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

* dndc-4FS-rank3 *

CA strain for 250214070608127607

--- 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
MET 1 SER 2 0.0002

SER 2 LYS 3 -0.0006

LYS 3 LEU 4 -0.0005

LEU 4 VAL 5 -0.0003

VAL 5 GLN 6 0.0001

GLN 6 ALA 7 0.0012

ALA 7 TYR 8 -0.0004

TYR 8 ASP 9 0.0004

ASP 9 LEU 10 -0.0015

LEU 10 ALA 11 -0.0002

ALA 11 GLU 12 0.0001

GLU 12 TYR 13 -0.0000

TYR 13 GLU 14 0.0001

GLU 14 ASP 15 -0.0005

ASP 15 PHE 16 -0.0016

PHE 16 ILE 17 -0.0001

ILE 17 ASN 18 0.0004

ASN 18 GLN 19 -0.0014

GLN 19 GLU 20 -0.0001

GLU 20 GLN 21 0.0002

GLN 21 PHE 22 0.0008

PHE 22 ALA 23 -0.0001

ALA 23 GLY 24 -0.0000

GLY 24 ARG 25 -0.0002

ARG 25 PRO 26 -0.0000

PRO 26 LEU 27 -0.0001

LEU 27 ALA 28 -0.0006

ALA 28 GLU 29 0.0000

GLU 29 TYR 30 0.0005

TYR 30 VAL 31 0.0002

VAL 31 ALA 32 -0.0000

ALA 32 GLU 33 0.0000

GLU 33 VAL 34 0.0001

VAL 34 GLN 35 -0.0001

GLN 35 ARG 36 -0.0001

ARG 36 ILE 37 -0.0026

ILE 37 TYR 38 -0.0000

TYR 38 CYS 39 0.0004

CYS 39 ALA 40 0.0016

ALA 40 ASP 41 0.0001

ASP 41 LYS 42 -0.0002

LYS 42 ARG 43 -0.0005

ARG 43 PRO 44 -0.0000

PRO 44 TRP 45 -0.0001

TRP 45 VAL 46 -0.0024

VAL 46 ILE 47 0.0002

ILE 47 GLY 48 -0.0003

GLY 48 TYR 49 0.0064

TYR 49 SER 50 -0.0002

SER 50 GLY 51 0.0001

GLY 51 GLY 52 0.0046

GLY 52 LYS 53 0.0000

LYS 53 ASP 54 0.0001

ASP 54 SER 55 0.0020

SER 55 SER 56 -0.0001

SER 56 ALA 57 -0.0004

ALA 57 VAL 58 0.0015

VAL 58 ILE 59 -0.0003

ILE 59 THR 60 0.0001

THR 60 LEU 61 0.0017

LEU 61 VAL 62 -0.0003

VAL 62 TYR 63 -0.0001

TYR 63 LEU 64 0.0009

LEU 64 ALA 65 0.0001

ALA 65 LEU 66 0.0002

LEU 66 LEU 67 -0.0015

LEU 67 GLY 68 -0.0001

GLY 68 LEU 69 -0.0001

LEU 69 PRO 70 0.0006

PRO 70 PRO 71 -0.0000

PRO 71 GLU 72 -0.0001

GLU 72 MET 73 -0.0009

MET 73 ARG 74 -0.0002

ARG 74 SER 75 0.0002

SER 75 LYS 76 -0.0040

LYS 76 ASP 77 0.0002

ASP 77 ILE 78 -0.0000

ILE 78 PHE 79 -0.0021

PHE 79 VAL 80 0.0000

VAL 80 VAL 81 -0.0001

VAL 81 SER 82 0.0009

SER 82 SER 83 0.0001

SER 83 ASP 84 -0.0002

ASP 84 THR 85 0.0003

THR 85 LEU 86 0.0001

LEU 86 VAL 87 -0.0002

VAL 87 GLU 88 -0.0016

GLU 88 THR 89 0.0005

THR 89 PRO 90 -0.0002

PRO 90 VAL 91 0.0082

VAL 91 VAL 92 0.0003

VAL 92 VAL 93 0.0003

VAL 93 ASP 94 -0.0064

