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

* dndc-4FS-rank3_truncation *

CA strain for 250214072227131043

--- 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 0.0000

SER 2 LYS 3 -0.0002

LYS 3 LEU 4 0.0101

LEU 4 VAL 5 -0.0000

VAL 5 GLN 6 0.0000

GLN 6 ALA 7 -0.0049

ALA 7 TYR 8 -0.0001

TYR 8 ASP 9 0.0004

ASP 9 LEU 10 -0.0034

LEU 10 ALA 11 0.0001

ALA 11 GLU 12 0.0004

GLU 12 TYR 13 -0.0009

TYR 13 GLU 14 -0.0000

GLU 14 ASP 15 0.0001

ASP 15 PHE 16 -0.0103

PHE 16 ILE 17 0.0001

ILE 17 ASN 18 -0.0000

ASN 18 GLN 19 0.0019

GLN 19 GLU 20 0.0003

GLU 20 GLN 21 -0.0000

GLN 21 PHE 22 -0.0010

PHE 22 ALA 23 0.0002

ALA 23 GLY 24 -0.0001

GLY 24 ARG 25 0.0038

ARG 25 PRO 26 -0.0003

PRO 26 LEU 27 0.0000

LEU 27 ALA 28 0.0027

ALA 28 GLU 29 -0.0001

GLU 29 TYR 30 0.0001

TYR 30 VAL 31 0.0098

VAL 31 ALA 32 -0.0000

ALA 32 GLU 33 0.0002

GLU 33 VAL 34 -0.0004

VAL 34 GLN 35 -0.0001

GLN 35 ARG 36 0.0001

ARG 36 ILE 37 -0.0033

ILE 37 TYR 38 0.0001

TYR 38 CYS 39 -0.0002

CYS 39 ALA 40 -0.0155

ALA 40 ASP 41 0.0003

ASP 41 LYS 42 -0.0005

LYS 42 ARG 43 0.0026

ARG 43 PRO 44 0.0002

PRO 44 TRP 45 -0.0003

TRP 45 VAL 46 0.0027

VAL 46 ILE 47 0.0001

ILE 47 GLY 48 0.0001

GLY 48 TYR 49 0.0019

TYR 49 SER 50 0.0002

SER 50 GLY 51 0.0001

GLY 51 GLY 52 -0.0265

GLY 52 LYS 53 0.0000

LYS 53 ASP 54 0.0002

ASP 54 SER 55 -0.0059

SER 55 SER 56 -0.0002

SER 56 ALA 57 0.0000

ALA 57 VAL 58 0.0053

VAL 58 ILE 59 0.0002

ILE 59 THR 60 0.0001

THR 60 LEU 61 -0.0029

LEU 61 VAL 62 0.0002

VAL 62 TYR 63 0.0002

TYR 63 LEU 64 0.0101

LEU 64 ALA 65 -0.0004

ALA 65 LEU 66 -0.0002

LEU 66 LEU 67 0.0039

LEU 67 GLY 68 -0.0002

GLY 68 LEU 69 -0.0001

LEU 69 PRO 70 -0.0030

PRO 70 PRO 71 -0.0000

PRO 71 GLU 72 0.0000

GLU 72 MET 73 0.0017

MET 73 ARG 74 0.0002

ARG 74 SER 75 -0.0001

SER 75 LYS 76 0.0102

LYS 76 ASP 77 -0.0001

ASP 77 ILE 78 0.0000

ILE 78 PHE 79 0.0244

PHE 79 VAL 80 0.0001

VAL 80 VAL 81 0.0001

VAL 81 SER 82 0.0096

SER 82 SER 83 0.0003

SER 83 ASP 84 0.0003

ASP 84 THR 85 0.0325

THR 85 LEU 86 0.0000

LEU 86 VAL 87 0.0000

VAL 87 GLU 88 0.0389

GLU 88 THR 89 0.0001

THR 89 PRO 90 -0.0000

PRO 90 VAL 91 0.0399

VAL 91 VAL 92 -0.0003

VAL 92 VAL 93 0.0002

VAL 93 ASP 94 0.0503

ASP 94 LEU 95 0.0001

LEU 95 ILE 96 0.0001

ILE 96 LYS 97 -0.0124

LYS 97 LYS 98 -0.0001

LYS 98 THR 99 -0.0001

THR 99 MET 100 -0.0102

MET 100 LEU 101 0.0000

