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

* dndc-4FS-rank3_truncation *

CA strain for 250214072227131043

--- 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 SER 2 0.0002

SER 2 LYS 3 -0.0003

LYS 3 LEU 4 -0.0010

LEU 4 VAL 5 0.0002

VAL 5 GLN 6 -0.0003

GLN 6 ALA 7 -0.0014

ALA 7 TYR 8 0.0003

TYR 8 ASP 9 0.0000

ASP 9 LEU 10 0.0054

LEU 10 ALA 11 0.0005

ALA 11 GLU 12 0.0000

GLU 12 TYR 13 -0.0003

TYR 13 GLU 14 0.0004

GLU 14 ASP 15 0.0003

ASP 15 PHE 16 0.0070

PHE 16 ILE 17 0.0001

ILE 17 ASN 18 0.0001

ASN 18 GLN 19 0.0040

GLN 19 GLU 20 -0.0003

GLU 20 GLN 21 -0.0000

GLN 21 PHE 22 -0.0027

PHE 22 ALA 23 0.0002

ALA 23 GLY 24 -0.0004

GLY 24 ARG 25 0.0009

ARG 25 PRO 26 0.0002

PRO 26 LEU 27 0.0001

LEU 27 ALA 28 0.0023

ALA 28 GLU 29 0.0000

GLU 29 TYR 30 -0.0002

TYR 30 VAL 31 -0.0017

VAL 31 ALA 32 0.0003

ALA 32 GLU 33 -0.0001

GLU 33 VAL 34 -0.0001

VAL 34 GLN 35 -0.0000

GLN 35 ARG 36 -0.0000

ARG 36 ILE 37 0.0070

ILE 37 TYR 38 0.0002

TYR 38 CYS 39 0.0002

CYS 39 ALA 40 -0.0006

ALA 40 ASP 41 -0.0001

ASP 41 LYS 42 -0.0002

LYS 42 ARG 43 0.0012

ARG 43 PRO 44 0.0003

PRO 44 TRP 45 0.0001

TRP 45 VAL 46 0.0044

VAL 46 ILE 47 0.0004

ILE 47 GLY 48 0.0001

GLY 48 TYR 49 -0.0139

TYR 49 SER 50 -0.0001

SER 50 GLY 51 0.0003

GLY 51 GLY 52 -0.0065

GLY 52 LYS 53 0.0000

LYS 53 ASP 54 -0.0002

ASP 54 SER 55 -0.0050

SER 55 SER 56 -0.0002

SER 56 ALA 57 0.0001

ALA 57 VAL 58 -0.0039

VAL 58 ILE 59 -0.0000

ILE 59 THR 60 0.0001

THR 60 LEU 61 -0.0031

LEU 61 VAL 62 0.0002

VAL 62 TYR 63 0.0000

TYR 63 LEU 64 -0.0055

LEU 64 ALA 65 -0.0002

ALA 65 LEU 66 -0.0002

LEU 66 LEU 67 0.0026

LEU 67 GLY 68 0.0002

GLY 68 LEU 69 -0.0000

LEU 69 PRO 70 -0.0009

PRO 70 PRO 71 0.0002

PRO 71 GLU 72 -0.0003

GLU 72 MET 73 0.0024

MET 73 ARG 74 0.0000

ARG 74 SER 75 -0.0002

SER 75 LYS 76 0.0093

LYS 76 ASP 77 0.0000

ASP 77 ILE 78 -0.0000

ILE 78 PHE 79 -0.0008

PHE 79 VAL 80 0.0000

VAL 80 VAL 81 0.0002

VAL 81 SER 82 -0.0042

SER 82 SER 83 -0.0001

SER 83 ASP 84 0.0002

ASP 84 THR 85 -0.0087

THR 85 LEU 86 -0.0001

LEU 86 VAL 87 0.0002

VAL 87 GLU 88 -0.0092

GLU 88 THR 89 -0.0001

THR 89 PRO 90 -0.0001

PRO 90 VAL 91 -0.0282

VAL 91 VAL 92 0.0001

VAL 92 VAL 93 -0.0003

VAL 93 ASP 94 0.0038

ASP 94 LEU 95 0.0003

LEU 95 ILE 96 -0.0002

ILE 96 LYS 97 0.0266

LYS 97 LYS 98 0.0002

LYS 98 THR 99 0.0001

THR 99 MET 100 0.0037

MET 100 LEU 101 -0.0002