ASP 94 LEU 95 -0.0003

LEU 95 ILE 96 -0.0002

ILE 96 LYS 97 -0.0091

LYS 97 LYS 98 -0.0000

LYS 98 THR 99 0.0001

THR 99 MET 100 -0.0006

MET 100 LEU 101 -0.0002

LEU 101 GLN 102 -0.0004

GLN 102 ILE 103 0.0020

ILE 103 GLU 104 0.0003

GLU 104 ALA 105 0.0006

ALA 105 GLY 106 0.0006

GLY 106 ALA 107 0.0001

ALA 107 LYS 108 -0.0002

LYS 108 ARG 109 -0.0011

ARG 109 ASN 110 0.0000

ASN 110 GLY 111 0.0002

GLY 111 LEU 112 -0.0030

LEU 112 PRO 113 -0.0002

PRO 113 ILE 114 0.0001

ILE 114 THR 115 0.0006

THR 115 GLN 116 -0.0002

GLN 116 HIS 117 0.0002

HIS 117 ALA 118 0.0103

ALA 118 VAL 119 -0.0001

VAL 119 THR 120 0.0002

THR 120 PRO 121 0.0037

PRO 121 LYS 122 0.0001

LYS 122 THR 123 -0.0003

THR 123 ASN 124 -0.0018

ASN 124 GLU 125 -0.0002

GLU 125 THR 126 0.0003

THR 126 PHE 127 -0.0003

PHE 127 TRP 128 0.0001

TRP 128 VAL 129 -0.0002

VAL 129 ASN 130 0.0006

ASN 130 LEU 131 0.0002

LEU 131 LEU 132 0.0000

LEU 132 GLY 133 -0.0011

GLY 133 LYS 134 0.0001

LYS 134 GLY 135 0.0001

GLY 135 TYR 136 -0.0032

TYR 136 PRO 137 0.0000

PRO 137 ALA 138 0.0002

ALA 138 PRO 139 -0.0015

PRO 139 THR 140 0.0001

THR 140 ARG 141 -0.0001

ARG 141 SER 142 0.0040

SER 142 PHE 143 0.0003

PHE 143 ARG 144 0.0001

ARG 144 TRP 145 0.0042

TRP 145 CYS 146 -0.0001

CYS 146 THR 147 0.0003

THR 147 GLU 148 0.0011

GLU 148 ARG 149 0.0002

ARG 149 MET 150 0.0001

MET 150 LYS 151 -0.0076

LYS 151 ILE 152 -0.0003

ILE 152 ASN 153 -0.0004

ASN 153 PRO 154 -0.0010

PRO 154 VAL 155 0.0002

VAL 155 SER 156 -0.0003

SER 156 ASP 157 -0.0026

ASP 157 PHE 158 -0.0004

PHE 158 ILE 159 0.0002

ILE 159 LYS 160 0.0051

LYS 160 ASP 161 0.0004

ASP 161 LYS 162 0.0001

LYS 162 VAL 163 0.0062

VAL 163 SER 164 -0.0005

SER 164 GLN 165 -0.0000

GLN 165 PHE 166 -0.0005

PHE 166 ASP 167 -0.0001

ASP 167 GLU 168 -0.0000

GLU 168 VAL 169 0.0025

VAL 169 ILE 170 0.0002

ILE 170 VAL 171 -0.0000

VAL 171 VAL 172 0.0018

VAL 172 LEU 173 0.0003

LEU 173 GLY 174 -0.0002

GLY 174 SER 175 -0.0020

SER 175 ARG 176 -0.0002

ARG 176 SER 177 -0.0001

SER 177 SER 178 -0.0022

SER 178 GLU 179 -0.0001

GLU 179 SER 180 -0.0002

SER 180 ALA 181 -0.0020

ALA 181 SER 182 -0.0002

SER 182 ARG 183 -0.0001

ARG 183 ALA 184 -0.0005

ALA 184 GLN 185 0.0002