LEU 101 GLN 102 -0.0004

GLN 102 ILE 103 -0.0182

ILE 103 GLU 104 0.0001

GLU 104 ALA 105 0.0004

ALA 105 GLY 106 0.0079

GLY 106 ALA 107 0.0001

ALA 107 LYS 108 0.0003

LYS 108 ARG 109 0.0053

ARG 109 ASN 110 -0.0001

ASN 110 GLY 111 -0.0000

GLY 111 LEU 112 0.0077

LEU 112 PRO 113 0.0002

PRO 113 ILE 114 0.0000

ILE 114 THR 115 0.0496

THR 115 GLN 116 -0.0000

GLN 116 HIS 117 -0.0003

HIS 117 ALA 118 0.0932

ALA 118 VAL 119 -0.0002

VAL 119 THR 120 -0.0002

THR 120 PRO 121 0.1410

PRO 121 LYS 122 0.0000

LYS 122 THR 123 -0.0001

THR 123 ASN 124 0.0105

ASN 124 GLU 125 0.0001

GLU 125 THR 126 -0.0001

THR 126 PHE 127 0.0004

PHE 127 TRP 128 -0.0001

TRP 128 VAL 129 -0.0004

VAL 129 ASN 130 -0.0160

ASN 130 LEU 131 -0.0004

LEU 131 LEU 132 -0.0000

LEU 132 GLY 133 -0.0135

GLY 133 LYS 134 -0.0001

LYS 134 GLY 135 0.0001

GLY 135 TYR 136 -0.0282

TYR 136 PRO 137 0.0003

PRO 137 ALA 138 -0.0003

ALA 138 PRO 139 0.0009

PRO 139 THR 140 0.0003

THR 140 ARG 141 0.0000

ARG 141 SER 142 -0.0141

SER 142 PHE 143 -0.0003

PHE 143 ARG 144 -0.0002

ARG 144 TRP 145 -0.0030

TRP 145 CYS 146 0.0004

CYS 146 THR 147 0.0001

THR 147 GLU 148 0.0017

GLU 148 ARG 149 -0.0001

ARG 149 MET 150 0.0000

MET 150 LYS 151 0.0091

LYS 151 ILE 152 0.0001

ILE 152 ASN 153 0.0001

ASN 153 PRO 154 0.0518

PRO 154 VAL 155 -0.0000

VAL 155 SER 156 0.0002

SER 156 ASP 157 0.0056

ASP 157 PHE 158 -0.0004

PHE 158 ILE 159 0.0000

ILE 159 LYS 160 -0.0040

LYS 160 ASP 161 0.0003

ASP 161 LYS 162 0.0002

LYS 162 VAL 163 -0.0133

VAL 163 SER 164 0.0002

SER 164 GLN 165 0.0000

GLN 165 PHE 166 0.0099

PHE 166 ASP 167 0.0001

ASP 167 GLU 168 -0.0002

GLU 168 VAL 169 -0.0035

VAL 169 ILE 170 -0.0003

ILE 170 VAL 171 -0.0001

VAL 171 VAL 172 -0.0000

VAL 172 LEU 173 0.0004

LEU 173 GLY 174 0.0000

GLY 174 SER 175 -0.0144

SER 175 ARG 176 0.0003

ARG 176 SER 177 0.0001

SER 177 SER 178 0.0096

SER 178 GLU 179 -0.0001

GLU 179 SER 180 -0.0001

SER 180 ALA 181 0.0275

ALA 181 SER 182 0.0001

SER 182 ARG 183 0.0001

ARG 183 ALA 184 -0.0052

ALA 184 GLN 185 0.0002

GLN 185 VAL 186 0.0000

VAL 186 ILE 187 -0.0063

ILE 187 ALA 188 0.0002

ALA 188 LYS 189 0.0003

LYS 189 HIS 190 0.0037

HIS 190 LYS 191 0.0003

LYS 191 ILE 192 0.0000

ILE 192 ASP 193 -0.0072

ASP 193 GLY 194 -0.0002

GLY 194 SER 195 0.0003

SER 195 ARG 196 0.0088

ARG 196 LEU 197 -0.0001

LEU 197 ALA 198 0.0003

ALA 198 ARG 199 -0.0208

