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

* 4fdo v/s 4p8l *

CA strain for 20122614375822011

--- normal mode 8 ---

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 7 THR 8 0.0003

THR 8 THR 9 -0.0001

THR 9 ALA 10 0.0551

ALA 10 THR 11 -0.0002

THR 11 ARG 12 0.0001

ARG 12 LEU 13 0.0528

LEU 13 THR 14 0.0001

THR 14 GLY 15 0.0002

GLY 15 TRP 16 0.1138

TRP 16 GLY 17 0.0002

GLY 17 ARG 18 -0.0002

ARG 18 THR 19 0.1416

THR 19 ALA 20 -0.0000

ALA 20 PRO 21 0.0000

PRO 21 SER 22 0.0565

SER 22 VAL 23 0.0002

VAL 23 ALA 24 -0.0002

ALA 24 ASN 25 0.0135

ASN 25 VAL 26 -0.0002

VAL 26 LEU 27 0.0002

LEU 27 ARG 28 0.0150

ARG 28 THR 29 -0.0000

THR 29 PRO 30 -0.0003

PRO 30 ASP 31 0.0284

ASP 31 ALA 32 -0.0001

ALA 32 GLU 33 -0.0002

GLU 33 MET 34 -0.0262

MET 34 ILE 35 0.0002

ILE 35 VAL 36 -0.0001

VAL 36 LYS 37 0.0037

LYS 37 ALA 38 -0.0001

ALA 38 VAL 39 0.0001

VAL 39 ALA 40 -0.0011

ALA 40 ARG 41 0.0002

ARG 41 VAL 42 -0.0001

VAL 42 ALA 43 0.0066

ALA 43 GLU 44 0.0001

GLU 44 SER 45 0.0003

SER 45 GLY 46 -0.0531

GLY 46 GLY 47 0.0005

GLY 47 GLY 48 -0.0002

GLY 48 ARG 49 0.0571

ARG 49 GLY 50 0.0001

GLY 50 ALA 51 -0.0001

ALA 51 ILE 52 0.0529

ILE 52 ALA 53 0.0002

ALA 53 ARG 54 -0.0003

ARG 54 GLY 55 0.2264

GLY 55 LEU 56 0.0002

LEU 56 GLY 57 -0.0003

GLY 57 ARG 58 -0.0074

ARG 58 SER 59 -0.0002

SER 59 TYR 60 0.0001

TYR 60 GLY 61 0.0835

GLY 61 ASP 62 0.0003

ASP 62 ASN 63 0.0000

ASN 63 ALA 64 -0.0238

ALA 64 GLN 65 -0.0001

GLN 65 ASN 66 0.0004

ASN 66 GLY 67 0.0421

GLY 67 GLY 68 0.0002

GLY 68 GLY 69 0.0003

GLY 69 LEU 70 0.0525

LEU 70 VAL 71 -0.0001

VAL 71 ILE 72 -0.0003

ILE 72 ASP 73 0.0760

ASP 73 MET 74 0.0001

MET 74 THR 75 -0.0003

THR 75 PRO 76 -0.0597

PRO 76 LEU 77 0.0005

LEU 77 ASN 78 -0.0002

ASN 78 THR 79 0.0318

THR 79 ILE 80 -0.0001

ILE 80 HIS 81 0.0001

HIS 81 SER 82 -0.0488

SER 82 ILE 83 0.0002

ILE 83 ASP 84 -0.0000

ASP 84 ALA 85 -0.0127

ALA 85 ASP 86 -0.0002

ASP 86 THR 87 0.0002

THR 87 LYS 88 -0.0056

LYS 88 LEU 89 -0.0001

LEU 89 VAL 90 -0.0000

VAL 90 ASP 91 -0.0329

ASP 91 ILE 92 -0.0001

ILE 92 ASP 93 0.0003

ASP 93 ALA 94 -0.0503

ALA 94 GLY 95 -0.0003

GLY 95 VAL 96 -0.0004

VAL 96 ASN 97 0.0734

ASN 97 LEU 98 -0.0000

LEU 98 ASP 99 -0.0002

ASP 99 GLN 100 -0.1329

GLN 100 LEU 101 -0.0001

LEU 101 MET 102 0.0001

MET 102 LYS 103 -0.0524

LYS 103 ALA 104 -0.0002

ALA 104 ALA 105 -0.0000

ALA 105 LEU 106 0.0876

LEU 106 PRO 107 0.0001

PRO 107 PHE 108 0.0001

PHE 108 GLY 109 0.0690

GLY 109 LEU 110 0.0003

LEU 110 TRP 111 -0.0001

TRP 111 VAL 112 0.0032

VAL 112 PRO 113 0.0002

PRO 113 VAL 114 -0.0003

VAL 114 LEU 115 -0.0530

LEU 115 PRO 116 0.0000