GLN 185 VAL 186 0.0001

VAL 186 ILE 187 -0.0005

ILE 187 ALA 188 0.0002

ALA 188 LYS 189 0.0003

LYS 189 HIS 190 -0.0003

HIS 190 LYS 191 0.0002

LYS 191 ILE 192 0.0000

ILE 192 ASP 193 -0.0006

ASP 193 GLY 194 0.0001

GLY 194 SER 195 0.0002

SER 195 ARG 196 -0.0020

ARG 196 LEU 197 -0.0003

LEU 197 ALA 198 0.0001

ALA 198 ARG 199 -0.0005

ARG 199 HIS 200 -0.0004

HIS 200 THR 201 0.0004

THR 201 THR 202 0.0001

THR 202 LEU 203 0.0001

LEU 203 ALA 204 -0.0003

ALA 204 ASN 205 -0.0031

ASN 205 ALA 206 -0.0001

ALA 206 PHE 207 0.0001

PHE 207 ILE 208 0.0033

ILE 208 TYR 209 0.0000

TYR 209 THR 210 -0.0001

THR 210 PRO 211 0.0016

PRO 211 ILE 212 0.0003

ILE 212 ASP 213 -0.0002

ASP 213 THR 214 0.0017

THR 214 TRP 215 0.0003

TRP 215 ASP 216 0.0000

ASP 216 VAL 217 -0.0021

VAL 217 GLU 218 -0.0002

GLU 218 ASP 219 -0.0001

ASP 219 VAL 220 0.0002

VAL 220 TRP 221 0.0002

TRP 221 LYS 222 0.0000

LYS 222 LEU 223 -0.0005

LEU 223 LEU 224 0.0002

LEU 224 ARG 225 0.0000

ARG 225 GLY 226 0.0011

GLY 226 ALA 227 0.0000

ALA 227 PHE 228 -0.0000

PHE 228 ARG 229 0.0008

ARG 229 TYR 230 -0.0003

TYR 230 ALA 231 0.0002

ALA 231 PRO 232 -0.0001

PRO 232 GLU 233 0.0002

GLU 233 ASP 234 -0.0002

ASP 234 ILE 235 -0.0008

ILE 235 ASP 236 0.0004

ASP 236 GLU 237 0.0003

GLU 237 TRP 238 -0.0011

TRP 238 GLU 239 0.0003

GLU 239 SER 240 -0.0002

SER 240 PRO 241 -0.0037

PRO 241 TRP 242 -0.0001

TRP 242 GLY 243 0.0001

GLY 243 GLY 244 -0.0023

GLY 244 ASN 245 -0.0002

ASN 245 ASN 246 0.0001

ASN 246 ARG 247 -0.0001

ARG 247 PRO 248 0.0001

PRO 248 LEU 249 -0.0000

LEU 249 TRP 250 0.0012

TRP 250 THR 251 -0.0001

THR 251 LEU 252 -0.0003

LEU 252 TYR 253 0.0031

TYR 253 MET 254 -0.0004

MET 254 ASP 255 -0.0003

ASP 255 SER 256 0.0002

SER 256 SER 257 0.0001

SER 257 ALA 258 0.0003

ALA 258 GLN 259 -0.0102

GLN 259 GLY 260 0.0001

GLY 260 GLU 261 0.0003

GLU 261 CYS 262 -0.0023

CYS 262 PRO 263 0.0000

PRO 263 LEU 264 -0.0001

LEU 264 VAL 265 0.0011

VAL 265 ILE 266 -0.0002

ILE 266 ASP 267 0.0003

ASP 267 ASP 268 0.0011

ASP 268 SER 269 0.0001

SER 269 THR 270 0.0000

THR 270 PRO 271 -0.0053

PRO 271 SER 272 -0.0002

SER 272 CYS 273 0.0001

CYS 273 GLY 274 -0.0099

GLY 274 ASN 275 0.0002

ASN 275 SER 276 0.0000

SER 276 ARG 277 -0.0139