LEU 101 GLN 102 -0.0000

GLN 102 ILE 103 -0.0012

ILE 103 GLU 104 0.0001

GLU 104 ALA 105 0.0003

ALA 105 GLY 106 -0.0044

GLY 106 ALA 107 -0.0002

ALA 107 LYS 108 -0.0001

LYS 108 ARG 109 0.0016

ARG 109 ASN 110 -0.0004

ASN 110 GLY 111 0.0000

GLY 111 LEU 112 0.0059

LEU 112 PRO 113 -0.0001

PRO 113 ILE 114 0.0000

ILE 114 THR 115 -0.0143

THR 115 GLN 116 -0.0000

GLN 116 HIS 117 0.0004

HIS 117 ALA 118 -0.0513

ALA 118 VAL 119 -0.0001

VAL 119 THR 120 0.0001

THR 120 PRO 121 -0.0482

PRO 121 LYS 122 0.0001

LYS 122 THR 123 -0.0003

THR 123 ASN 124 -0.0001

ASN 124 GLU 125 0.0000

GLU 125 THR 126 0.0001

THR 126 PHE 127 0.0024

PHE 127 TRP 128 0.0002

TRP 128 VAL 129 0.0002

VAL 129 ASN 130 0.0060

ASN 130 LEU 131 -0.0004

LEU 131 LEU 132 0.0001

LEU 132 GLY 133 -0.0012

GLY 133 LYS 134 -0.0002

LYS 134 GLY 135 -0.0001

GLY 135 TYR 136 0.0167

TYR 136 PRO 137 -0.0001

PRO 137 ALA 138 0.0002

ALA 138 PRO 139 0.0021

PRO 139 THR 140 -0.0001

THR 140 ARG 141 0.0002

ARG 141 SER 142 -0.0088

SER 142 PHE 143 0.0002

PHE 143 ARG 144 0.0001

ARG 144 TRP 145 -0.0085

TRP 145 CYS 146 0.0001

CYS 146 THR 147 -0.0001

THR 147 GLU 148 -0.0020

GLU 148 ARG 149 0.0003

ARG 149 MET 150 -0.0003

MET 150 LYS 151 0.0148

LYS 151 ILE 152 -0.0001

ILE 152 ASN 153 0.0002

ASN 153 PRO 154 -0.0081

PRO 154 VAL 155 0.0002

VAL 155 SER 156 0.0004

SER 156 ASP 157 0.0057

ASP 157 PHE 158 -0.0003

PHE 158 ILE 159 -0.0003

ILE 159 LYS 160 -0.0115

LYS 160 ASP 161 -0.0002

ASP 161 LYS 162 -0.0001

LYS 162 VAL 163 -0.0136

VAL 163 SER 164 0.0003

SER 164 GLN 165 0.0000

GLN 165 PHE 166 -0.0000

PHE 166 ASP 167 -0.0004

ASP 167 GLU 168 -0.0000

GLU 168 VAL 169 -0.0054

VAL 169 ILE 170 0.0001

ILE 170 VAL 171 -0.0002

VAL 171 VAL 172 -0.0062

VAL 172 LEU 173 -0.0000

LEU 173 GLY 174 0.0000

GLY 174 SER 175 0.0101

SER 175 ARG 176 -0.0002

ARG 176 SER 177 -0.0002

SER 177 SER 178 0.0048

SER 178 GLU 179 0.0001

GLU 179 SER 180 0.0002

SER 180 ALA 181 0.0021

ALA 181 SER 182 0.0001

SER 182 ARG 183 0.0002

ARG 183 ALA 184 0.0014

ALA 184 GLN 185 0.0002

GLN 185 VAL 186 0.0002

VAL 186 ILE 187 0.0034

ILE 187 ALA 188 0.0000

ALA 188 LYS 189 0.0002

LYS 189 HIS 190 -0.0002

HIS 190 LYS 191 0.0001

LYS 191 ILE 192 0.0001

ILE 192 ASP 193 0.0032

ASP 193 GLY 194 0.0002

GLY 194 SER 195 -0.0001

SER 195 ARG 196 0.0047

ARG 196 LEU 197 -0.0000

LEU 197 ALA 198 -0.0004

ALA 198 ARG 199 0.0052

