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

* Apo AMPK *

CA strain for 260711175133601569

--- normal mode 11 ---

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
ARG 10 VAL 11 0.0001

VAL 11 LYS 12 -0.0002

LYS 12 ILE 13 0.0067

ILE 13 GLY 14 0.0005

GLY 14 HIS 15 -0.0001

HIS 15 TYR 16 -0.0012

TYR 16 ILE 17 0.0001

ILE 17 LEU 18 0.0001

LEU 18 GLY 19 -0.0005

GLY 19 ASP 20 -0.0005

ASP 20 THR 21 -0.0001

THR 21 LEU 22 -0.0119

LEU 22 GLY 23 -0.0002

GLY 23 VAL 24 -0.0002

VAL 24 GLY 25 0.0038

GLY 25 THR 26 -0.0002

THR 26 PHE 27 0.0000

PHE 27 GLY 28 -0.0015

GLY 28 LYS 29 0.0003

LYS 29 VAL 30 -0.0002

VAL 30 LYS 31 0.0001

LYS 31 VAL 32 0.0002

VAL 32 GLY 33 0.0001

GLY 33 LYS 34 0.0039

LYS 34 HIS 35 -0.0002

HIS 35 GLU 36 0.0001

GLU 36 LEU 37 -0.0011

LEU 37 THR 38 0.0000

THR 38 GLY 39 -0.0004

GLY 39 HIS 40 0.0031

HIS 40 LYS 41 -0.0003

LYS 41 VAL 42 0.0000

VAL 42 ALA 43 0.0049

ALA 43 VAL 44 -0.0000

VAL 44 LYS 45 0.0001

LYS 45 ILE 46 -0.0066

ILE 46 LEU 47 0.0002

LEU 47 ASN 48 -0.0005

ASN 48 ARG 49 -0.0050

ARG 49 GLN 50 0.0005

GLN 50 LYS 51 -0.0001

LYS 51 ILE 52 0.0091

ILE 52 ARG 53 -0.0004

ARG 53 SER 54 -0.0001

SER 54 LEU 55 -0.0016

LEU 55 ASP 56 0.0004

ASP 56 VAL 57 0.0001

VAL 57 VAL 58 -0.0028

VAL 58 GLY 59 0.0005

GLY 59 LYS 60 -0.0004

LYS 60 ILE 61 -0.0046

ILE 61 ARG 62 0.0002

ARG 62 ARG 63 -0.0001

ARG 63 GLU 64 0.0054

GLU 64 ILE 65 0.0003

ILE 65 GLN 66 0.0001

GLN 66 ASN 67 0.0054

ASN 67 LEU 68 0.0001

LEU 68 LYS 69 -0.0001

LYS 69 LEU 70 0.0058

LEU 70 PHE 71 0.0001

PHE 71 ARG 72 -0.0002

ARG 72 HIS 73 0.0021

HIS 73 PRO 74 -0.0002

PRO 74 HIS 75 -0.0000

HIS 75 ILE 76 0.0006

ILE 76 ILE 77 -0.0002

ILE 77 LYS 78 -0.0004

LYS 78 LEU 79 0.0009

LEU 79 TYR 80 0.0004

TYR 80 GLN 81 -0.0001

GLN 81 VAL 82 0.0007

VAL 82 ILE 83 0.0001

ILE 83 SER 84 -0.0000

SER 84 THR 85 0.0060

THR 85 PRO 86 0.0000

PRO 86 SER 87 -0.0002

SER 87 ASP 88 -0.0006

ASP 88 ILE 89 0.0003

ILE 89 PHE 90 0.0004

PHE 90 MET 91 0.0022

MET 91 VAL 92 -0.0001

VAL 92 MET 93 -0.0000

MET 93 GLU 94 -0.0069

GLU 94 TYR 95 -0.0000

TYR 95 VAL 96 -0.0001

VAL 96 SER 97 0.0032

SER 97 GLY 98 0.0000

GLY 98 GLY 99 -0.0005

GLY 99 GLU 100 -0.0073

GLU 100 LEU 101 -0.0003

LEU 101 PHE 102 -0.0002

PHE 102 ASP 103 0.0060

ASP 103 TYR 104 0.0000

TYR 104 ILE 105 0.0002

ILE 105 CYS 106 -0.0006

CYS 106 LYS 107 0.0002

LYS 107 ASN 108 -0.0001

ASN 108 GLY 109 -0.0037

