Should you encounter any unexpected behaviour,
please let us know.

* AEPR2skrt *

CA strain for 2403060955371871371

--- normal mode 10 ---

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
MET 1 ALA 2 0.0000

ALA 2 ALA 3 -0.0002

ALA 3 ARG 4 -0.0002

ARG 4 TRP 5 -0.0001

TRP 5 CYS 6 0.0001

CYS 6 PHE 7 0.0012

PHE 7 ALA 8 -0.0001

ALA 8 LEU 9 0.0000

LEU 9 LEU 10 0.0039

LEU 10 LEU 11 -0.0002

LEU 11 ALA 12 0.0000

ALA 12 LEU 13 -0.0031

LEU 13 SER 14 -0.0001

SER 14 ALA 15 0.0002

ALA 15 ALA 16 -0.0106

ALA 16 ALA 17 -0.0003

ALA 17 ALA 18 -0.0000

ALA 18 GLY 19 -0.0538

GLY 19 ALA 20 -0.0002

ALA 20 GLY 21 0.0003

GLY 21 ALA 22 -0.0309

ALA 22 LYS 23 -0.0002

LYS 23 ARG 24 0.0002

ARG 24 THR 25 -0.0267

THR 25 TRP 26 0.0002

TRP 26 GLU 27 0.0002

GLU 27 PRO 28 0.0222

PRO 28 VAL 29 -0.0001

VAL 29 ILE 30 -0.0002

ILE 30 ARG 31 -0.0048

ARG 31 MET 32 0.0001

MET 32 PRO 33 0.0003

PRO 33 GLY 34 0.0026

GLY 34 GLU 35 0.0002

GLU 35 VAL 36 -0.0002

VAL 36 VAL 37 -0.0041

VAL 37 GLU 38 -0.0000

GLU 38 GLU 39 0.0000

GLU 39 GLU 40 -0.0071

GLU 40 VAL 41 0.0000

VAL 41 ALA 42 -0.0002

ALA 42 THR 43 -0.0040

THR 43 VAL 44 0.0001

VAL 44 PRO 45 -0.0000

PRO 45 ARG 46 -0.0016

ARG 46 GLY 47 0.0002

GLY 47 SER 48 -0.0002

SER 48 GLU 49 -0.0011

GLU 49 GLY 50 0.0001

GLY 50 THR 51 -0.0002

THR 51 GLU 52 -0.0002

GLU 52 GLU 53 0.0001

GLU 53 GLU 54 -0.0002

GLU 54 GLU 55 -0.0003

GLU 55 LYS 56 0.0001

LYS 56 ASP 57 -0.0001

ASP 57 GLY 58 0.0004

GLY 58 VAL 59 -0.0004

VAL 59 GLY 60 0.0002

GLY 60 THR 61 -0.0001

THR 61 ARG 62 0.0001

ARG 62 TRP 63 -0.0000

TRP 63 ALA 64 -0.0000

ALA 64 VAL 65 0.0002

VAL 65 LEU 66 -0.0004

LEU 66 VAL 67 0.0006

VAL 67 ALA 68 -0.0001

ALA 68 GLY 69 0.0000

GLY 69 SER 70 -0.0001

SER 70 SER 71 -0.0000

SER 71 GLY 72 0.0001

GLY 72 TYR 73 0.0009

TYR 73 GLY 74 0.0000

GLY 74 ASN 75 0.0002

ASN 75 TYR 76 0.0008

TYR 76 ARG 77 0.0004

ARG 77 HIS 78 0.0001

HIS 78 GLN 79 0.0001

GLN 79 ALA 80 -0.0002

ALA 80 ASP 81 -0.0002

ASP 81 VAL 82 -0.0008

VAL 82 CYS 83 -0.0000

CYS 83 HIS 84 0.0000

HIS 84 ALA 85 -0.0004

ALA 85 TYR 86 0.0002

TYR 86 GLN 87 0.0000

GLN 87 ILE 88 0.0011

ILE 88 LEU 89 0.0002

LEU 89 ARG 90 -0.0001

ARG 90 LYS 91 -0.0001

LYS 91 GLY 92 0.0000

GLY 92 GLY 93 0.0004

GLY 93 LEU 94 -0.0004

LEU 94 LYS 95 0.0001

LYS 95 GLU 96 -0.0000

GLU 96 GLU 97 -0.0001

GLU 97 ASN 98 -0.0001

ASN 98 ILE 99 -0.0004

ILE 99 VAL 100 0.0003

VAL 100 VAL 101 -0.0000

VAL 101 PHE 102 0.0006

