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

* AlphaFold *

CA strain for 23010308584016806

--- normal mode 7 ---

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 0.0001

ALA 2 ARG 3 -0.0000

ARG 3 MET 4 -0.0021

MET 4 ASN 5 -0.0003

ASN 5 GLU 6 -0.0000

GLU 6 PHE 7 -0.0011

PHE 7 LYS 8 0.0001

LYS 8 THR 9 -0.0003

THR 9 GLN 10 -0.0002

GLN 10 ASN 11 -0.0001

ASN 11 ALA 12 -0.0002

ALA 12 THR 13 -0.0006

THR 13 GLU 14 -0.0002

GLU 14 THR 15 0.0002

THR 15 GLN 16 0.0064

GLN 16 LEU 17 -0.0001

LEU 17 LEU 18 -0.0003

LEU 18 ASP 19 0.0049

ASP 19 GLU 20 -0.0003

GLU 20 GLY 21 -0.0000

GLY 21 ASP 22 -0.0144

ASP 22 ILE 23 -0.0001

ILE 23 LEU 24 0.0002

LEU 24 GLU 25 -0.0022

GLU 25 ARG 26 -0.0001

ARG 26 VAL 27 -0.0002

VAL 27 ILE 28 0.0001

ILE 28 SER 29 -0.0003

SER 29 ALA 30 -0.0003

ALA 30 THR 31 -0.0002

THR 31 LYS 32 -0.0004

LYS 32 GLN 33 0.0004

GLN 33 THR 34 -0.0002

THR 34 SER 35 0.0003

SER 35 ALA 36 -0.0002

ALA 36 ASP 37 0.0001

ASP 37 ASP 38 -0.0001

ASP 38 THR 39 0.0001

THR 39 ARG 40 0.0005

ARG 40 ASP 41 0.0000

ASP 41 LEU 42 -0.0002

LEU 42 ILE 43 -0.0003

ILE 43 ARG 44 0.0001

ARG 44 ASN 45 -0.0001

ASN 45 LEU 46 -0.0008

LEU 46 VAL 47 -0.0002

VAL 47 GLU 48 -0.0001

GLU 48 GLU 49 0.0003

GLU 49 VAL 50 0.0002

VAL 50 GLN 51 0.0001

GLN 51 GLU 52 -0.0069

GLU 52 GLY 53 -0.0000

GLY 53 THR 54 0.0003

THR 54 VAL 55 0.0019

VAL 55 VAL 56 -0.0003

VAL 56 TRP 57 0.0003

TRP 57 ASP 58 -0.0002

ASP 58 ARG 59 0.0003

ARG 59 ASN 60 0.0001

ASN 60 ILE 61 0.0002

ILE 61 ALA 62 0.0000

ALA 62 LYS 63 -0.0002

LYS 63 THR 64 -0.0003

THR 64 ILE 65 0.0001

ILE 65 ASN 66 0.0002

ASN 66 ARG 67 0.0006

ARG 67 ALA 68 0.0002

ALA 68 ILE 69 0.0003

ILE 69 ALA 70 0.0017

ALA 70 GLN 71 0.0000

GLN 71 ILE 72 -0.0002

ILE 72 ASP 73 -0.0008

ASP 73 SER 74 -0.0003

SER 74 LYS 75 -0.0004

LYS 75 ILE 76 -0.0007

ILE 76 SER 77 -0.0000

SER 77 SER 78 0.0000

SER 78 GLN 79 -0.0012

GLN 79 LEU 80 0.0002

LEU 80 ALA 81 -0.0001

ALA 81 GLU 82 0.0002

GLU 82 ILE 83 -0.0004

ILE 83 MET 84 0.0002

MET 84 HIS 85 0.0006

HIS 85 ALA 86 0.0002

ALA 86 ASP 87 0.0002

ASP 87 ASP 88 0.0001

ASP 88 PHE 89 0.0002

PHE 89 LYS 90 -0.0002

LYS 90 LYS 91 0.0001

LYS 91 LEU 92 -0.0001

LEU 92 GLU 93 -0.0003

GLU 93 GLY 94 0.0002

GLY 94 SER 95 -0.0000

SER 95 TRP 96 0.0002

TRP 96 ARG 97 -0.0002

ARG 97 GLY 98 0.0000

GLY 98 LEU 99 -0.0000

LEU 99 SER 100 -0.0001

SER 100 TYR 101 0.0000

TYR 101 LEU 102 0.0001

LEU 102 VAL 103 0.0000

VAL 103 HIS 104 0.0001