GLY 109 ARG 110 -0.0001

ARG 110 LEU 111 -0.0000

LEU 111 ASP 112 -0.0008

ASP 112 GLU 113 -0.0001

GLU 113 LYS 114 -0.0004

LYS 114 GLU 115 -0.0011

GLU 115 SER 116 0.0001

SER 116 ARG 117 -0.0000

ARG 117 ARG 118 -0.0043

ARG 118 LEU 119 0.0004

LEU 119 PHE 120 -0.0000

PHE 120 GLN 121 0.0064

GLN 121 GLN 122 0.0001

GLN 122 ILE 123 0.0000

ILE 123 LEU 124 -0.0043

LEU 124 SER 125 -0.0002

SER 125 GLY 126 -0.0004

GLY 126 VAL 127 -0.0005

VAL 127 ASP 128 0.0003

ASP 128 TYR 129 -0.0002

TYR 129 CYS 130 -0.0021

CYS 130 HIS 131 -0.0001

HIS 131 ARG 132 0.0001

ARG 132 HIS 133 0.0077

HIS 133 MET 134 0.0001

MET 134 VAL 135 0.0003

VAL 135 VAL 136 -0.0029

VAL 136 HIS 137 -0.0001

HIS 137 ARG 138 -0.0002

ARG 138 ASP 139 0.0241

ASP 139 LEU 140 0.0002

LEU 140 LYS 141 0.0000

LYS 141 PRO 142 0.0104

PRO 142 GLU 143 0.0000

GLU 143 ASN 144 -0.0003

ASN 144 VAL 145 0.0051

VAL 145 LEU 146 0.0001

LEU 146 LEU 147 -0.0004

LEU 147 ASP 148 0.0041

ASP 148 ALA 149 0.0002

ALA 149 HIS 150 -0.0003

HIS 150 MET 151 -0.0003

MET 151 ASN 152 0.0002

ASN 152 ALA 153 -0.0003

ALA 153 LYS 154 0.0014

LYS 154 ILE 155 -0.0000

ILE 155 ALA 156 -0.0001

ALA 156 ASP 157 0.0018

ASP 157 PHE 158 0.0002

PHE 158 GLY 159 0.0001

GLY 159 LEU 160 0.0068

LEU 160 SER 161 -0.0001

SER 161 ASN 162 -0.0002

ASN 162 MET 163 0.0218

MET 163 MET 164 0.0002

MET 164 SER 165 -0.0000

SER 165 ASP 166 0.0970

ASP 166 GLY 167 -0.0001

GLY 167 GLU 168 -0.0001

GLU 168 PHE 169 0.0525

PHE 169 LEU 170 -0.0004

LEU 170 ARG 171 0.0002

ARG 171 SER 173 0.0462

SER 173 CYS 174 -0.0001

CYS 174 GLY 175 0.0000

GLY 175 SER 176 0.0187

SER 176 PRO 177 -0.0003

PRO 177 ASN 178 0.0000

ASN 178 TYR 179 -0.0030

TYR 179 ALA 180 -0.0000

ALA 180 ALA 181 -0.0001

ALA 181 PRO 182 -0.0037

PRO 182 GLU 183 0.0000

GLU 183 VAL 184 -0.0002

VAL 184 ILE 185 0.0031

ILE 185 SER 186 0.0002

SER 186 GLY 187 0.0000

GLY 187 ARG 188 0.0110

ARG 188 LEU 189 0.0002

LEU 189 TYR 190 0.0003

TYR 190 ALA 191 -0.0009

ALA 191 GLY 192 0.0001

GLY 192 PRO 193 -0.0001

PRO 193 GLU 194 0.0155

GLU 194 VAL 195 -0.0002

VAL 195 ASP 196 0.0002

ASP 196 ILE 197 0.0079

ILE 197 TRP 198 -0.0004

TRP 198 SER 199 -0.0001

SER 199 SER 200 0.0023

SER 200 GLY 201 -0.0001

GLY 201 VAL 202 -0.0002

VAL 202 ILE 203 -0.0068

ILE 203 LEU 204 -0.0002

LEU 204 TYR 205 -0.0005

TYR 205 ALA 206 -0.0116

ALA 206 LEU 207 0.0002

LEU 207 LEU 208 -0.0001

LEU 208 CYS 209 0.0061

CYS 209 GLY 210 0.0002

