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

* *

CA strain for 2406112217162288715

--- normal mode 9 ---

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
THR 1 VAL 2 -0.0003

VAL 2 ASP 3 -0.0002

ASP 3 ASP 4 0.0000

ASP 4 ILE 5 -0.0000

ILE 5 LEU 6 0.0001

LEU 6 GLU 7 0.0002

GLU 7 GLN 8 0.0004

GLN 8 VAL 9 0.0001

VAL 9 GLY 10 0.0009

GLY 10 GLU 11 -0.0004

GLU 11 SER 12 0.0000

SER 12 GLY 13 0.0014

GLY 13 TRP 14 -0.0003

TRP 14 PHE 15 -0.0001

PHE 15 GLN 16 -0.0000

GLN 16 LYS 17 0.0000

LYS 17 GLN 18 -0.0003

GLN 18 ALA 19 0.0000

ALA 19 PHE 20 0.0000

PHE 20 LEU 21 -0.0003

LEU 21 ILE 22 0.0011

ILE 22 LEU 23 0.0000

LEU 23 CYS 24 0.0000

CYS 24 LEU 25 0.0009

LEU 25 LEU 26 0.0001

LEU 26 SER 27 -0.0002

SER 27 ALA 28 0.0006

ALA 28 ALA 29 -0.0002

ALA 29 PHE 30 -0.0001

PHE 30 ALA 31 -0.0006

ALA 31 PRO 32 0.0001

PRO 32 ILE 33 -0.0004

ILE 33 CYS 34 -0.0002

CYS 34 VAL 35 -0.0002

VAL 35 GLY 36 0.0003

GLY 36 ILE 37 0.0013

ILE 37 VAL 38 0.0003

VAL 38 PHE 39 -0.0002

PHE 39 LEU 40 0.0009

LEU 40 GLY 41 0.0003

GLY 41 PHE 42 0.0000

PHE 42 THR 43 0.0034

THR 43 PRO 44 -0.0001

PRO 44 ASP 45 -0.0001

ASP 45 HIS 46 0.0027

HIS 46 HIS 47 -0.0001

HIS 47 CYS 48 0.0001

CYS 48 GLN 49 0.0000

GLN 49 SER 50 0.0001

SER 50 PRO 51 -0.0001

PRO 51 GLY 52 -0.0011

GLY 52 VAL 53 -0.0004

VAL 53 ALA 54 -0.0001

ALA 54 GLU 55 0.0001

GLU 55 LEU 56 -0.0003

LEU 56 SER 57 0.0001

SER 57 GLN 58 0.0003

GLN 58 ARG 59 0.0002

ARG 59 CYS 60 0.0001

CYS 60 GLY 61 0.0003

GLY 61 TRP 62 -0.0002

TRP 62 SER 63 -0.0000

SER 63 PRO 64 0.0002

PRO 64 ALA 65 0.0003

ALA 65 GLU 66 -0.0001

GLU 66 GLU 67 -0.0003

GLU 67 LEU 68 0.0001

LEU 68 ASN 69 -0.0001

ASN 69 TYR 70 0.0004

TYR 70 THR 71 0.0002

THR 71 VAL 72 0.0001

VAL 72 PRO 73 0.0001

PRO 73 GLY 74 -0.0001

GLY 74 LEU 75 0.0000

LEU 75 GLY 76 -0.0002

GLY 76 PRO 77 0.0003

PRO 77 ALA 78 0.0003

ALA 78 GLY 79 0.0004

GLY 79 GLU 80 -0.0001

GLU 80 ALA 81 0.0002

ALA 81 PHE 82 0.0010

PHE 82 LEU 83 -0.0000

LEU 83 GLY 84 0.0003

GLY 84 GLN 85 0.0006

GLN 85 CYS 86 -0.0003

CYS 86 ARG 87 0.0001

ARG 87 ARG 88 -0.0018

ARG 88 TYR 89 0.0003

TYR 89 GLU 90 -0.0002

GLU 90 VAL 91 -0.0019

VAL 91 ASP 92 -0.0002

ASP 92 TRP 93 0.0003

TRP 93 ASN 94 -0.0006

ASN 94 GLN 95 -0.0000

GLN 95 SER 96 0.0001