PHE 102 MET 103 0.0006

MET 103 TYR 104 0.0004

TYR 104 ASP 105 -0.0002

ASP 105 ASP 106 0.0022

ASP 106 ILE 107 0.0002

ILE 107 ALA 108 -0.0001

ALA 108 ASN 109 0.0007

ASN 109 ASN 110 0.0005

ASN 110 ILE 111 -0.0002

ILE 111 LEU 112 0.0008

LEU 112 ASN 113 -0.0002

ASN 113 PRO 114 0.0002

PRO 114 ARG 115 0.0009

ARG 115 PRO 116 -0.0002

PRO 116 GLY 117 -0.0003

GLY 117 VAL 118 0.0007

VAL 118 ILE 119 -0.0003

ILE 119 VAL 120 0.0004

VAL 120 ASN 121 0.0010

ASN 121 HIS 122 0.0001

HIS 122 PRO 123 -0.0002

PRO 123 GLN 124 -0.0009

GLN 124 GLY 125 -0.0003

GLY 125 GLU 126 -0.0000

GLU 126 ASP 127 -0.0024

ASP 127 VAL 128 0.0003

VAL 128 TYR 129 0.0001

TYR 129 ALA 130 0.0003

ALA 130 GLY 131 0.0003

GLY 131 VAL 132 0.0001

VAL 132 PRO 133 -0.0010

PRO 133 LYS 134 -0.0000

LYS 134 ASP 135 -0.0004

ASP 135 TYR 136 -0.0000

TYR 136 THR 137 -0.0004

THR 137 GLY 138 -0.0000

GLY 138 ASP 139 -0.0009

ASP 139 GLU 140 -0.0002

GLU 140 VAL 141 0.0004

VAL 141 THR 142 -0.0008

THR 142 GLU 143 0.0002

GLU 143 LYS 144 -0.0001

LYS 144 ASN 145 0.0001

ASN 145 PHE 146 -0.0001

PHE 146 TYR 147 -0.0002

TYR 147 ALA 148 -0.0000

ALA 148 VAL 149 -0.0005

VAL 149 LEU 150 -0.0001

LEU 150 LEU 151 0.0003

LEU 151 GLY 152 0.0002

GLY 152 ASN 153 0.0002

ASN 153 LYS 154 -0.0001

LYS 154 THR 155 -0.0000

THR 155 ALA 156 0.0002

ALA 156 VAL 157 0.0003

VAL 157 THR 158 -0.0002

THR 158 GLY 159 0.0002

GLY 159 GLY 160 -0.0002

GLY 160 SER 161 0.0001

SER 161 ARG 162 -0.0001

ARG 162 LYS 163 -0.0003

LYS 163 VAL 164 0.0004

VAL 164 ILE 165 0.0001

ILE 165 ASP 166 0.0002

ASP 166 SER 167 0.0002

SER 167 LYS 168 0.0001

LYS 168 PRO 169 0.0002

PRO 169 ASN 170 -0.0001

ASN 170 ASP 171 0.0003

ASP 171 HIS 172 -0.0007

HIS 172 ILE 173 0.0000

ILE 173 PHE 174 0.0001

PHE 174 ILE 175 0.0005

ILE 175 PHE 176 -0.0006

PHE 176 TYR 177 -0.0001

TYR 177 SER 178 0.0000

SER 178 ASP 179 0.0002

ASP 179 HIS 180 0.0001

HIS 180 GLY 181 -0.0001

GLY 181 GLY 182 0.0000

GLY 182 PRO 183 -0.0000

PRO 183 GLY 184 0.0001

GLY 184 VAL 185 0.0002

VAL 185 LEU 186 0.0000

LEU 186 GLY 187 -0.0002

GLY 187 MET 188 -0.0005

MET 188 PRO 189 0.0002

PRO 189 ASN 190 -0.0009

ASN 190 LEU 191 0.0001

LEU 191 PRO 192 0.0001

PRO 192 TYR 193 0.0002

TYR 193 LEU 194 -0.0000

LEU 194 TYR 195 -0.0001

TYR 195 ALA 196 0.0006

ALA 196 ALA 197 0.0001

ALA 197 ASP 198 0.0003

ASP 198 PHE 199 -0.0005

PHE 199 MET 200 -0.0000

MET 200 LYS 201 0.0005

LYS 201 VAL 202 -0.0001