ARG 277 PHE 278 -0.0002

PHE 278 GLY 279 0.0004

GLY 279 CYS 280 -0.0073

CYS 280 TRP 281 0.0002

TRP 281 THR 282 0.0002

THR 282 CYS 283 0.0024

CYS 283 THR 284 0.0002

THR 284 VAL 285 -0.0000

VAL 285 VAL 286 0.0015

VAL 286 THR 287 0.0002

THR 287 LYS 288 0.0001

LYS 288 ASP 289 -0.0040

ASP 289 LYS 290 0.0001

LYS 290 ALA 291 -0.0001

ALA 291 MET 292 -0.0071

MET 292 GLU 293 0.0000

GLU 293 SER 294 -0.0002

SER 294 LEU 295 0.0002

LEU 295 ILE 296 0.0003

ILE 296 LYS 297 0.0002

LYS 297 ASN 298 0.0047

ASN 298 GLY 299 0.0001

GLY 299 GLU 300 0.0001

GLU 300 GLU 301 0.0043

GLU 301 TRP 302 -0.0001

TRP 302 MET 303 -0.0002

MET 303 SER 304 0.0086

SER 304 PRO 305 0.0001

PRO 305 LEU 306 0.0003

LEU 306 LEU 307 -0.0037

LEU 307 LYS 308 0.0001

LYS 308 TYR 309 0.0001

TYR 309 ARG 310 -0.0052

ARG 310 ASP 311 -0.0002

ASP 311 LEU 312 -0.0003

LEU 312 LEU 313 0.0003

LEU 313 ALA 314 0.0002

ALA 314 PHE 315 0.0002

PHE 315 THR 316 -0.0067

THR 316 THR 317 0.0003

THR 317 ASP 318 -0.0001

ASP 318 PRO 319 -0.0019

PRO 319 VAL 320 0.0000

VAL 320 ASN 321 0.0000

ASN 321 LYS 322 0.0040

LYS 322 ASP 323 -0.0004

ASP 323 THR 324 0.0003

THR 324 PHE 325 0.0078

PHE 325 ARG 326 -0.0000

ARG 326 ASN 327 0.0001

ASN 327 TYR 328 0.0196

TYR 328 LYS 329 -0.0001

LYS 329 ARG 330 0.0002

ARG 330 ARG 331 -0.0135

ARG 331 THR 332 0.0001

THR 332 GLY 333 0.0000

GLY 333 LYS 334 -0.0295

LYS 334 VAL 335 -0.0001

VAL 335 SER 336 0.0001

SER 336 TYR 337 0.0092

TYR 337 GLN 338 0.0002

GLN 338 TYR 339 -0.0001

TYR 339 ALA 340 -0.0117

ALA 340 LYS 341 0.0000

LYS 341 GLU 342 0.0003

GLU 342 SER 343 -0.0018

SER 343 ASP 344 0.0000

ASP 344 GLU 345 0.0003

GLU 345 PRO 346 -0.0014

PRO 346 GLY 347 -0.0004

GLY 347 ALA 348 0.0002

ALA 348 GLU 349 0.0023

GLU 349 ARG 350 0.0003

ARG 350 LYS 351 0.0000

LYS 351 HIS 352 -0.0100

HIS 352 VAL 353 -0.0002

VAL 353 PRO 354 -0.0005

PRO 354 GLY 355 -0.0138

GLY 355 PRO 356 -0.0005

PRO 356 TYR 357 0.0001

TYR 357 TRP 358 -0.0141

TRP 358 LEU 359 -0.0002

LEU 359 LYS 360 -0.0002

LYS 360 TYR 361 0.0018

TYR 361 ARG 362 0.0004

ARG 362 GLN 363 0.0003

GLN 363 GLN 364 -0.0118

GLN 364 TRP 365 0.0001

TRP 365 LEU 366 0.0000

LEU 366 LYS 367 -0.0051

LYS 367 GLU 368 0.0000

GLU 368 LEU 369 0.0000