ARG 199 HIS 200 -0.0004

HIS 200 THR 201 0.0004

THR 201 THR 202 -0.0192

THR 202 LEU 203 0.0001

LEU 203 ALA 204 0.0002

ALA 204 ASN 205 -0.0042

ASN 205 ALA 206 0.0003

ALA 206 PHE 207 0.0001

PHE 207 ILE 208 0.0039

ILE 208 TYR 209 -0.0001

TYR 209 THR 210 0.0000

THR 210 PRO 211 -0.0036

PRO 211 ILE 212 -0.0003

ILE 212 ASP 213 -0.0000

ASP 213 THR 214 -0.0058

THR 214 TRP 215 -0.0001

TRP 215 ASP 216 0.0002

ASP 216 VAL 217 0.0118

VAL 217 GLU 218 -0.0001

GLU 218 ASP 219 -0.0001

ASP 219 VAL 220 -0.0031

VAL 220 TRP 221 -0.0003

TRP 221 LYS 222 -0.0001

LYS 222 LEU 223 -0.0002

LEU 223 LEU 224 0.0001

LEU 224 ARG 225 -0.0001

ARG 225 GLY 226 -0.0094

GLY 226 ALA 227 -0.0003

ALA 227 PHE 228 -0.0002

PHE 228 ARG 229 0.0080

ARG 229 TYR 230 -0.0000

TYR 230 ALA 231 0.0004

ALA 231 PRO 232 -0.0004

PRO 232 GLU 233 0.0002

GLU 233 ASP 234 -0.0002

ASP 234 ILE 235 0.0137

ILE 235 ASP 236 0.0001

ASP 236 GLU 237 0.0001

GLU 237 TRP 238 -0.0071

TRP 238 GLU 239 0.0002

GLU 239 SER 240 -0.0000

SER 240 PRO 241 -0.0262

PRO 241 TRP 242 -0.0000

TRP 242 GLY 243 0.0000

GLY 243 GLY 244 -0.0574

GLY 244 ASN 245 -0.0003

ASN 245 ASN 246 0.0002

ASN 246 ARG 247 -0.0213

ARG 247 PRO 248 0.0003

PRO 248 LEU 249 -0.0001

LEU 249 TRP 250 0.0190

TRP 250 THR 251 0.0004

THR 251 LEU 252 -0.0002

LEU 252 TYR 253 -0.0038

TYR 253 MET 254 -0.0002

MET 254 ASP 255 -0.0004

ASP 255 SER 256 -0.0245

SER 256 SER 257 0.0001

SER 257 ALA 258 -0.0000

ALA 258 GLN 259 -0.0516

GLN 259 GLY 260 -0.0001

GLY 260 GLU 261 -0.0003

GLU 261 CYS 262 -0.0025

CYS 262 PRO 263 -0.0000

PRO 263 LEU 264 0.0001

LEU 264 VAL 265 -0.0001

VAL 265 ILE 266 -0.0002

ILE 266 ASP 267 -0.0000

ASP 267 ASP 268 -0.0017

ASP 268 SER 269 -0.0003

SER 269 THR 270 -0.0001

THR 270 PRO 271 -0.0178

PRO 271 SER 272 -0.0003

SER 272 CYS 273 0.0004

CYS 273 GLY 274 -0.0452

GLY 274 ASN 275 -0.0001

ASN 275 SER 276 0.0002

SER 276 ARG 277 -0.0995

ARG 277 PHE 278 0.0001

PHE 278 GLY 279 0.0003

GLY 279 CYS 280 -0.0438

CYS 280 TRP 281 -0.0004

TRP 281 THR 282 -0.0000

THR 282 CYS 283 0.0206

CYS 283 THR 284 0.0003

THR 284 VAL 285 -0.0000

VAL 285 VAL 286 -0.0024

VAL 286 THR 287 0.0002

THR 287 LYS 288 -0.0003

LYS 288 ASP 289 -0.0243

ASP 289 LYS 290 0.0000

LYS 290 ALA 291 -0.0002

ALA 291 MET 292 0.0009

MET 292 GLU 293 -0.0002

GLU 293 SER 294 -0.0003

SER 294 LEU 295 0.0010