GLY 210 THR 211 -0.0002

THR 211 LEU 212 0.0060

LEU 212 PRO 213 0.0004

PRO 213 PHE 214 0.0002

PHE 214 ASP 215 -0.0013

ASP 215 ASP 216 0.0001

ASP 216 ASP 217 0.0000

ASP 217 HIS 218 0.0011

HIS 218 VAL 219 0.0001

VAL 219 PRO 220 -0.0003

PRO 220 THR 221 0.0001

THR 221 LEU 222 0.0000

LEU 222 PHE 223 -0.0001

PHE 223 LYS 224 -0.0026

LYS 224 LYS 225 0.0000

LYS 225 ILE 226 -0.0003

ILE 226 CYS 227 -0.0035

CYS 227 ASP 228 -0.0000

ASP 228 GLY 229 0.0002

GLY 229 ILE 230 -0.0086

ILE 230 PHE 231 0.0002

PHE 231 TYR 232 -0.0002

TYR 232 THR 233 0.0065

THR 233 PRO 234 -0.0003

PRO 234 GLN 235 0.0001

GLN 235 TYR 236 0.0017

TYR 236 LEU 237 0.0001

LEU 237 ASN 238 0.0001

ASN 238 PRO 239 -0.0019

PRO 239 SER 240 0.0000

SER 240 VAL 241 -0.0000

VAL 241 ILE 242 0.0015

ILE 242 SER 243 -0.0002

SER 243 LEU 244 -0.0001

LEU 244 LEU 245 0.0080

LEU 245 LYS 246 0.0000

LYS 246 HIS 247 -0.0000

HIS 247 MET 248 0.0016

MET 248 LEU 249 -0.0001

LEU 249 GLN 250 0.0005

GLN 250 VAL 251 -0.0029

VAL 251 ASP 252 0.0001

ASP 252 PRO 253 0.0000

PRO 253 MET 254 -0.0041

MET 254 LYS 255 -0.0003

LYS 255 ARG 256 -0.0001

ARG 256 ALA 257 -0.0106

ALA 257 THR 258 0.0000

THR 258 ILE 259 -0.0001

ILE 259 LYS 260 0.0005

LYS 260 ASP 261 -0.0004

ASP 261 ILE 262 -0.0001

ILE 262 ARG 263 0.0024

ARG 263 GLU 264 -0.0001

GLU 264 HIS 265 -0.0002

HIS 265 GLU 266 -0.0010

GLU 266 TRP 267 -0.0003

TRP 267 PHE 268 -0.0000

PHE 268 LYS 269 0.0022

LYS 269 GLN 270 -0.0002

GLN 270 ASP 271 -0.0001

ASP 271 LEU 272 0.0004

LEU 272 PRO 273 0.0003

PRO 273 LYS 274 -0.0001

LYS 274 TYR 275 -0.0040

TYR 275 LEU 276 0.0001

LEU 276 PHE 277 -0.0003

PHE 277 PRO 278 0.0032

PRO 278 GLU 279 -0.0001

GLU 279 ASP 280 0.0002

ASP 280 ALA 321 0.1376

ALA 321 VAL 322 -0.0003

VAL 322 ALA 323 0.0001

ALA 323 TYR 324 0.0065

TYR 324 HIS 325 0.0001

HIS 325 LEU 326 0.0005

LEU 326 ILE 327 0.0162

ILE 327 ILE 328 0.0002

ILE 328 ASP 329 0.0000

ASP 329 ASN 330 0.0081

ASN 330 ARG 331 -0.0001

ARG 331 ARG 332 0.0002

ARG 332 ILE 333 0.0532

ILE 333 MET 334 0.0001

MET 334 ASN 335 -0.0000

ASN 335 GLU 336 0.0332

GLU 336 ALA 337 0.0004

ALA 337 LYS 338 -0.0000

LYS 338 ASP 339 0.0333

ASP 339 PHE 340 0.0000

PHE 340 TYR 341 0.0004

TYR 341 LEU 342 -0.0025

LEU 342 ALA 343 -0.0000

ALA 343 THR 344 -0.0001

THR 344 SER 345 -0.1021

SER 345 PRO 346 -0.0000

PRO 346 PRO 347 0.0001

PRO 347 ASP 348 -0.0835

ASP 348 SER 349 0.0002

SER 349 PHE 350 -0.0000