LEU 369 LEU 370 -0.0021

LEU 370 GLU 371 -0.0003

GLU 371 ILE 372 -0.0001

ILE 372 GLU 373 0.0046

GLU 373 ARG 374 0.0004

ARG 374 ASP 375 -0.0001

ASP 375 LEU 376 0.0054

LEU 376 ASN 377 0.0002

ASN 377 ALA 378 -0.0001

ALA 378 GLN 379 0.0005

GLN 379 GLY 380 0.0001

GLY 380 HIS 381 0.0002

HIS 381 THR 382 -0.0108

THR 382 ILE 383 0.0004

ILE 383 THR 384 0.0000

THR 384 LEU 385 -0.0022

LEU 385 ILE 386 0.0002

ILE 386 THR 387 0.0001

THR 387 LYS 388 0.0049

LYS 388 PRO 389 0.0001

PRO 389 GLU 390 0.0000

GLU 390 LEU 391 0.0077

LEU 391 HIS 392 -0.0002

HIS 392 ALA 393 0.0004

ALA 393 ILE 394 0.0020

ILE 394 ARG 395 0.0002

ARG 395 GLN 396 -0.0001

GLN 396 GLU 397 -0.0055

GLU 397 TRP 398 -0.0002

TRP 398 LEU 399 0.0001

LEU 399 LYS 400 0.0006

LYS 400 ASP 401 0.0001

ASP 401 PRO 402 -0.0001

PRO 402 ASN 403 -0.0034

ASN 403 GLU 404 0.0003

GLU 404 PRO 405 0.0002

PRO 405 ASP 406 0.0075

ASP 406 TRP 407 0.0001

TRP 407 TYR 408 0.0000

TYR 408 ASP 409 0.0228

ASP 409 THR 410 -0.0001

THR 410 LEU 411 0.0000

LEU 411 PRO 412 0.0020

PRO 412 GLY 413 0.0001

GLY 413 ILE 414 0.0001

ILE 414 TYR 415 0.0042

TYR 415 ARG 416 0.0001

ARG 416 GLU 417 0.0003

GLU 417 VAL 418 0.0048

VAL 418 TYR 419 -0.0000

TYR 419 GLN 420 -0.0002

GLN 420 GLN 421 -0.0043

GLN 421 ASP 422 -0.0001

ASP 422 LEU 423 0.0001

LEU 423 ASP 424 -0.0069

ASP 424 TRP 425 0.0002

TRP 425 VAL 426 0.0002

VAL 426 VAL 427 0.0087

VAL 427 ASP 428 0.0002

ASP 428 ASP 429 -0.0005

ASP 429 GLN 430 -0.0081

GLN 430 SER 431 -0.0001

SER 431 ARG 432 0.0003

ARG 432 PHE 433 -0.0019

PHE 433 ASP 434 0.0002

ASP 434 ALA 435 -0.0001

ALA 435 SER 436 0.0019

SER 436 ASP 437 -0.0002

ASP 437 ALA 438 -0.0001

ALA 438 ASP 439 -0.0012

ASP 439 LEU 440 0.0001

LEU 440 LEU 441 0.0000

LEU 441 VAL 442 -0.0019

VAL 442 GLN 443 -0.0002

GLN 443 ILE 444 -0.0005

ILE 444 ALA 445 -0.0010

ALA 445 GLN 446 0.0000

GLN 446 GLY 447 0.0002

GLY 447 PHE 448 -0.0003

PHE 448 ASP 449 0.0003

ASP 449 VAL 450 -0.0001

VAL 450 VAL 451 -0.0020

VAL 451 PRO 452 -0.0002

PRO 452 GLU 453 -0.0001

GLU 453 MET 454 -0.0027

MET 454 VAL 455 -0.0002

VAL 455 MET 456 -0.0003

MET 456 LYS 457 -0.0015

LYS 457 LEU 458 -0.0001

LEU 458 ILE 459 -0.0002

ILE 459 GLU 460 -0.0019