ARG 199 HIS 200 -0.0001

HIS 200 THR 201 -0.0001

THR 201 THR 202 0.0041

THR 202 LEU 203 -0.0002

LEU 203 ALA 204 0.0000

ALA 204 ASN 205 0.0109

ASN 205 ALA 206 0.0000

ALA 206 PHE 207 0.0003

PHE 207 ILE 208 -0.0092

ILE 208 TYR 209 -0.0001

TYR 209 THR 210 -0.0004

THR 210 PRO 211 -0.0039

PRO 211 ILE 212 -0.0004

ILE 212 ASP 213 -0.0002

ASP 213 THR 214 -0.0036

THR 214 TRP 215 0.0003

TRP 215 ASP 216 -0.0002

ASP 216 VAL 217 0.0046

VAL 217 GLU 218 -0.0001

GLU 218 ASP 219 0.0003

ASP 219 VAL 220 0.0004

VAL 220 TRP 221 -0.0002

TRP 221 LYS 222 0.0005

LYS 222 LEU 223 -0.0008

LEU 223 LEU 224 -0.0004

LEU 224 ARG 225 0.0001

ARG 225 GLY 226 -0.0004

GLY 226 ALA 227 -0.0004

ALA 227 PHE 228 -0.0001

PHE 228 ARG 229 -0.0049

ARG 229 TYR 230 0.0002

TYR 230 ALA 231 -0.0002

ALA 231 PRO 232 -0.0006

PRO 232 GLU 233 0.0001

GLU 233 ASP 234 -0.0001

ASP 234 ILE 235 -0.0013

ILE 235 ASP 236 0.0002

ASP 236 GLU 237 -0.0005

GLU 237 TRP 238 0.0037

TRP 238 GLU 239 0.0005

GLU 239 SER 240 -0.0002

SER 240 PRO 241 0.0160

PRO 241 TRP 242 0.0001

TRP 242 GLY 243 0.0001

GLY 243 GLY 244 0.0176

GLY 244 ASN 245 -0.0000

ASN 245 ASN 246 0.0000

ASN 246 ARG 247 0.0047

ARG 247 PRO 248 -0.0001

PRO 248 LEU 249 0.0003

LEU 249 TRP 250 -0.0084

TRP 250 THR 251 0.0003

THR 251 LEU 252 0.0002

LEU 252 TYR 253 -0.0080

TYR 253 MET 254 -0.0001

MET 254 ASP 255 -0.0004

ASP 255 SER 256 0.0018

SER 256 SER 257 -0.0001

SER 257 ALA 258 0.0002

ALA 258 GLN 259 0.0365

GLN 259 GLY 260 0.0000

GLY 260 GLU 261 0.0003

GLU 261 CYS 262 0.0075

CYS 262 PRO 263 0.0002

PRO 263 LEU 264 -0.0000

LEU 264 VAL 265 -0.0025

VAL 265 ILE 266 0.0002

ILE 266 ASP 267 -0.0002

ASP 267 ASP 268 -0.0028

ASP 268 SER 269 -0.0000

SER 269 THR 270 0.0002

THR 270 PRO 271 0.0171

PRO 271 SER 272 -0.0001

SER 272 CYS 273 0.0001

CYS 273 GLY 274 0.0342

GLY 274 ASN 275 -0.0003

ASN 275 SER 276 0.0001

SER 276 ARG 277 0.0501

ARG 277 PHE 278 0.0003

PHE 278 GLY 279 0.0000

GLY 279 CYS 280 0.0229

CYS 280 TRP 281 0.0003

TRP 281 THR 282 0.0000

THR 282 CYS 283 -0.0118

CYS 283 THR 284 -0.0002

THR 284 VAL 285 0.0004

VAL 285 VAL 286 -0.0084

VAL 286 THR 287 0.0001

THR 287 LYS 288 0.0001

LYS 288 ASP 289 0.0165

ASP 289 LYS 290 -0.0001

LYS 290 ALA 291 -0.0002

ALA 291 MET 292 0.0208

MET 292 GLU 293 -0.0001

GLU 293 SER 294 0.0002

SER 294 LEU 295 -0.0012

LEU 295 ILE 296 0.0001

ILE 296 LYS 297 0.0001