PHE 350 LEU 351 -0.0179

LEU 351 ASP 352 0.0002

ASP 352 ASP 353 -0.0000

ASP 353 HIS 354 -0.0033

HIS 354 HIS 355 0.0002

HIS 355 LEU 356 0.0000

LEU 356 THR 357 0.0701

THR 357 ARG 358 0.0001

ARG 358 PRO 359 0.0002

PRO 359 HIS 360 -0.0338

HIS 360 PRO 361 -0.0000

PRO 361 GLU 362 -0.0002

GLU 362 ARG 363 0.0318

ARG 363 VAL 364 0.0002

VAL 364 PRO 365 0.0001

PRO 365 PHE 366 0.0842

PHE 366 LEU 367 -0.0001

LEU 367 VAL 368 0.0002

VAL 368 ALA 369 0.0057

ALA 369 GLU 370 -0.0001

GLU 370 THR 371 0.0000

THR 371 PRO 372 -0.0324

PRO 372 ARG 373 -0.0001

ARG 373 ALA 374 0.0001

ALA 374 ALA 394 -1.2814

ALA 394 LYS 395 0.0001

LYS 395 TRP 396 -0.0001

TRP 396 HIS 397 -0.0125

HIS 397 LEU 398 -0.0000

LEU 398 GLY 399 -0.0002

GLY 399 ILE 400 -0.0065

ILE 400 ARG 401 -0.0000

ARG 401 SER 402 -0.0002

SER 402 GLN 403 0.0026

GLN 403 SER 404 0.0002

SER 404 ARG 405 -0.0001

ARG 405 PRO 406 0.0043

PRO 406 ASN 407 -0.0002

ASN 407 ASP 408 -0.0002

ASP 408 ILE 409 0.0013

ILE 409 MET 410 0.0000

MET 410 ALA 411 0.0000

ALA 411 GLU 412 0.0132

GLU 412 VAL 413 -0.0002

VAL 413 CYS 414 0.0003

CYS 414 ARG 415 0.0026

ARG 415 ALA 416 0.0000

ALA 416 ILE 417 0.0003

ILE 417 LYS 418 0.0015

LYS 418 GLN 419 0.0003

GLN 419 LEU 420 -0.0001

LEU 420 ASP 421 -0.0005

ASP 421 TYR 422 0.0001

TYR 422 GLU 423 0.0003

GLU 423 TRP 424 0.0042

TRP 424 LYS 425 0.0002

LYS 425 VAL 426 0.0000

VAL 426 VAL 427 0.0071

VAL 427 ASN 428 -0.0001

ASN 428 PRO 429 -0.0001

PRO 429 TYR 430 0.0001

TYR 430 TYR 431 0.0001

TYR 431 LEU 432 0.0003

LEU 432 ARG 433 -0.0007

ARG 433 VAL 434 -0.0000

VAL 434 ARG 435 0.0000

ARG 435 ARG 436 0.0034

ARG 436 LYS 437 0.0001

LYS 437 ASN 438 -0.0003

ASN 438 PRO 439 -0.0004

PRO 439 VAL 440 0.0001

VAL 440 THR 441 0.0001

THR 441 SER 442 0.0067

SER 442 THR 443 0.0003

THR 443 PHE 444 -0.0002

PHE 444 SER 445 0.0043

SER 445 LYS 446 0.0002

LYS 446 MET 447 -0.0001

MET 447 SER 448 0.0143

SER 448 LEU 449 -0.0000

LEU 449 GLN 450 -0.0004

GLN 450 LEU 451 -0.0001

LEU 451 TYR 452 0.0003

TYR 452 GLN 453 0.0000

GLN 453 VAL 454 0.0098

VAL 454 ASP 455 0.0001

ASP 455 SER 456 -0.0000

SER 456 ARG 457 -0.0010

ARG 457 THR 458 0.0002

THR 458 TYR 459 -0.0005

TYR 459 LEU 460 0.0007

LEU 460 LEU 461 -0.0002

LEU 461 ASP 462 -0.0003

ASP 462 PHE 463 0.0018

PHE 463 ARG 464 -0.0001

ARG 464 SER 465 0.0002

SER 465 ILE 466 -0.0075

ILE 466 ASP 467 0.0003

ASP 467 ASP 468 0.0001

ASP 468 GLU 469 0.0212