SER 96 ALA 97 0.0002

ALA 97 LEU 98 0.0003

LEU 98 SER 99 -0.0004

SER 99 CYS 100 0.0004

CYS 100 VAL 101 0.0004

VAL 101 ASP 102 -0.0004

ASP 102 PRO 103 -0.0003

PRO 103 LEU 104 0.0003

LEU 104 ALA 105 -0.0001

ALA 105 SER 106 0.0006

SER 106 LEU 107 0.0001

LEU 107 ALA 108 0.0000

ALA 108 THR 109 0.0003

THR 109 ASN 110 0.0000

ASN 110 ARG 111 0.0001

ARG 111 SER 112 -0.0000

SER 112 HIS 113 -0.0002

HIS 113 LEU 114 0.0001

LEU 114 PRO 115 -0.0009

PRO 115 LEU 116 0.0002

LEU 116 GLY 117 -0.0001

GLY 117 PRO 118 0.0002

PRO 118 CYS 119 0.0001

CYS 119 GLN 120 0.0001

GLN 120 ASP 121 0.0011

ASP 121 GLY 122 0.0000

GLY 122 TRP 123 0.0002

TRP 123 VAL 124 0.0003

VAL 124 TYR 125 0.0004

TYR 125 ASP 126 0.0003

ASP 126 THR 127 0.0050

THR 127 PRO 128 -0.0002

PRO 128 GLY 129 0.0004

GLY 129 SER 130 0.0003

SER 130 SER 131 0.0003

SER 131 ILE 132 -0.0003

ILE 132 VAL 133 0.0002

VAL 133 THR 134 -0.0003

THR 134 GLU 135 -0.0005

GLU 135 PHE 136 0.0005

PHE 136 ASN 137 0.0003

ASN 137 LEU 138 0.0002

LEU 138 VAL 139 0.0002

VAL 139 CYS 140 -0.0000

CYS 140 ALA 141 -0.0003

ALA 141 ASP 142 -0.0013

ASP 142 SER 143 0.0005

SER 143 TRP 144 -0.0000

TRP 144 LYS 145 -0.0004

LYS 145 LEU 146 0.0001

LEU 146 ASP 147 -0.0001

ASP 147 LEU 148 0.0017

LEU 148 PHE 149 -0.0000

PHE 149 GLN 150 -0.0002

GLN 150 SER 151 -0.0009

SER 151 CYS 152 -0.0002

CYS 152 LEU 153 -0.0003

LEU 153 ASN 154 -0.0008

ASN 154 ALA 155 0.0002

ALA 155 GLY 156 -0.0001

GLY 156 PHE 157 -0.0003

PHE 157 LEU 158 0.0002

LEU 158 PHE 159 0.0001

PHE 159 GLY 160 -0.0003

GLY 160 SER 161 -0.0002

SER 161 LEU 162 -0.0000

LEU 162 GLY 163 0.0001

GLY 163 VAL 164 -0.0003

VAL 164 GLY 165 0.0002

GLY 165 TYR 166 -0.0005

TYR 166 PHE 167 0.0000

PHE 167 ALA 168 0.0001

ALA 168 ASP 169 0.0002

ASP 169 ARG 170 0.0003

ARG 170 PHE 171 0.0001

PHE 171 GLY 172 -0.0002

GLY 172 ARG 173 -0.0003

ARG 173 LYS 174 0.0000

LYS 174 LEU 175 0.0001

LEU 175 CYS 176 -0.0005

CYS 176 LEU 177 0.0005

LEU 177 LEU 178 0.0003

LEU 178 GLY 179 -0.0001

GLY 179 THR 180 0.0004

THR 180 VAL 181 -0.0003

VAL 181 LEU 182 0.0002

LEU 182 VAL 183 0.0002

VAL 183 ASN 184 0.0002

ASN 184 ALA 185 0.0002

ALA 185 VAL 186 -0.0001

VAL 186 SER 187 -0.0002

SER 187 GLY 188 0.0001

GLY 188 VAL 189 -0.0003