PRO 116 GLY 117 -0.0000

GLY 117 THR 118 -0.0104

THR 118 ARG 119 -0.0002

ARG 119 GLN 120 0.0002

GLN 120 VAL 121 0.0265

VAL 121 THR 122 0.0001

THR 122 VAL 123 -0.0001

VAL 123 GLY 124 0.0110

GLY 124 GLY 125 0.0005

GLY 125 ALA 126 -0.0001

ALA 126 ILE 127 -0.0037

ILE 127 ALA 128 -0.0004

ALA 128 CYS 129 0.0001

CYS 129 ASP 130 -0.0065

ASP 130 ILE 131 -0.0004

ILE 131 HIS 132 -0.0000

HIS 132 GLY 133 -0.0235

GLY 133 LYS 134 0.0002

LYS 134 ASN 135 -0.0002

ASN 135 HIS 136 -0.0385

HIS 136 HIS 137 -0.0002

HIS 137 SER 138 0.0002

SER 138 ALA 139 0.0151

ALA 139 GLY 140 0.0002

GLY 140 SER 141 -0.0002

SER 141 PHE 142 0.0490

PHE 142 GLY 143 0.0003

GLY 143 ASN 144 -0.0001

ASN 144 HIS 145 0.0766

HIS 145 VAL 146 0.0005

VAL 146 ARG 147 -0.0002

ARG 147 SER 148 -0.1567

SER 148 MET 149 0.0006

MET 149 ASP 150 -0.0004

ASP 150 LEU 151 -0.0235

LEU 151 LEU 152 0.0002

LEU 152 THR 153 -0.0001

THR 153 ALA 154 -0.0165

ALA 154 ASP 155 0.0001

ASP 155 GLY 156 -0.0002

GLY 156 GLU 157 -0.0524

GLU 157 ILE 158 -0.0003

ILE 158 ARG 159 0.0002

ARG 159 HIS 160 -0.0798

HIS 160 LEU 161 -0.0002

LEU 161 THR 162 0.0003

THR 162 PRO 163 0.0514

PRO 163 THR 164 -0.0002

THR 164 GLY 165 0.0005

GLY 165 GLU 166 -0.0246

GLU 166 ASP 167 -0.0000

ASP 167 ALA 168 -0.0000

ALA 168 GLU 169 0.0334

GLU 169 LEU 170 0.0004

LEU 170 PHE 171 -0.0001

PHE 171 TRP 172 0.0345

TRP 172 ALA 173 -0.0004

ALA 173 THR 174 0.0002

THR 174 VAL 175 -0.0351

VAL 175 GLY 176 0.0000

GLY 176 GLY 177 -0.0002

GLY 177 ASN 178 -0.0181

ASN 178 GLY 179 -0.0005

GLY 179 LEU 180 0.0002

LEU 180 THR 181 0.0101

THR 181 GLY 182 -0.0003

GLY 182 ILE 183 0.0004

ILE 183 ILE 184 0.0277

ILE 184 MET 185 0.0001

MET 185 ARG 186 0.0002

ARG 186 ALA 187 -0.0309

ALA 187 THR 188 0.0002

THR 188 ILE 189 -0.0000

ILE 189 GLU 190 -0.0712

GLU 190 MET 191 -0.0002

MET 191 THR 192 0.0001

THR 192 PRO 193 -0.2019

PRO 193 THR 194 -0.0004

THR 194 SER 195 0.0005

SER 195 THR 196 -0.0988

THR 196 ALA 197 -0.0004

ALA 197 TYR 198 0.0002

TYR 198 PHE 199 -0.0560

PHE 199 ILE 200 -0.0000

ILE 200 ALA 201 -0.0004

ALA 201 ASP 202 0.0218

ASP 202 GLY 203 0.0000

GLY 203 ASP 204 0.0002

ASP 204 VAL 205 0.0230

VAL 205 THR 206 0.0000

THR 206 ALA 207 0.0001

ALA 207 SER 208 -0.0571

SER 208 LEU 209 0.0001

LEU 209 ASP 210 -0.0001

ASP 210 GLU 211 -0.0368

GLU 211 THR 212 0.0000

THR 212 ILE 213 -0.0001

ILE 213 ALA 214 -0.0257

ALA 214 LEU 215 0.0001

LEU 215 HIS 216 0.0001

HIS 216 SER 217 0.0114

SER 217 ASP 218 0.0000

ASP 218 GLY 219 0.0001

GLY 219 SER 220 -0.0155

SER 220 GLU 221 0.0003

GLU 221 ALA 222 0.0002

ALA 222 ARG 223 0.0158

ARG 223 TYR 224 0.0002