HIS 104 ASN 105 0.0002

ASN 105 SER 106 -0.0002

SER 106 GLU 107 0.0002

GLU 107 THR 108 0.0003

THR 108 ASN 109 0.0002

ASN 109 ALA 110 -0.0002

ALA 110 ASN 111 0.0002

ASN 111 LEU 112 -0.0001

LEU 112 LYS 113 -0.0002

LYS 113 ILE 114 0.0001

ILE 114 ARG 115 -0.0002

ARG 115 VAL 116 0.0000

VAL 116 LEU 117 -0.0001

LEU 117 ASN 118 -0.0002

ASN 118 LEU 119 -0.0004

LEU 119 THR 120 0.0001

THR 120 LYS 121 -0.0001

LYS 121 ARG 122 -0.0000

ARG 122 GLU 123 0.0000

GLU 123 LEU 124 -0.0002

LEU 124 TYR 125 0.0002

TYR 125 LYS 126 0.0002

LYS 126 ASP 127 -0.0001

ASP 127 LEU 128 0.0001

LEU 128 ASP 129 0.0001

ASP 129 ARG 130 0.0001

ARG 130 ALA 131 0.0002

ALA 131 VAL 132 -0.0001

VAL 132 GLU 133 -0.0000

GLU 133 PHE 134 0.0001

PHE 134 ASP 135 0.0001

ASP 135 GLN 136 -0.0002

GLN 136 SER 137 0.0001

SER 137 GLU 138 -0.0003

GLU 138 THR 139 -0.0001

THR 139 PHE 140 -0.0001

PHE 140 LYS 141 0.0001

LYS 141 LYS 142 0.0001

LYS 142 ILE 143 -0.0000

ILE 143 TYR 144 -0.0001

TYR 144 GLU 145 0.0005

GLU 145 SER 146 0.0000

SER 146 GLU 147 0.0001

GLU 147 PHE 148 0.0001

PHE 148 GLY 149 0.0003

GLY 149 THR 150 0.0001

THR 150 PRO 151 0.0003

PRO 151 GLY 152 -0.0003

GLY 152 GLY 153 0.0001

GLY 153 GLU 154 0.0002

GLU 154 PRO 155 -0.0001

PRO 155 TYR 156 0.0004

TYR 156 GLY 157 0.0001

GLY 157 ALA 158 -0.0001

ALA 158 VAL 159 0.0001

VAL 159 ILE 160 0.0000

ILE 160 GLY 161 0.0004

GLY 161 ASP 162 0.0001

ASP 162 PHE 163 -0.0001

PHE 163 GLU 164 0.0003

GLU 164 PHE 165 -0.0002

PHE 165 THR 166 -0.0001

THR 166 ASN 167 0.0000

ASN 167 HIS 168 -0.0001

HIS 168 PRO 169 -0.0001

PRO 169 GLU 170 0.0005

GLU 170 ASP 171 -0.0001

ASP 171 ILE 172 0.0003

ILE 172 GLU 173 -0.0004

GLU 173 LEU 174 0.0004

LEU 174 LEU 175 0.0000

LEU 175 SER 176 0.0001

SER 176 LYS 177 -0.0001

LYS 177 MET 178 -0.0002

MET 178 SER 179 -0.0000

SER 179 ASN 180 0.0004

ASN 180 VAL 181 -0.0000

VAL 181 ALA 182 -0.0002

ALA 182 ALA 183 0.0002

ALA 183 SER 184 -0.0001

SER 184 ALA 185 -0.0004

ALA 185 PHE 186 -0.0001

PHE 186 CYS 187 -0.0002

CYS 187 PRO 188 -0.0002

PRO 188 PHE 189 0.0000

PHE 189 ILE 190 0.0000

ILE 190 SER 191 0.0002

SER 191 ALA 192 -0.0001

ALA 192 ALA 193 0.0001

ALA 193 ASP 194 -0.0002

ASP 194 HIS 195 -0.0001

HIS 195 SER 196 -0.0003

SER 196 LEU 197 0.0004

LEU 197 PHE 198 -0.0000

PHE 198 GLY 199 -0.0004

GLY 199 LEU 200 -0.0001

LEU 200 GLU 201 0.0001

GLU 201 SER 202 0.0002

SER 202 TRP 203 -0.0003

TRP 203 ASN 204 0.0004

ASN 204 GLU 205 -0.0004

GLU 205 LEU 206 0.0001