VAL 202 LEU 203 0.0002

LEU 203 GLN 204 -0.0001

GLN 204 GLU 205 -0.0002

GLU 205 LYS 206 -0.0000

LYS 206 HIS 207 0.0001

HIS 207 ALA 208 0.0003

ALA 208 SER 209 0.0000

SER 209 ASN 210 0.0002

ASN 210 THR 211 0.0002

THR 211 TYR 212 -0.0001

TYR 212 ALA 213 -0.0000

ALA 213 LYS 214 -0.0004

LYS 214 MET 215 0.0003

MET 215 VAL 216 0.0002

VAL 216 ILE 217 0.0001

ILE 217 TYR 218 0.0001

TYR 218 VAL 219 0.0000

VAL 219 GLU 220 -0.0003

GLU 220 ALA 221 0.0001

ALA 221 CYS 222 -0.0001

CYS 222 GLU 223 0.0001

GLU 223 SER 224 0.0003

SER 224 GLY 225 0.0002

GLY 225 SER 226 0.0005

SER 226 ILE 227 -0.0004

ILE 227 PHE 228 0.0001

PHE 228 GLU 229 -0.0000

GLU 229 GLY 230 -0.0002

GLY 230 LEU 231 -0.0002

LEU 231 MET 232 0.0003

MET 232 PRO 233 0.0000

PRO 233 GLU 234 0.0000

GLU 234 ASP 235 0.0002

ASP 235 LEU 236 -0.0001

LEU 236 ASN 237 -0.0001

ASN 237 ILE 238 -0.0006

ILE 238 TYR 239 -0.0001

TYR 239 VAL 240 -0.0003

VAL 240 THR 241 -0.0005

THR 241 THR 242 -0.0003

THR 242 ALA 243 0.0002

ALA 243 SER 244 0.0007

SER 244 ASN 245 -0.0001

ASN 245 ALA 246 0.0001

ALA 246 GLU 247 0.0000

GLU 247 GLU 248 0.0001

GLU 248 SER 249 -0.0003

SER 249 SER 250 0.0007

SER 250 TRP 251 -0.0004

TRP 251 GLY 252 0.0003

GLY 252 THR 253 0.0021

THR 253 TYR 254 -0.0003

TYR 254 CYS 255 0.0003

CYS 255 PRO 256 -0.0011

PRO 256 GLY 257 0.0002

GLY 257 MET 258 0.0004

MET 258 GLU 259 -0.0010

GLU 259 PRO 260 -0.0002

PRO 260 SER 261 0.0002

SER 261 PRO 262 -0.0003

PRO 262 PRO 263 -0.0003

PRO 263 SER 264 0.0005

SER 264 GLU 265 -0.0007

GLU 265 TYR 266 0.0003

TYR 266 ILE 267 -0.0002

ILE 267 THR 268 0.0010

THR 268 CYS 269 0.0002

CYS 269 LEU 270 -0.0000

LEU 270 GLY 271 0.0009

GLY 271 ASP 272 -0.0001

ASP 272 LEU 273 0.0000

LEU 273 TYR 274 -0.0019

TYR 274 SER 275 -0.0000

SER 275 VAL 276 0.0002

VAL 276 SER 277 0.0007

SER 277 TRP 278 -0.0002

TRP 278 MET 279 0.0000

MET 279 GLU 280 0.0006

GLU 280 ASP 281 0.0001

ASP 281 SER 282 0.0001

SER 282 GLU 283 0.0011

GLU 283 THR 284 -0.0001

THR 284 HIS 285 -0.0002

HIS 285 ASN 286 -0.0014

ASN 286 LEU 287 -0.0001

LEU 287 LYS 288 0.0001

LYS 288 GLU 289 0.0003

GLU 289 GLU 290 -0.0000

GLU 290 SER 291 0.0003

SER 291 ILE 292 0.0000

ILE 292 LYS 293 -0.0001

LYS 293 LYS 294 0.0001

LYS 294 GLN 295 -0.0000

GLN 295 TYR 296 -0.0001

TYR 296 GLU 297 -0.0000

GLU 297 MET 298 -0.0002

MET 298 VAL 299 -0.0003

VAL 299 LYS 300 0.0001

LYS 300 LYS 301 -0.0002

LYS 301 ARG 302 -0.0003

ARG 302 THR 303 0.0003