TYR 224 THR 225 -0.0002

THR 225 TYR 226 0.0539

TYR 226 SER 227 0.0001

SER 227 SER 228 0.0001

SER 228 ALA 229 -0.0314

ALA 229 TRP 230 -0.0001

TRP 230 PHE 231 0.0002

PHE 231 ASP 232 -0.0726

ASP 232 ALA 233 -0.0000

ALA 233 ILE 234 -0.0001

ILE 234 SER 235 -0.0004

SER 235 ALA 236 0.0002

ALA 236 PRO 237 0.0001

PRO 237 PRO 238 0.0049

PRO 238 LYS 239 0.0000

LYS 239 LEU 240 -0.0002

LEU 240 GLY 241 -0.0203

GLY 241 ARG 242 0.0004

ARG 242 ALA 243 0.0001

ALA 243 ALA 244 -0.0597

ALA 244 VAL 245 -0.0002

VAL 245 SER 246 -0.0001

SER 246 ARG 247 0.0188

ARG 247 GLY 248 0.0001

GLY 248 ARG 249 0.0000

ARG 249 LEU 250 0.1152

LEU 250 ALA 251 -0.0002

ALA 251 THR 252 -0.0002

THR 252 VAL 253 -0.0185

VAL 253 GLU 254 0.0002

GLU 254 GLN 255 -0.0002

GLN 255 LEU 256 -0.0082

LEU 256 PRO 257 -0.0001

PRO 257 ALA 258 0.0002

ALA 258 LYS 259 0.0574

LYS 259 LEU 260 0.0004

LEU 260 ARG 261 0.0001

ARG 261 SER 262 0.0372

SER 262 GLU 263 -0.0001

GLU 263 PRO 264 -0.0002

PRO 264 LEU 265 0.1149

LEU 265 LYS 266 0.0001

LYS 266 PHE 267 -0.0001

PHE 267 ASP 268 -0.0921

ASP 268 ARG 298 0.2002

ARG 298 LYS 299 0.0001

LYS 299 SER 300 0.0001

SER 300 GLY 301 0.3243

GLY 301 THR 302 0.0001

THR 302 TYR 303 0.0002

TYR 303 ARG 304 -0.1377

ARG 304 GLY 305 0.0002

GLY 305 LYS 306 -0.0002

LYS 306 VAL 307 -0.0707

VAL 307 GLN 308 0.0000

GLN 308 ASN 309 -0.0000

ASN 309 LEU 310 0.0763

LEU 310 THR 311 0.0001

THR 311 GLN 312 -0.0003

GLN 312 PHE 313 -0.1327

PHE 313 TYR 314 -0.0002

TYR 314 HIS 315 0.0000

HIS 315 PRO 316 0.1233

PRO 316 LEU 317 -0.0001

LEU 317 ASP 318 -0.0001

ASP 318 MET 319 -0.1764

MET 319 PHE 320 0.0003

PHE 320 GLY 321 -0.0000

GLY 321 GLU 322 0.0788

GLU 322 TRP 323 0.0001

TRP 323 ASN 324 -0.0004

ASN 324 ARG 325 0.0079

ARG 325 ALA 326 -0.0004

ALA 326 TYR 327 -0.0000

TYR 327 GLY 328 0.0940

GLY 328 PRO 329 -0.0002

PRO 329 ALA 330 0.0001

ALA 330 GLY 331 0.0250

GLY 331 PHE 332 0.0000

PHE 332 LEU 333 0.0001

LEU 333 GLN 334 -0.0566

GLN 334 TYR 335 -0.0001

TYR 335 GLN 336 -0.0003

GLN 336 PHE 337 -0.0156

PHE 337 VAL 338 -0.0003

VAL 338 ILE 339 -0.0001

ILE 339 PRO 340 0.0139

PRO 340 THR 341 -0.0002

THR 341 GLU 342 0.0002

GLU 342 ALA 343 0.0393

ALA 343 VAL 344 -0.0003

VAL 344 ASP 345 -0.0003

ASP 345 GLU 346 -0.0298

GLU 346 PHE 347 -0.0002

PHE 347 LYS 348 0.0002

LYS 348 LYS 349 -0.0320

LYS 349 ILE 350 0.0000

ILE 350 ILE 351 -0.0000

ILE 351 GLY 352 0.0095

GLY 352 VAL 353 -0.0000

VAL 353 ILE 354 -0.0000

ILE 354 GLN 355 0.0166

GLN 355 ALA 356 0.0004

ALA 356 SER 357 -0.0003

SER 357 GLY 358 -0.0048

GLY 358 HIS 359 0.0001

HIS 359 TYR 360 -0.0003

TYR 360 SER 361 -0.0468