LEU 295 ILE 296 -0.0001

ILE 296 LYS 297 0.0002

LYS 297 ASN 298 -0.0033

ASN 298 GLY 299 0.0001

GLY 299 GLU 300 -0.0001

GLU 300 GLU 301 0.0035

GLU 301 TRP 302 -0.0002

TRP 302 MET 303 0.0000

MET 303 SER 304 -0.0408

SER 304 PRO 305 0.0000

PRO 305 LEU 306 0.0000

LEU 306 LEU 307 0.0201

LEU 307 LYS 308 -0.0002

LYS 308 TYR 309 -0.0001

TYR 309 ARG 310 0.0242

ARG 310 ASP 311 -0.0002

ASP 311 LEU 312 0.0002

LEU 312 LEU 313 0.0158

LEU 313 ALA 314 -0.0003

ALA 314 PHE 315 0.0002

PHE 315 THR 316 -0.0312

THR 316 THR 317 0.0002

THR 317 ASP 318 -0.0003

ASP 318 PRO 319 -0.0179

PRO 319 VAL 320 -0.0002

VAL 320 ASN 321 0.0000

ASN 321 LYS 322 -0.0141

LYS 322 ASP 323 0.0004

ASP 323 THR 324 -0.0001

THR 324 PHE 325 -0.0193

PHE 325 ARG 326 -0.0001

ARG 326 ASN 327 0.0001

ASN 327 TYR 328 -0.0163

TYR 328 LYS 329 -0.0001

LYS 329 ARG 330 -0.0004

ARG 330 ARG 331 0.0693

ARG 331 THR 332 -0.0000

THR 332 GLY 333 -0.0004

GLY 333 LYS 334 0.0683

LYS 334 VAL 335 -0.0001

VAL 335 SER 336 -0.0001

SER 336 TYR 337 0.1253

TYR 337 GLN 338 -0.0002

GLN 338 TYR 339 0.0001

TYR 339 ALA 340 0.0768

ALA 340 LYS 341 0.0002

LYS 341 GLU 342 -0.0002

GLU 342 SER 343 0.0388

SER 343 ASP 344 -0.0001

ASP 344 GLU 345 -0.0003

GLU 345 PRO 346 -0.0130

PRO 346 GLY 347 0.0002

GLY 347 ALA 348 -0.0001

ALA 348 GLU 349 -0.0396

GLU 349 ARG 350 0.0001

ARG 350 LYS 351 -0.0001

LYS 351 HIS 352 -0.0251

HIS 352 VAL 353 -0.0003

VAL 353 PRO 354 0.0002

PRO 354 GLY 355 0.0208

GLY 355 PRO 356 0.0001

PRO 356 TYR 357 -0.0001

TYR 357 TRP 358 0.0070

TRP 358 LEU 359 0.0000

LEU 359 LYS 360 -0.0003

LYS 360 TYR 361 -0.0117

TYR 361 ARG 362 -0.0005

ARG 362 GLN 363 -0.0001

GLN 363 GLN 364 0.0008

GLN 364 TRP 365 -0.0002

TRP 365 LEU 366 0.0001

LEU 366 LYS 367 0.0083

LYS 367 GLU 368 0.0002

GLU 368 LEU 369 -0.0001

LEU 369 LEU 370 -0.0018

LEU 370 GLU 371 0.0002

GLU 371 ILE 372 0.0001

ILE 372 GLU 373 -0.0001

GLU 373 ARG 374 0.0000

ARG 374 ASP 375 0.0001

ASP 375 LEU 376 0.0314

LEU 376 ASN 377 -0.0001

ASN 377 ALA 378 -0.0003

ALA 378 GLN 379 0.0026

GLN 379 GLY 380 0.0002

GLY 380 HIS 381 0.0004

HIS 381 THR 382 0.0076

THR 382 ILE 383 -0.0001

ILE 383 THR 384 -0.0001

THR 384 LEU 385 -0.0153

LEU 385 ILE 386 -0.0000

ILE 386 THR 387 -0.0002

THR 387 LYS 388 0.0559

LYS 388 PRO 389 -0.0000

PRO 389 GLU 390 -0.0001

GLU 390 LEU 391 -0.0288

LEU 391 HIS 392 -0.0003

HIS 392 ALA 393 0.0000