LYS 297 ASN 298 -0.0107

ASN 298 GLY 299 0.0002

GLY 299 GLU 300 -0.0000

GLU 300 GLU 301 -0.0090

GLU 301 TRP 302 -0.0004

TRP 302 MET 303 -0.0001

MET 303 SER 304 -0.0144

SER 304 PRO 305 0.0000

PRO 305 LEU 306 -0.0002

LEU 306 LEU 307 0.0045

LEU 307 LYS 308 0.0000

LYS 308 TYR 309 -0.0002

TYR 309 ARG 310 0.0051

ARG 310 ASP 311 -0.0002

ASP 311 LEU 312 0.0005

LEU 312 LEU 313 -0.0067

LEU 313 ALA 314 -0.0000

ALA 314 PHE 315 0.0001

PHE 315 THR 316 0.0217

THR 316 THR 317 -0.0001

THR 317 ASP 318 -0.0002

ASP 318 PRO 319 0.0206

PRO 319 VAL 320 -0.0003

VAL 320 ASN 321 0.0001

ASN 321 LYS 322 -0.0085

LYS 322 ASP 323 0.0001

ASP 323 THR 324 -0.0001

THR 324 PHE 325 -0.0194

PHE 325 ARG 326 -0.0001

ARG 326 ASN 327 0.0001

ASN 327 TYR 328 -0.0320

TYR 328 LYS 329 -0.0002

LYS 329 ARG 330 -0.0001

ARG 330 ARG 331 0.0767

ARG 331 THR 332 -0.0001

THR 332 GLY 333 -0.0001

GLY 333 LYS 334 -0.0151

LYS 334 VAL 335 0.0001

VAL 335 SER 336 -0.0002

SER 336 TYR 337 0.0435

TYR 337 GLN 338 -0.0001

GLN 338 TYR 339 0.0000

TYR 339 ALA 340 0.0666

ALA 340 LYS 341 -0.0000

LYS 341 GLU 342 0.0002

GLU 342 SER 343 0.0178

SER 343 ASP 344 -0.0000

ASP 344 GLU 345 0.0001

GLU 345 PRO 346 -0.0079

PRO 346 GLY 347 -0.0000

GLY 347 ALA 348 0.0000

ALA 348 GLU 349 -0.0495

GLU 349 ARG 350 -0.0001

ARG 350 LYS 351 0.0001

LYS 351 HIS 352 -0.0485

HIS 352 VAL 353 -0.0002

VAL 353 PRO 354 0.0002

PRO 354 GLY 355 0.0494

GLY 355 PRO 356 -0.0003

PRO 356 TYR 357 -0.0000

TYR 357 TRP 358 0.0374

TRP 358 LEU 359 0.0001

LEU 359 LYS 360 -0.0001

LYS 360 TYR 361 -0.0001

TYR 361 ARG 362 0.0003

ARG 362 GLN 363 0.0003

GLN 363 GLN 364 0.0265

GLN 364 TRP 365 0.0002

TRP 365 LEU 366 0.0000

LEU 366 LYS 367 0.0089

LYS 367 GLU 368 0.0001

GLU 368 LEU 369 0.0001

LEU 369 LEU 370 0.0054

LEU 370 GLU 371 -0.0000

GLU 371 ILE 372 -0.0001

ILE 372 GLU 373 -0.0099

GLU 373 ARG 374 -0.0000

ARG 374 ASP 375 -0.0004

ASP 375 LEU 376 -0.0159

LEU 376 ASN 377 -0.0000

ASN 377 ALA 378 0.0002

ALA 378 GLN 379 -0.0014

GLN 379 GLY 380 0.0006

GLY 380 HIS 381 0.0001

HIS 381 THR 382 0.0213

THR 382 ILE 383 0.0001

ILE 383 THR 384 -0.0000

THR 384 LEU 385 0.0070

LEU 385 ILE 386 0.0000

ILE 386 THR 387 0.0003

THR 387 LYS 388 -0.0214

LYS 388 PRO 389 -0.0002

PRO 389 GLU 390 -0.0001

GLU 390 LEU 391 -0.0094

LEU 391 HIS 392 -0.0001

HIS 392 ALA 393 0.0001

ALA 393 ILE 394 -0.0048

ILE 394 ARG 395 0.0001