THR 303 SER 304 0.0005

SER 304 ASP 305 0.0001

ASP 305 MET 306 -0.0002

MET 306 ASN 307 0.0007

ASN 307 SER 308 0.0004

SER 308 TYR 309 0.0002

TYR 309 GLY 310 -0.0023

GLY 310 ALA 311 -0.0002

ALA 311 GLY 312 -0.0000

GLY 312 SER 313 -0.0031

SER 313 HIS 314 0.0001

HIS 314 VAL 315 -0.0000

VAL 315 MET 316 -0.0004

MET 316 GLU 317 -0.0004

GLU 317 TYR 318 -0.0000

TYR 318 GLY 319 -0.0004

GLY 319 ASP 320 0.0000

ASP 320 ARG 321 0.0002

ARG 321 THR 322 0.0002

THR 322 PHE 323 -0.0000

PHE 323 LYS 324 -0.0001

LYS 324 ASP 325 -0.0001

ASP 325 ASP 326 0.0000

ASP 326 LYS 327 -0.0000

LYS 327 LEU 328 0.0005

LEU 328 TYR 329 -0.0002

TYR 329 LEU 330 -0.0003

LEU 330 TYR 331 0.0001

TYR 331 GLN 332 -0.0002

GLN 332 GLY 333 -0.0001

GLY 333 PHE 334 0.0002

PHE 334 ASP 335 -0.0001

ASP 335 PRO 336 -0.0003

PRO 336 ALA 337 -0.0000

ALA 337 ASN 338 -0.0001

ASN 338 ALA 339 0.0001

ALA 339 GLU 340 0.0002

GLU 340 VAL 341 0.0002

VAL 341 LYS 342 -0.0001

LYS 342 ASN 343 -0.0012

ASN 343 LYS 344 -0.0002

LYS 344 LEU 345 -0.0000

LEU 345 SER 346 -0.0012

SER 346 TRP 347 -0.0000

TRP 347 GLU 348 0.0002

GLU 348 GLY 349 0.0007

GLY 349 PRO 350 0.0002

PRO 350 LYS 351 -0.0003

LYS 351 ALA 352 -0.0024

ALA 352 ALA 353 0.0005

ALA 353 VAL 354 -0.0002

VAL 354 ASN 355 0.0035

ASN 355 GLN 356 -0.0002

GLN 356 ARG 357 -0.0001

ARG 357 ASP 358 0.0023

ASP 358 ALA 359 -0.0001

ALA 359 ASP 360 0.0003

ASP 360 LEU 361 0.0011

LEU 361 LEU 362 0.0001

LEU 362 PHE 363 -0.0003

PHE 363 LEU 364 -0.0000

LEU 364 TRP 365 0.0001

TRP 365 ARG 366 -0.0006

ARG 366 ARG 367 -0.0030

ARG 367 TYR 368 0.0002

TYR 368 GLU 369 0.0002

GLU 369 LEU 370 -0.0015

LEU 370 LEU 371 0.0003

LEU 371 HIS 372 0.0000

HIS 372 ASP 373 0.0005

ASP 373 LYS 374 -0.0002

LYS 374 SER 375 -0.0001

SER 375 GLU 376 -0.0007

GLU 376 GLU 377 0.0002

GLU 377 LYS 378 0.0001

LYS 378 LEU 379 0.0004

LEU 379 LYS 380 -0.0001

LYS 380 ALA 381 0.0002

ALA 381 LEU 382 -0.0003

LEU 382 ARG 383 0.0001

ARG 383 GLU 384 0.0000

GLU 384 ILE 385 -0.0002

ILE 385 SER 386 -0.0002

SER 386 ASP 387 -0.0000

ASP 387 THR 388 -0.0010

THR 388 VAL 389 0.0002

VAL 389 MET 390 0.0004

MET 390 HIS 391 0.0021

HIS 391 ARG 392 0.0004

ARG 392 LYS 393 -0.0000

LYS 393 LEU 394 0.0024

LEU 394 LEU 395 0.0003

LEU 395 ASP 396 0.0000

ASP 396 SER 397 0.0012

SER 397 SER 398 0.0002

SER 398 VAL 399 0.0000

VAL 399 ASP 400 0.0003

ASP 400 LEU 401 0.0002

LEU 401 VAL 402 -0.0001

VAL 402 GLY 403 -0.0002