VAL 189 LEU 190 0.0005

LEU 190 MET 191 0.0001

MET 191 ALA 192 -0.0002

ALA 192 PHE 193 0.0003

PHE 193 SER 194 0.0000

SER 194 PRO 195 0.0002

PRO 195 ASN 196 0.0005

ASN 196 TYR 197 -0.0003

TYR 197 MET 198 0.0002

MET 198 SER 199 -0.0005

SER 199 MET 200 0.0001

MET 200 LEU 201 0.0003

LEU 201 LEU 202 -0.0005

LEU 202 PHE 203 0.0002

PHE 203 ARG 204 -0.0001

ARG 204 LEU 205 -0.0000

LEU 205 LEU 206 -0.0002

LEU 206 GLN 207 -0.0001

GLN 207 GLY 208 -0.0003

GLY 208 LEU 209 0.0001

LEU 209 VAL 210 0.0001

VAL 210 SER 211 -0.0000

SER 211 LYS 212 0.0000

LYS 212 GLY 213 0.0004

GLY 213 ASN 214 0.0001

ASN 214 TRP 215 0.0001

TRP 215 MET 216 -0.0002

MET 216 ALA 217 0.0003

ALA 217 GLY 218 0.0004

GLY 218 TYR 219 -0.0000

TYR 219 THR 220 -0.0004

THR 220 LEU 221 0.0002

LEU 221 ILE 222 0.0002

ILE 222 THR 223 -0.0002

THR 223 GLU 224 0.0003

GLU 224 PHE 225 0.0002

PHE 225 VAL 226 0.0003

VAL 226 GLY 227 -0.0001

GLY 227 SER 228 -0.0000

SER 228 GLY 229 -0.0005

GLY 229 SER 230 -0.0002

SER 230 ARG 231 0.0002

ARG 231 ARG 232 0.0025

ARG 232 THR 233 0.0002

THR 233 VAL 234 0.0002

VAL 234 ALA 235 0.0006

ALA 235 ILE 236 0.0000

ILE 236 MET 237 -0.0000

MET 237 TYR 238 0.0006

TYR 238 GLN 239 -0.0001

GLN 239 MET 240 -0.0002

MET 240 ALA 241 0.0025

ALA 241 PHE 242 -0.0005

PHE 242 THR 243 0.0004

THR 243 VAL 244 0.0001

VAL 244 GLY 245 0.0002

GLY 245 LEU 246 -0.0000

LEU 246 VAL 247 -0.0010

VAL 247 ALA 248 -0.0001

ALA 248 LEU 249 0.0001

LEU 249 THR 250 -0.0005

THR 250 GLY 251 -0.0003

GLY 251 LEU 252 0.0004

LEU 252 ALA 253 0.0003

ALA 253 TYR 254 0.0000

TYR 254 ALA 255 -0.0002

ALA 255 LEU 256 -0.0000

LEU 256 PRO 257 -0.0002

PRO 257 HIS 258 0.0004

HIS 258 TRP 259 -0.0002

TRP 259 ARG 260 -0.0004

ARG 260 TRP 261 0.0003

TRP 261 LEU 262 0.0001

LEU 262 GLN 263 -0.0001

GLN 263 LEU 264 -0.0003

LEU 264 ALA 265 -0.0001

ALA 265 VAL 266 -0.0001

VAL 266 SER 267 0.0001

SER 267 LEU 268 0.0001

LEU 268 PRO 269 0.0002

PRO 269 THR 270 0.0003

THR 270 PHE 271 0.0001

PHE 271 LEU 272 0.0002

LEU 272 PHE 273 -0.0000

PHE 273 LEU 274 -0.0000

LEU 274 LEU 275 0.0001

LEU 275 TYR 276 0.0003

TYR 276 TYR 277 0.0004

TYR 277 TRP 278 -0.0001

TRP 278 CYS 279 0.0001

CYS 279 VAL 280 -0.0002

VAL 280 PRO 281 0.0001

PRO 281 GLU 282 0.0003

GLU 282 SER 283 -0.0003