ARG 395 GLN 396 0.0002

GLN 396 GLU 397 0.0127

GLU 397 TRP 398 -0.0001

TRP 398 LEU 399 0.0001

LEU 399 LYS 400 0.0019

LYS 400 ASP 401 -0.0004

ASP 401 PRO 402 0.0002

PRO 402 ASN 403 0.0050

ASN 403 GLU 404 0.0002

GLU 404 PRO 405 0.0003

PRO 405 ASP 406 -0.0122

ASP 406 TRP 407 -0.0001

TRP 407 TYR 408 0.0000

TYR 408 ASP 409 -0.0260

ASP 409 THR 410 -0.0001

THR 410 LEU 411 0.0001

LEU 411 PRO 412 -0.0037

PRO 412 GLY 413 -0.0004

GLY 413 ILE 414 0.0001

ILE 414 TYR 415 -0.0079

TYR 415 ARG 416 -0.0000

ARG 416 GLU 417 -0.0003

GLU 417 VAL 418 -0.0115

VAL 418 TYR 419 0.0001

TYR 419 GLN 420 -0.0001

GLN 420 GLN 421 0.0082

GLN 421 ASP 422 0.0001

ASP 422 LEU 423 -0.0006

LEU 423 ASP 424 0.0029

ASP 424 TRP 425 0.0003

TRP 425 VAL 426 -0.0000

VAL 426 VAL 427 -0.0221

VAL 427 ASP 428 0.0004

ASP 428 ASP 429 -0.0000

ASP 429 GLN 430 -0.0013

GLN 430 SER 431 0.0000

SER 431 ARG 432 0.0000

ARG 432 PHE 433 0.0005

PHE 433 ASP 434 -0.0001

ASP 434 ALA 435 -0.0000

ALA 435 SER 436 -0.0029

SER 436 ASP 437 -0.0003

ASP 437 ALA 438 -0.0001

ALA 438 ASP 439 -0.0001

ASP 439 LEU 440 -0.0000

LEU 440 LEU 441 -0.0002

LEU 441 VAL 442 -0.0009

VAL 442 GLN 443 -0.0001

GLN 443 ILE 444 0.0000

ILE 444 ALA 445 0.0037

ALA 445 GLN 446 0.0001

GLN 446 GLY 447 -0.0001

GLY 447 PHE 448 0.0007

PHE 448 ASP 449 -0.0002

ASP 449 VAL 450 -0.0001

VAL 450 VAL 451 0.0062

VAL 451 PRO 452 -0.0000

PRO 452 GLU 453 -0.0001

GLU 453 MET 454 0.0030

MET 454 VAL 455 -0.0001

VAL 455 MET 456 0.0001

MET 456 LYS 457 -0.0013

LYS 457 LEU 458 -0.0001

LEU 458 ILE 459 -0.0001

ILE 459 GLU 460 -0.0026

GLU 460 LEU 461 0.0004

LEU 461 GLU 462 -0.0001

GLU 462 VAL 463 -0.0044

VAL 463 SER 464 -0.0001

SER 464 MET 465 0.0001

MET 465 GLU 466 -0.0009

GLU 466 GLY 467 0.0003

GLY 467 LEU 468 0.0000

LEU 468 SER 469 -0.0037

SER 469 ARG 470 -0.0002

ARG 470 ARG 471 -0.0001

ARG 471 GLN 472 0.0001

GLN 472 GLY 473 -0.0001

GLY 473 ILE 474 -0.0002

ILE 474 PHE 475 -0.0010

PHE 475 ASP 476 0.0003

ASP 476 LYS 477 -0.0000

LYS 477 LEU 478 -0.0006

LEU 478 GLY 479 0.0002

GLY 479 THR 480 0.0001

THR 480 ILE 481 0.0002

ILE 481 LEU 482 -0.0000

LEU 482 LYS 483 -0.0001

LYS 483 GLN 484 0.0134

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_truncation ***

CA strain for 250214072227131043

--- normal mode 7 ---

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

* dndc-4FS-rank3_truncation *