GLY 403 LYS 404 0.0004

LYS 404 LEU 405 -0.0003

LEU 405 LEU 406 -0.0003

LEU 406 PHE 407 -0.0001

PHE 407 GLY 408 0.0003

GLY 408 PHE 409 -0.0006

PHE 409 GLY 410 0.0005

GLY 410 ASN 411 -0.0001

ASN 411 GLY 412 -0.0000

GLY 412 PRO 413 0.0002

PRO 413 SER 414 0.0002

SER 414 VAL 415 -0.0005

VAL 415 LEU 416 0.0003

LEU 416 GLN 417 -0.0003

GLN 417 ALA 418 -0.0009

ALA 418 VAL 419 -0.0001

VAL 419 ARG 420 0.0001

ARG 420 PRO 421 0.0001

PRO 421 SER 422 -0.0001

SER 422 GLY 423 -0.0001

GLY 423 GLN 424 -0.0001

GLN 424 PRO 425 0.0002

PRO 425 LEU 426 0.0001

LEU 426 VAL 427 0.0004

VAL 427 ASP 428 0.0003

ASP 428 ASP 429 -0.0003

ASP 429 TRP 430 -0.0003

TRP 430 ASP 431 -0.0001

ASP 431 CYS 432 0.0003

CYS 432 LEU 433 -0.0001

LEU 433 LYS 434 0.0000

LYS 434 ARG 435 0.0003

ARG 435 MET 436 -0.0000

MET 436 VAL 437 0.0007

VAL 437 ARG 438 -0.0003

ARG 438 ILE 439 -0.0011

ILE 439 PHE 440 -0.0000

PHE 440 GLU 441 0.0000

GLU 441 SER 442 -0.0005

SER 442 HIS 443 -0.0000

HIS 443 CYS 444 0.0001

CYS 444 GLY 445 -0.0007

GLY 445 PRO 446 -0.0001

PRO 446 LEU 447 0.0001

LEU 447 THR 448 -0.0008

THR 448 GLN 449 0.0003

GLN 449 TYR 450 0.0004

TYR 450 GLY 451 -0.0002

GLY 451 MET 452 0.0004

MET 452 LYS 453 -0.0002

LYS 453 HIS 454 0.0010

HIS 454 MET 455 -0.0001

MET 455 ARG 456 -0.0002

ARG 456 ALA 457 0.0008

ALA 457 PHE 458 -0.0000

PHE 458 ALA 459 -0.0001

ALA 459 ASN 460 0.0001

ASN 460 ILE 461 -0.0000

ILE 461 CYS 462 -0.0000

CYS 462 ASN 463 -0.0002

ASN 463 ASN 464 -0.0002

ASN 464 GLY 465 0.0002

GLY 465 ILE 466 0.0005

ILE 466 SER 467 0.0003

SER 467 GLY 468 0.0000

GLY 468 ALA 469 -0.0004

ALA 469 SER 470 0.0000

SER 470 MET 471 -0.0003

MET 471 LYS 472 0.0005

LYS 472 GLU 473 -0.0002

GLU 473 ALA 474 -0.0001

ALA 474 SER 475 0.0002

SER 475 ILE 476 -0.0000

ILE 476 ALA 477 -0.0002

ALA 477 THR 478 0.0005

THR 478 CYS 479 0.0001

CYS 479 SER 480 0.0004

SER 480 SER 481 0.0004

SER 481 HIS 482 0.0001

HIS 482 ASN 483 0.0004

ASN 483 SER 484 -0.0005

SER 484 GLY 485 0.0002

GLY 485 ARG 486 0.0001

ARG 486 TRP 487 -0.0006

TRP 487 SER 488 -0.0000

SER 488 SER 489 -0.0001

SER 489 LEU 490 0.0003

LEU 490 VAL 491 -0.0000

VAL 491 GLN 492 0.0003

GLN 492 GLY 493 0.0022

GLY 493 TYR 494 0.0003

TYR 494 SER 495 -0.0004

SER 495 ALA 496 0.0010

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** AEPR2skrt ***

CA strain for 2403060955371871371

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.

* AEPR2skrt *