LEU 206 SER 207 -0.0002

SER 207 ARG 208 -0.0001

ARG 208 PRO 209 -0.0001

PRO 209 ARG 210 0.0001

ARG 210 ASP 211 -0.0002

ASP 211 LEU 212 0.0003

LEU 212 GLU 213 0.0001

GLU 213 LYS 214 -0.0002

LYS 214 VAL 215 -0.0001

VAL 215 PHE 216 -0.0002

PHE 216 ASP 217 0.0000

ASP 217 SER 218 0.0002

SER 218 LYS 219 0.0000

LYS 219 GLU 220 -0.0004

GLU 220 TYR 221 0.0000

TYR 221 ILE 222 0.0002

ILE 222 LYS 223 -0.0001

LYS 223 TRP 224 0.0001

TRP 224 ARG 225 0.0000

ARG 225 SER 226 0.0003

SER 226 PHE 227 -0.0001

PHE 227 ARG 228 -0.0002

ARG 228 ASP 229 0.0000

ASP 229 SER 230 0.0002

SER 230 GLU 231 -0.0002

GLU 231 ASP 232 0.0001

ASP 232 SER 233 0.0001

SER 233 ARG 234 0.0001

ARG 234 PHE 235 -0.0003

PHE 235 VAL 236 -0.0001

VAL 236 SER 237 0.0004

SER 237 LEU 238 -0.0002

LEU 238 THR 239 -0.0001

THR 239 LEU 240 0.0001

LEU 240 PRO 241 -0.0002

PRO 241 ARG 242 0.0003

ARG 242 THR 243 0.0001

THR 243 LEU 244 0.0000

LEU 244 ALA 245 -0.0001

ALA 245 ARG 246 0.0001

ARG 246 LEU 247 -0.0003

LEU 247 PRO 248 0.0001

PRO 248 TYR 249 0.0002

TYR 249 GLY 250 0.0002

GLY 250 SER 251 -0.0000

SER 251 ASP 252 0.0000

ASP 252 THR 253 -0.0003

THR 253 LEU 254 0.0003

LEU 254 SER 255 0.0001

SER 255 VAL 256 0.0009

VAL 256 GLU 257 -0.0001

GLU 257 ALA 258 0.0003

ALA 258 PHE 259 -0.0000

PHE 259 ASN 260 -0.0001

ASN 260 TYR 261 0.0002

TYR 261 GLU 262 -0.0002

GLU 262 GLU 263 0.0001

GLU 263 ALA 264 0.0000

ALA 264 LEU 265 0.0011

LEU 265 LYS 266 -0.0003

LYS 266 THR 267 -0.0001

THR 267 PRO 268 -0.0001

PRO 268 ASP 269 -0.0004

ASP 269 GLY 270 0.0002

GLY 270 LYS 271 0.0002

LYS 271 ALA 272 -0.0001

ALA 272 LEU 273 0.0003

LEU 273 PRO 274 0.0002

PRO 274 LEU 275 -0.0001

LEU 275 PRO 276 0.0002

PRO 276 HIS 277 -0.0010

HIS 277 GLU 278 0.0004

GLU 278 ASP 279 -0.0000

ASP 279 TYR 280 0.0003

TYR 280 CYS 281 0.0003

CYS 281 TRP 282 -0.0001

TRP 282 MET 283 0.0000

MET 283 ASN 284 -0.0001

ASN 284 ALA 285 0.0002

ALA 285 ALA 286 -0.0001

ALA 286 TYR 287 0.0003

TYR 287 VAL 288 0.0001

VAL 288 MET 289 -0.0000

MET 289 GLY 290 -0.0000

GLY 290 THR 291 -0.0000

THR 291 ARG 292 -0.0002

ARG 292 LEU 293 0.0001

LEU 293 THR 294 -0.0004

THR 294 HIS 295 -0.0003

HIS 295 SER 296 0.0000

SER 296 PHE 297 0.0002

PHE 297 SER 298 -0.0002

SER 298 THR 299 0.0001

THR 299 THR 300 -0.0001

THR 300 GLY 301 -0.0002

GLY 301 TRP 302 0.0003

TRP 302 CYS 303 -0.0005

CYS 303 THR 304 0.0002

THR 304 SER 305 -0.0002

SER 305 ILE 306 -0.0000

ILE 306 ARG 307 -0.0004

ARG 307 GLY 308 -0.0000