SER 283 PRO 284 -0.0004

PRO 284 ARG 285 -0.0003

ARG 285 TRP 286 0.0001

TRP 286 LEU 287 0.0002

LEU 287 LEU 288 0.0002

LEU 288 SER 289 0.0005

SER 289 GLN 290 0.0003

GLN 290 LYS 291 0.0001

LYS 291 ARG 292 0.0007

ARG 292 ASN 293 0.0000

ASN 293 THR 294 0.0002

THR 294 GLU 295 -0.0001

GLU 295 ALA 296 0.0000

ALA 296 ILE 297 0.0004

ILE 297 LYS 298 0.0001

LYS 298 ILE 299 0.0004

ILE 299 MET 300 0.0005

MET 300 ASP 301 0.0001

ASP 301 HIS 302 -0.0002

HIS 302 ILE 303 -0.0001

ILE 303 ALA 304 -0.0002

ALA 304 GLN 305 -0.0001

GLN 305 LYS 306 -0.0001

LYS 306 ASN 307 -0.0001

ASN 307 GLY 308 -0.0003

GLY 308 LYS 309 0.0000

LYS 309 LEU 310 0.0003

LEU 310 PRO 311 -0.0004

PRO 311 PRO 312 -0.0001

PRO 312 ALA 313 0.0001

ALA 313 ASP 314 0.0002

ASP 314 LEU 315 -0.0001

LEU 315 LYS 316 0.0002

LYS 316 MET 317 0.0002

MET 317 LEU 318 0.0002

LEU 318 SER 319 -0.0007

SER 319 LEU 320 0.0004

LEU 320 GLU 321 -0.0003

GLU 321 GLU 322 0.0006

GLU 322 ASP 323 0.0001

ASP 323 VAL 324 0.0000

VAL 324 THR 325 0.0011

THR 325 GLU 326 0.0001

GLU 326 LYS 327 -0.0002

LYS 327 LEU 328 0.0026

LEU 328 SER 329 -0.0001

SER 329 PRO 330 0.0002

PRO 330 SER 331 0.0024

SER 331 PHE 332 -0.0000

PHE 332 ALA 333 -0.0001

ALA 333 ASP 334 -0.0008

ASP 334 LEU 335 -0.0000

LEU 335 PHE 336 0.0000

PHE 336 ARG 337 -0.0020

ARG 337 THR 338 0.0004

THR 338 LEU 339 -0.0001

LEU 339 ARG 340 -0.0002

ARG 340 LEU 341 -0.0002

LEU 341 ARG 342 0.0002

ARG 342 LYS 343 0.0074

LYS 343 ARG 344 0.0001

ARG 344 THR 345 -0.0000

THR 345 PHE 346 0.0002

PHE 346 ILE 347 -0.0001

ILE 347 LEU 348 0.0003

LEU 348 MET 349 0.0009

MET 349 TYR 350 0.0004

TYR 350 LEU 351 -0.0002

LEU 351 TRP 352 -0.0001

TRP 352 PHE 353 0.0000

PHE 353 THR 354 0.0001

THR 354 ASP 355 -0.0005

ASP 355 SER 356 -0.0001

SER 356 VAL 357 0.0001

VAL 357 LEU 358 -0.0006

LEU 358 TYR 359 -0.0001

TYR 359 GLN 360 -0.0000

GLN 360 GLY 361 0.0005

GLY 361 LEU 362 -0.0001

LEU 362 ILE 363 0.0003

ILE 363 LEU 364 0.0007

LEU 364 HIS 365 0.0001

HIS 365 MET 366 0.0004

MET 366 GLY 367 0.0008

GLY 367 ALA 368 -0.0001

ALA 368 THR 369 -0.0001

THR 369 SER 370 -0.0004

SER 370 GLY 371 -0.0004

GLY 371 ASN 372 -0.0000

ASN 372 LEU 373 -0.0002

LEU 373 TYR 374 -0.0001

TYR 374 LEU 375 0.0002

LEU 375 ASP 376 -0.0005