SER 361 PHE 362 0.0002

PHE 362 LEU 363 0.0004

LEU 363 ASN 364 0.0045

ASN 364 VAL 365 0.0000

VAL 365 PHE 366 0.0002

PHE 366 LYS 367 -0.0235

LYS 367 LEU 368 0.0001

LEU 368 PHE 369 -0.0001

PHE 369 GLY 370 -0.0135

GLY 370 PRO 371 0.0001

PRO 371 ARG 372 -0.0003

ARG 372 ASN 373 0.0602

ASN 373 GLN 374 0.0000

GLN 374 ALA 375 0.0003

ALA 375 PRO 376 0.0277

PRO 376 LEU 377 0.0004

LEU 377 SER 378 0.0002

SER 378 PHE 379 -0.0002

PHE 379 PRO 380 0.0003

PRO 380 ILE 381 -0.0003

ILE 381 PRO 382 -0.0355

PRO 382 GLY 383 -0.0004

GLY 383 TRP 384 0.0003

TRP 384 ASN 385 -0.0042

ASN 385 ILE 386 0.0002

ILE 386 CYS 387 0.0000

CYS 387 VAL 388 -0.0303

VAL 388 ASP 389 -0.0003

ASP 389 PHE 390 0.0003

PHE 390 PRO 391 0.0129

PRO 391 ILE 392 -0.0003

ILE 392 LYS 393 -0.0001

LYS 393 ASP 394 -0.0448

ASP 394 GLY 395 -0.0000

GLY 395 LEU 396 0.0002

LEU 396 GLY 397 0.0431

GLY 397 LYS 398 0.0001

LYS 398 PHE 399 -0.0001

PHE 399 VAL 400 0.0066

VAL 400 SER 401 0.0001

SER 401 GLU 402 0.0002

GLU 402 LEU 403 0.0025

LEU 403 ASP 404 -0.0000

ASP 404 ARG 405 0.0002

ARG 405 ARG 406 -0.0400

ARG 406 VAL 407 0.0004

VAL 407 LEU 408 0.0002

LEU 408 GLU 409 -0.0669

GLU 409 PHE 410 0.0001

PHE 410 GLY 411 -0.0000

GLY 411 GLY 412 0.0181

GLY 412 ARG 413 -0.0001

ARG 413 LEU 414 0.0003

LEU 414 TYR 415 -0.0163

TYR 415 THR 416 -0.0000

THR 416 ALA 417 -0.0001

ALA 417 LYS 418 -0.0154

LYS 418 ASP 419 -0.0001

ASP 419 SER 420 -0.0002

SER 420 ARG 421 -0.1118

ARG 421 THR 422 -0.0001

THR 422 THR 423 -0.0004

THR 423 ALA 424 0.1352

ALA 424 GLU 425 -0.0000

GLU 425 THR 426 -0.0001

THR 426 PHE 427 0.0138

PHE 427 HIS 428 -0.0001

HIS 428 ALA 429 0.0001

ALA 429 MET 430 -0.0305

MET 430 TYR 431 -0.0002

TYR 431 PRO 432 0.0004

PRO 432 ARG 433 0.1330

ARG 433 VAL 434 0.0001

VAL 434 ASP 435 -0.0001

ASP 435 GLU 436 0.1140

GLU 436 TRP 437 0.0002

TRP 437 ILE 438 -0.0002

ILE 438 SER 439 0.0464

SER 439 VAL 440 0.0002

VAL 440 ARG 441 -0.0000

ARG 441 ARG 442 -0.0196

ARG 442 LYS 443 -0.0001

LYS 443 VAL 444 0.0001

VAL 444 ASP 445 -0.0234

ASP 445 PRO 446 -0.0000

PRO 446 LEU 447 -0.0003

LEU 447 ARG 448 0.0350

ARG 448 VAL 449 0.0002

VAL 449 PHE 450 0.0002

PHE 450 ALA 451 0.0228

ALA 451 SER 452 0.0001

SER 452 ASP 453 -0.0001

ASP 453 MET 454 -0.0689

MET 454 ALA 455 -0.0005

ALA 455 ARG 456 -0.0003

ARG 456 ARG 457 -0.0699

ARG 457 LEU 458 0.0001

LEU 458 GLU 459 0.0001

GLU 459 LEU 460 0.0588

LEU 460 LEU 461 0.0000

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.

*** 4fdo v/s 4p8l ***

CA strain for 20122614375822011

--- normal mode 8 ---

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

* 4fdo v/s 4p8l *