GLY 308 ALA 309 -0.0000

ALA 309 GLU 310 0.0001

GLU 310 GLY 311 0.0002

GLY 311 GLY 312 0.0000

GLY 312 GLY 313 0.0006

GLY 313 LYS 314 0.0002

LYS 314 VAL 315 -0.0000

VAL 315 GLU 316 -0.0002

GLU 316 ASN 317 -0.0001

ASN 317 LEU 318 0.0001

LEU 318 PRO 319 0.0006

PRO 319 ALA 320 -0.0002

ALA 320 HIS 321 0.0004

HIS 321 ILE 322 0.0002

ILE 322 PHE 323 -0.0001

PHE 323 THR 324 0.0000

THR 324 SER 325 0.0003

SER 325 ASP 326 0.0002

ASP 326 ASP 327 0.0000

ASP 327 GLY 328 -0.0001

GLY 328 ASP 329 0.0002

ASP 329 LEU 330 -0.0004

LEU 330 ASP 331 -0.0004

ASP 331 LEU 332 0.0005

LEU 332 LYS 333 -0.0000

LYS 333 CYS 334 -0.0005

CYS 334 PRO 335 -0.0001

PRO 335 THR 336 -0.0000

THR 336 GLU 337 -0.0001

GLU 337 ILE 338 -0.0002

ILE 338 GLY 339 0.0002

GLY 339 ILE 340 -0.0005

ILE 340 THR 341 0.0002

THR 341 ASP 342 0.0000

ASP 342 ARG 343 -0.0001

ARG 343 ARG 344 -0.0001

ARG 344 GLU 345 -0.0001

GLU 345 ALA 346 -0.0003

ALA 346 GLU 347 -0.0001

GLU 347 LEU 348 0.0001

LEU 348 SER 349 0.0005

SER 349 LYS 350 -0.0001

LYS 350 LEU 351 -0.0003

LEU 351 GLY 352 -0.0002

GLY 352 PHE 353 0.0001

PHE 353 LEU 354 -0.0001

LEU 354 PRO 355 0.0000

PRO 355 LEU 356 -0.0003

LEU 356 CYS 357 0.0001

CYS 357 HIS 358 -0.0002

HIS 358 TYR 359 0.0002

TYR 359 LYS 360 -0.0003

LYS 360 ASN 361 0.0003

ASN 361 THR 362 0.0000

THR 362 ASP 363 0.0002

ASP 363 TYR 364 -0.0004

TYR 364 ALA 365 0.0003

ALA 365 VAL 366 -0.0005

VAL 366 PHE 367 -0.0001

PHE 367 PHE 368 0.0000

PHE 368 GLY 369 -0.0001

GLY 369 GLY 370 -0.0000

GLY 370 GLN 371 0.0002

GLN 371 SER 372 -0.0001

SER 372 THR 373 0.0002

THR 373 GLN 374 -0.0000

GLN 374 LYS 375 0.0003

LYS 375 PRO 376 0.0000

PRO 376 LYS 377 -0.0002

LYS 377 LYS 378 0.0001

LYS 378 TYR 379 0.0000

TYR 379 ASP 380 -0.0002

ASP 380 ARG 381 -0.0001

ARG 381 PRO 382 -0.0001

PRO 382 GLU 383 0.0003

GLU 383 ALA 384 0.0003

ALA 384 THR 385 0.0002

THR 385 ALA 386 -0.0002

ALA 386 ASN 387 -0.0000

ASN 387 ALA 388 0.0000

ALA 388 ALA 389 0.0001

ALA 389 ILE 390 0.0002

ILE 390 SER 391 0.0001

SER 391 ALA 392 -0.0001

ALA 392 ARG 393 -0.0002

ARG 393 LEU 394 0.0004

LEU 394 PRO 395 -0.0003

PRO 395 TYR 396 0.0001

TYR 396 LEU 397 -0.0002

LEU 397 MET 398 0.0004

MET 398 ALA 399 -0.0000

ALA 399 THR 400 0.0002

THR 400 SER 401 -0.0002

SER 401 ARG 402 0.0001

ARG 402 PHE 403 0.0001

PHE 403 THR 404 -0.0001

THR 404 HIS 405 0.0001

HIS 405 TYR 406 0.0005

TYR 406 LEU 407 0.0000

LEU 407 LYS 408 0.0005

LYS 408 VAL 409 0.0003

VAL 409 MET 410 -0.0001