GLU 460 LEU 461 -0.0003

LEU 461 GLU 462 0.0000

GLU 462 VAL 463 -0.0000

VAL 463 SER 464 0.0001

SER 464 MET 465 0.0001

MET 465 GLU 466 0.0005

GLU 466 GLY 467 0.0000

GLY 467 LEU 468 0.0002

LEU 468 SER 469 0.0015

SER 469 ARG 470 0.0002

ARG 470 ARG 471 0.0002

ARG 471 GLN 472 0.0001

GLN 472 GLY 473 0.0001

GLY 473 ILE 474 0.0001

ILE 474 PHE 475 -0.0008

PHE 475 ASP 476 0.0001

ASP 476 LYS 477 -0.0003

LYS 477 LEU 478 0.0003

LEU 478 GLY 479 0.0001

GLY 479 THR 480 0.0000

THR 480 ILE 481 -0.0016

ILE 481 LEU 482 0.0002

LEU 482 LYS 483 -0.0001

LYS 483 GLN 484 -0.0010

GLN 484 ASP 485 0.0006

ASP 485 TRP 486 0.0001

TRP 486 GLY 487 -0.0007

GLY 487 THR 488 0.0002

THR 488 LEU 489 -0.0000

LEU 489 GLU 490 0.0309

GLU 490 GLU 491 -0.0000

GLU 491 ILE 492 0.0001

ILE 492 GLU 493 0.0019

GLU 493 GLN 494 -0.0002

GLN 494 GLN 495 0.0002

GLN 495 GLN 496 0.0304

GLN 496 VAL 497 0.0001

VAL 497 THR 498 -0.0001

THR 498 LEU 499 0.0352

LEU 499 GLN 500 -0.0003

GLN 500 LYS 501 0.0003

LYS 501 ARG 502 0.0191

ARG 502 VAL 503 0.0003

VAL 503 GLU 504 0.0001

GLU 504 ARG 505 0.0056

ARG 505 ASP 506 -0.0001

ASP 506 ILE 507 0.0002

ILE 507 HIS 508 0.0137

HIS 508 GLN 509 0.0001

GLN 509 GLU 510 0.0005

GLU 510 GLU 511 0.0017

GLU 511 LEU 512 -0.0001

LEU 512 THR 513 -0.0000

THR 513 LYS 514 -0.0384

LYS 514 LEU 515 0.0000

LEU 515 GLU 516 0.0003

GLU 516 THR 517 -0.0513

THR 517 GLU 518 -0.0002

GLU 518 LEU 519 0.0001

LEU 519 GLN 520 0.0181

GLN 520 VAL 521 0.0003

VAL 521 LEU 522 0.0003

LEU 522 GLN 523 0.0462

GLN 523 ARG 524 -0.0002

ARG 524 ARG 525 -0.0000

ARG 525 ILE 526 0.0409

ILE 526 VAL 527 -0.0000

VAL 527 ASP 528 0.0001

ASP 528 ALA 529 0.0029

ALA 529 SER 530 -0.0001

SER 530 GLU 531 -0.0002

GLU 531 SER 532 -0.0405

SER 532 SER 533 0.0000

SER 533 LEU 534 0.0001

LEU 534 LEU 535 -0.0102

LEU 535 ILE 536 -0.0003

ILE 536 GLY 537 0.0000

GLY 537 GLU 538 -0.0019

GLU 538 GLU 539 -0.0000

GLU 539 LYS 540 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).
Last modification: April 8th, 2025.

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

*** dndc-4FS-rank3 ***

CA strain for 250214070608127607

--- normal mode 9 ---

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

* dndc-4FS-rank3 *