GLU 469 ILE 470 0.0001

ILE 470 LYS 203 0.0229

LYS 203 SER 204 -0.0003

SER 204 PRO 205 0.0001

PRO 205 PRO 206 0.0161

PRO 206 ILE 207 0.0003

ILE 207 LEU 208 -0.0001

LEU 208 PRO 209 -0.0334

PRO 209 PRO 210 -0.0000

PRO 210 HIS 211 -0.0001

HIS 211 LEU 212 -0.0622

LEU 212 LEU 213 -0.0001

LEU 213 GLN 214 -0.0002

GLN 214 VAL 215 -0.1069

VAL 215 ILE 216 0.0001

ILE 216 LEU 217 0.0001

LEU 217 ASN 218 0.0331

ASN 218 LYS 219 -0.0000

LYS 219 ASP 220 0.0002

ASP 220 THR 221 0.0241

THR 221 ASN 222 -0.0004

ASN 222 ILE 223 -0.0002

ILE 223 SER 224 -0.0008

SER 224 CYS 225 0.0002

CYS 225 ASP 226 -0.0001

ASP 226 PRO 227 0.0373

PRO 227 ALA 228 0.0003

ALA 228 LEU 229 -0.0001

LEU 229 LEU 230 0.0128

LEU 230 PRO 231 -0.0004

PRO 231 GLU 232 -0.0000

GLU 232 PRO 233 0.0702

PRO 233 ASN 234 0.0000

ASN 234 HIS 235 -0.0002

HIS 235 VAL 236 0.0161

VAL 236 MET 237 -0.0000

MET 237 LEU 238 -0.0001

LEU 238 ASN 239 0.0076

ASN 239 HIS 240 -0.0003

HIS 240 LEU 241 0.0003

LEU 241 TYR 242 0.0106

TYR 242 ALA 243 -0.0003

ALA 243 LEU 244 0.0003

LEU 244 SER 245 0.0057

SER 245 ILE 246 0.0001

ILE 246 LYS 247 -0.0003

LYS 247 ASP 248 -0.0058

ASP 248 SER 249 -0.0000

SER 249 VAL 250 0.0001

VAL 250 MET 251 0.0194

MET 251 VAL 252 -0.0006

VAL 252 LEU 253 0.0002

LEU 253 SER 254 0.0077

SER 254 ALA 255 0.0001

ALA 255 THR 256 0.0005

THR 256 HIS 257 0.0041

HIS 257 ARG 258 0.0000

ARG 258 TYR 259 0.0003

TYR 259 LYS 260 -0.0008

LYS 260 LYS 261 0.0004

LYS 261 LYS 262 -0.0001

LYS 262 TYR 263 0.0115

TYR 263 VAL 264 -0.0005

VAL 264 THR 265 -0.0000

THR 265 THR 266 -0.0336

THR 266 LEU 267 0.0000

LEU 267 LEU 268 0.0002

LEU 268 TYR 269 -0.0044

TYR 269 LYS 270 -0.0001

LYS 270 PRO 271 0.0002

PRO 271 PRO 528 -0.0154

PRO 528 GLY 529 -0.0001

GLY 529 SER 530 -0.0002

SER 530 HIS 531 0.0091

HIS 531 THR 532 0.0001

THR 532 ILE 533 -0.0002

ILE 533 GLU 534 -0.0002

GLU 534 PHE 535 0.0002

PHE 535 PHE 536 0.0000

PHE 536 GLU 537 -0.0002

GLU 537 MET 538 -0.0000

MET 538 CYS 539 0.0002

CYS 539 ALA 540 0.0074

ALA 540 ASN 541 0.0001

ASN 541 LEU 542 -0.0003

LEU 542 ILE 543 -0.0066

ILE 543 LYS 544 0.0001

LYS 544 ILE 545 -0.0002

ILE 545 LEU 546 -0.0017

LEU 546 ALA 547 -0.0004

ALA 547 GLN 548 0.0003

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.

*** Apo AMPK ***

CA strain for 260711175133601569

--- normal mode 11 ---

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

* Apo AMPK *