.0000

VAL 251 LEU 252 0.0003

LEU 252 SER 253 0.0039

SER 253 GLN 254 0.0001

GLN 254 SER 255 -0.0001

SER 255 TYR 256 0.0020

TYR 256 ALA 257 -0.0001

ALA 257 LYS 258 -0.0000

LYS 258 ASN 259 0.0314

ASN 259 MET 260 -0.0001

MET 260 GLY 261 -0.0002

GLY 261 LEU 262 0.0410

LEU 262 TYR 263 0.0001

TYR 263 GLY 264 -0.0000

GLY 264 GLU 265 -0.0065

GLU 265 ARG 266 -0.0001

ARG 266 ALA 267 -0.0001

ALA 267 GLY 268 -0.0014

GLY 268 ALA 269 0.0004

ALA 269 PHE 270 -0.0002

PHE 270 THR 271 0.0059

THR 271 VAL 272 -0.0002

VAL 272 ILE 273 0.0001

ILE 273 CYS 274 0.0085

CYS 274 ARG 275 -0.0004

ARG 275 ASP 276 -0.0003

ASP 276 ALA 277 -0.0000

ALA 277 GLU 278 0.0000

GLU 278 GLU 279 -0.0002

GLU 279 ALA 280 0.0060

ALA 280 LYS 281 -0.0002

LYS 281 ARG 282 -0.0002

ARG 282 VAL 283 0.0044

VAL 283 GLU 284 0.0005

GLU 284 SER 285 -0.0002

SER 285 GLN 286 0.0032

GLN 286 LEU 287 0.0000

LEU 287 LYS 288 0.0002

LYS 288 ILE 289 0.0020

ILE 289 LEU 290 0.0003

LEU 290 ILE 291 -0.0004

ILE 291 ARG 292 -0.0002

ARG 292 PRO 293 -0.0003

PRO 293 MET 294 0.0001

MET 294 TYR 295 -0.0003

TYR 295 SER 296 -0.0002

SER 296 ASN 297 0.0003

ASN 297 PRO 298 -0.0007

PRO 298 PRO 299 0.0001

PRO 299 MET 300 -0.0000

MET 300 ASN 301 0.0015

ASN 301 GLY 302 0.0001

GLY 302 ALA 303 0.0003

ALA 303 ARG 304 -0.0128

ARG 304 ILE 305 0.0001

ILE 305 ALA 306 -0.0001

ALA 306 SER 307 0.0185

SER 307 LEU 308 -0.0000

LEU 308 ILE 309 0.0001

ILE 309 LEU 310 0.0080

LEU 310 ASN 311 0.0002

ASN 311 THR 312 0.0003

THR 312 PRO 313 -0.0028

PRO 313 GLU 314 0.0003

GLU 314 LEU 315 0.0001

LEU 315 ARG 316 0.0030

ARG 316 LYS 317 0.0000

LYS 317 GLU 318 0.0001

GLU 318 TRP 319 0.0126

TRP 319 LEU 320 0.0000

LEU 320 VAL 321 0.0003

VAL 321 GLU 322 0.0114

GLU 322 VAL 323 -0.0002

VAL 323 LYS 324 0.0001

LYS 324 GLY 325 -0.0036

GLY 325 MET 326 -0.0002

MET 326 ALA 327 -0.0001

ALA 327 ASP 328 0.0429

ASP 328 ARG 329 -0.0001

ARG 329 ILE 330 0.0004

ILE 330 ILE 331 0.0033

ILE 331 SER 332 -0.0000

SER 332 MET 333 0.0001

MET 333 ARG 334 -0.0402

ARG 334 THR 335 0.0000

THR 335 GLN 336 -0.0002

GLN 336 LEU 337 -0.0111

LEU 337 VAL 338 0.0003

VAL 338 SER 339 -0.0002

SER 339 ASN 340 0.0151

ASN 340 LEU 341 -0.0002

LEU 341 LYS 342 -0.0001

LYS 342 LYS 343 -0.0086

LYS 343 GLU 344 0.0003

GLU 344 GLY 345 -0.0000

GLY 345 SER 346 -0.0113

SER 346 SER 347 0.0001

SER 347 HIS 348 0.0001

HIS 348 ASN 349 -0.0179

ASN 349 TRP 350 -0.0000

TRP 350 GLN 351 -0.0006

GLN 351 HIS 352 -0.0078

HIS 352 ILE 353 0.0004

ILE 353 THR 354 0.0003

THR 354 ASP 355 -0.0108

ASP 355 GLN 356 -0.0001

GLN 356 ILE 357 -0.0001

ILE 357 GLY 358 -0.0036

GLY 358 MET 359 0.0000

MET 359 PHE 360 0.0002

PHE 360 CYS 361 0.0072

CYS 361 PHE 362 -0.0000

PHE 362 THR 363 0.0004

THR 363 GLY 364 0.0054

GLY 364 LEU 365 0.0001

LEU 365 LYS 366 0.0005

LYS 366 PRO 367 -0.0122

PRO 367 GLU 368 0.0003

GLU 368 GLN 369 -0.0000

GLN 369 VAL 370 0.0068

VAL 370 GLU 371 0.0002

GLU 371 ARG 372 -0.0003

ARG 372 LEU 373 -0.0131

LEU 373 THR 374 0.0005

THR 374 LYS 375 0.0003

LYS 375 GLU 376 -0.0156

GLU 376 PHE 377 -0.0001

PHE 377 SER 378 0.0002

SER 378 ILE 379 0.0055

ILE 379 TYR 380 0.0002

TYR 380 MET 381 -0.0002

MET 381 THR 382 0.0088

THR 382 LYS 383 0.0004

LYS 383 ASP 384 -0.0001

ASP 384 GLY 385 -0.0376

GLY 385 ARG 386 0.0000

ARG 386 ILE 387 -0.0002

ILE 387 SER 388 -0.0594

SER 388 VAL 389 -0.0001

VAL 389 ALA 390 0.0002

ALA 390 GLY 391 -0.0159

GLY 391 VAL 392 0.0001

VAL 392 ALA 393 0.0001

ALA 393 SER 394 -0.0181

SER 394 SER 395 -0.0001

SER 395 ASN 396 -0.0001

ASN 396 VAL 397 -0.0245

VAL 397 GLY 398 0.0002

GLY 398 TYR 399 -0.0000

TYR 399 LEU 400 -0.0177

LEU 400 ALA 401 0.0005

ALA 401 HIS 402 0.0005

HIS 402 ALA 403 -0.0253

ALA 403 ILE 404 -0.0000

ILE 404 HIS 405 -0.0003

HIS 405 GLN 406 -0.0156

GLN 406 VAL 408 -0.0001

VAL 408 THR 409 -0.0001

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.

*** aspartate open to closed cut off 8 ***

CA strain for 2604241226251976617

--- 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.

* aspartate open to closed cut off 8 *