ASP 376 PHE 377 0.0003

PHE 377 LEU 378 -0.0000

LEU 378 TYR 379 0.0001

TYR 379 SER 380 0.0004

SER 380 ALA 381 0.0001

ALA 381 LEU 382 0.0001

LEU 382 VAL 383 -0.0003

VAL 383 GLU 384 0.0002

GLU 384 ILE 385 -0.0009

ILE 385 PRO 386 0.0002

PRO 386 GLY 387 -0.0002

GLY 387 ALA 388 -0.0009

ALA 388 PHE 389 -0.0001

PHE 389 ILE 390 0.0000

ILE 390 ALA 391 0.0005

ALA 391 LEU 392 -0.0001

LEU 392 ILE 393 0.0003

ILE 393 THR 394 0.0005

THR 394 ILE 395 0.0000

ILE 395 ASP 396 0.0003

ASP 396 ARG 397 -0.0004

ARG 397 VAL 398 0.0001

VAL 398 GLY 399 0.0007

GLY 399 ARG 400 -0.0039

ARG 400 ILE 401 -0.0000

ILE 401 TYR 402 0.0001

TYR 402 PRO 403 0.0002

PRO 403 MET 404 -0.0002

MET 404 ALA 405 0.0002

ALA 405 MET 406 0.0013

MET 406 SER 407 -0.0001

SER 407 ASN 408 0.0000

ASN 408 LEU 409 -0.0002

LEU 409 LEU 410 -0.0000

LEU 410 ALA 411 0.0001

ALA 411 GLY 412 0.0001

GLY 412 ALA 413 0.0002

ALA 413 ALA 414 -0.0000

ALA 414 CYS 415 0.0003

CYS 415 LEU 416 -0.0000

LEU 416 VAL 417 0.0004

VAL 417 MET 418 0.0003

MET 418 ILE 419 -0.0002

ILE 419 PHE 420 0.0000

PHE 420 ILE 421 -0.0004

ILE 421 SER 422 0.0000

SER 422 PRO 423 0.0001

PRO 423 ASP 424 0.0001

ASP 424 LEU 425 0.0001

LEU 425 HIS 426 -0.0002

HIS 426 TRP 427 0.0004

TRP 427 LEU 428 0.0000

LEU 428 ASN 429 -0.0004

ASN 429 ILE 430 -0.0004

ILE 430 ILE 431 0.0001

ILE 431 ILE 432 0.0000

ILE 432 MET 433 -0.0000

MET 433 CYS 434 0.0001

CYS 434 VAL 435 -0.0003

VAL 435 GLY 436 -0.0002

GLY 436 ARG 437 0.0005

ARG 437 MET 438 0.0001

MET 438 GLY 439 0.0008

GLY 439 ILE 440 -0.0001

ILE 440 THR 441 -0.0003

THR 441 ILE 442 0.0020

ILE 442 ALA 443 0.0001

ALA 443 ILE 444 -0.0000

ILE 444 GLN 445 -0.0001

GLN 445 MET 446 0.0002

MET 446 ILE 447 0.0004

ILE 447 CYS 448 -0.0016

CYS 448 LEU 449 0.0003

LEU 449 VAL 450 0.0000

VAL 450 ASN 451 -0.0025

ASN 451 ALA 452 -0.0001

ALA 452 GLU 453 0.0001

GLU 453 LEU 454 0.0004

LEU 454 TYR 455 0.0001

TYR 455 PRO 456 -0.0001

PRO 456 THR 457 -0.0022

THR 457 PHE 458 -0.0001

PHE 458 VAL 459 -0.0001

VAL 459 ARG 460 -0.0016

ARG 460 ASN 461 -0.0001

ASN 461 LEU 462 -0.0003

LEU 462 GLY 463 0.0015

GLY 463 VAL 464 0.0002

VAL 464 MET 465 0.0001

MET 465 VAL 466 -0.0004

VAL 466 CYS 467 -0.0005

CYS 467 SER 468 0.0002

SER 468 SER 469 0.0015