ALA 393 ILE 394 -0.0088

ILE 394 ARG 395 -0.0001

ARG 395 GLN 396 0.0002

GLN 396 GLU 397 -0.0233

GLU 397 TRP 398 0.0004

TRP 398 LEU 399 0.0001

LEU 399 LYS 400 -0.0079

LYS 400 ASP 401 -0.0000

ASP 401 PRO 402 0.0001

PRO 402 ASN 403 -0.0043

ASN 403 GLU 404 -0.0002

GLU 404 PRO 405 0.0001

PRO 405 ASP 406 0.0154

ASP 406 TRP 407 -0.0002

TRP 407 TYR 408 0.0003

TYR 408 ASP 409 -0.0143

ASP 409 THR 410 0.0001

THR 410 LEU 411 0.0001

LEU 411 PRO 412 -0.0068

PRO 412 GLY 413 0.0001

GLY 413 ILE 414 -0.0004

ILE 414 TYR 415 -0.0079

TYR 415 ARG 416 0.0001

ARG 416 GLU 417 0.0001

GLU 417 VAL 418 0.0111

VAL 418 TYR 419 0.0004

TYR 419 GLN 420 0.0001

GLN 420 GLN 421 -0.0021

GLN 421 ASP 422 0.0000

ASP 422 LEU 423 -0.0000

LEU 423 ASP 424 0.0646

ASP 424 TRP 425 -0.0003

TRP 425 VAL 426 0.0001

VAL 426 VAL 427 0.0595

VAL 427 ASP 428 0.0002

ASP 428 ASP 429 0.0001

ASP 429 GLN 430 0.0632

GLN 430 SER 431 -0.0000

SER 431 ARG 432 0.0005

ARG 432 PHE 433 0.0124

PHE 433 ASP 434 0.0002

ASP 434 ALA 435 -0.0001

ALA 435 SER 436 0.0001

SER 436 ASP 437 -0.0001

ASP 437 ALA 438 -0.0003

ALA 438 ASP 439 0.0099

ASP 439 LEU 440 0.0001

LEU 440 LEU 441 0.0000

LEU 441 VAL 442 0.0089

VAL 442 GLN 443 -0.0000

GLN 443 ILE 444 0.0001

ILE 444 ALA 445 -0.0052

ALA 445 GLN 446 -0.0006

GLN 446 GLY 447 -0.0001

GLY 447 PHE 448 -0.0050

PHE 448 ASP 449 0.0001

ASP 449 VAL 450 -0.0002

VAL 450 VAL 451 -0.0221

VAL 451 PRO 452 0.0001

PRO 452 GLU 453 -0.0007

GLU 453 MET 454 -0.0120

MET 454 VAL 455 -0.0003

VAL 455 MET 456 -0.0005

MET 456 LYS 457 0.0042

LYS 457 LEU 458 -0.0004

LEU 458 ILE 459 -0.0001

ILE 459 GLU 460 0.0172

GLU 460 LEU 461 0.0000

LEU 461 GLU 462 -0.0001

GLU 462 VAL 463 0.0224

VAL 463 SER 464 -0.0001

SER 464 MET 465 -0.0003

MET 465 GLU 466 -0.0028

GLU 466 GLY 467 -0.0001

GLY 467 LEU 468 0.0001

LEU 468 SER 469 0.0155

SER 469 ARG 470 -0.0002

ARG 470 ARG 471 -0.0001

ARG 471 GLN 472 0.0002

GLN 472 GLY 473 0.0000

GLY 473 ILE 474 -0.0001

ILE 474 PHE 475 0.0009

PHE 475 ASP 476 -0.0001

ASP 476 LYS 477 -0.0003

LYS 477 LEU 478 -0.0097

LEU 478 GLY 479 0.0002

GLY 479 THR 480 -0.0002

THR 480 ILE 481 0.0042

ILE 481 LEU 482 -0.0002

LEU 482 LYS 483 -0.0001

LYS 483 GLN 484 -0.0093

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 9 ---

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

* dndc-4FS-rank3_truncation *