MET 410 ALA 411 -0.0002

ALA 411 ARG 412 -0.0005

ARG 412 ASP 413 -0.0000

ASP 413 LYS 414 -0.0003

LYS 414 ILE 415 0.0004

ILE 415 GLY 416 -0.0002

GLY 416 SER 417 -0.0001

SER 417 PHE 418 -0.0001

PHE 418 MET 419 0.0003

MET 419 GLU 420 -0.0002

GLU 420 ALA 421 -0.0002

ALA 421 ASP 422 -0.0000

ASP 422 ASP 423 0.0002

ASP 423 VAL 424 0.0001

VAL 424 GLU 425 -0.0001

GLU 425 ALA 426 -0.0002

ALA 426 TRP 427 0.0002

TRP 427 LEU 428 0.0004

LEU 428 ASN 429 -0.0003

ASN 429 ARG 430 0.0001

ARG 430 TRP 431 0.0001

TRP 431 LEU 432 -0.0000

LEU 432 MET 433 -0.0001

MET 433 ASN 434 0.0004

ASN 434 TYR 435 0.0002

TYR 435 VAL 436 -0.0002

VAL 436 ASN 437 0.0003

ASN 437 ASP 438 0.0001

ASP 438 ASN 439 -0.0005

ASN 439 PRO 440 -0.0001

PRO 440 ASN 441 0.0003

ASN 441 SER 442 -0.0001

SER 442 GLY 443 0.0003

GLY 443 PRO 444 0.0002

PRO 444 GLU 445 -0.0001

GLU 445 MET 446 -0.0004

MET 446 LYS 447 0.0000

LYS 447 ALA 448 -0.0000

ALA 448 ARG 449 0.0000

ARG 449 TYR 450 0.0002

TYR 450 PRO 451 0.0000

PRO 451 LEU 452 0.0003

LEU 452 LYS 453 -0.0003

LYS 453 GLU 454 0.0002

GLU 454 ALA 455 0.0000

ALA 455 LYS 456 -0.0001

LYS 456 VAL 457 0.0000

VAL 457 MET 458 0.0000

MET 458 VAL 459 0.0001

VAL 459 THR 460 0.0000

THR 460 GLU 461 -0.0001

GLU 461 VAL 462 0.0000

VAL 462 PRO 463 0.0002

PRO 463 GLY 464 0.0001

GLY 464 GLN 465 0.0005

GLN 465 PRO 466 -0.0003

PRO 466 GLY 467 -0.0001

GLY 467 SER 468 0.0001

SER 468 TYR 469 -0.0002

TYR 469 ASN 470 0.0002

ASN 470 VAL 471 0.0000

VAL 471 VAL 472 -0.0003

VAL 472 ALA 473 -0.0000

ALA 473 TRP 474 -0.0002

TRP 474 MET 475 -0.0000

MET 475 ARG 476 -0.0000

ARG 476 PRO 477 0.0003

PRO 477 TRP 478 0.0001

TRP 478 LEU 479 -0.0003

LEU 479 GLN 480 -0.0000

GLN 480 LEU 481 0.0007

LEU 481 GLU 482 0.0000

GLU 482 GLU 483 0.0001

GLU 483 LEU 484 -0.0028

LEU 484 THR 485 0.0001

THR 485 VAL 486 -0.0002

VAL 486 SER 487 -0.0017

SER 487 MET 488 -0.0003

MET 488 ARG 489 0.0004

ARG 489 MET 490 0.0001

MET 490 VAL 491 0.0001

VAL 491 ALA 492 0.0000

ALA 492 LYS 493 -0.0005

LYS 493 ILE 494 -0.0001

ILE 494 PRO 495 0.0002

PRO 495 GLN 496 -0.0000

GLN 496 LEU 497 -0.0002

LEU 497 GLY 498 -0.0001

GLY 498 LYS 499 0.0001

LYS 499 ASP 500 -0.0004

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: October 18th, 2018.

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

*** AlphaFold ***

CA strain for 23010308584016806

--- normal mode 7 ---

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

* AlphaFold *