SER 469 LEU 470 -0.0003

LEU 470 CYS 471 -0.0003

CYS 471 ASP 472 -0.0003

ASP 472 ILE 473 -0.0002

ILE 473 GLY 474 -0.0000

GLY 474 GLY 475 -0.0016

GLY 475 ILE 476 -0.0004

ILE 476 ILE 477 -0.0000

ILE 477 THR 478 0.0010

THR 478 PRO 479 0.0004

PRO 479 PHE 480 -0.0000

PHE 480 ILE 481 -0.0001

ILE 481 VAL 482 0.0004

VAL 482 PHE 483 0.0002

PHE 483 ARG 484 0.0003

ARG 484 LEU 485 0.0001

LEU 485 ARG 486 -0.0001

ARG 486 GLU 487 -0.0007

GLU 487 VAL 488 0.0001

VAL 488 TRP 489 -0.0001

TRP 489 GLN 490 -0.0002

GLN 490 ALA 491 0.0001

ALA 491 LEU 492 -0.0002

LEU 492 PRO 493 0.0004

PRO 493 LEU 494 0.0001

LEU 494 ILE 495 -0.0000

ILE 495 LEU 496 0.0007

LEU 496 PHE 497 0.0001

PHE 497 ALA 498 -0.0002

ALA 498 VAL 499 0.0007

VAL 499 LEU 500 -0.0004

LEU 500 GLY 501 0.0001

GLY 501 LEU 502 -0.0001

LEU 502 LEU 503 0.0004

LEU 503 ALA 504 -0.0002

ALA 504 ALA 505 -0.0005

ALA 505 GLY 506 -0.0003

GLY 506 VAL 507 -0.0002

VAL 507 THR 508 -0.0010

THR 508 LEU 509 -0.0001

LEU 509 LEU 510 0.0002

LEU 510 LEU 511 -0.0029

LEU 511 PRO 512 0.0002

PRO 512 GLU 513 -0.0002

GLU 513 THR 514 -0.0050

THR 514 LYS 515 0.0001

LYS 515 GLY 516 -0.0003

GLY 516 VAL 517 0.0095

VAL 517 ALA 518 0.0001

ALA 518 LEU 519 0.0000

LEU 519 PRO 520 -0.0040

PRO 520 GLU 521 0.0002

GLU 521 THR 522 0.0001

THR 522 MET 523 0.0002

MET 523 LYS 524 -0.0001

LYS 524 ASP 525 -0.0000

ASP 525 ALA 526 0.0025

ALA 526 GLU 527 -0.0000

GLU 527 ASN 528 -0.0001

ASN 528 LEU 529 0.0010

LEU 529 GLY 530 -0.0001

GLY 530 ARG 531 0.0002

ARG 531 LYS 532 -0.0173

LYS 532 ALA 533 -0.0001

ALA 533 LYS 534 -0.0002

LYS 534 PRO 535 0.1190

PRO 535 LYS 536 0.0002

LYS 536 GLU 537 -0.0002

GLU 537 ASN 538 -0.0263

ASN 538 THR 539 -0.0000

THR 539 ILE 540 0.0002

ILE 540 TYR 541 -0.0235

TYR 541 LEU 542 -0.0005

LEU 542 LYS 543 -0.0001

LYS 543 VAL 544 -0.0757

VAL 544 GLN 545 0.0000

GLN 545 THR 546 -0.0000

THR 546 SER 547 -0.0089

SER 547 GLU 548 -0.0000

GLU 548 PRO 549 -0.0000

PRO 549 SER 550 -0.0147

SER 550 GLY 551 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).
Last modification: April 25th, 2023.

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

*** ***

CA strain for 2406112217162288715

--- normal mode 9 ---

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

* *