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

* 4P8L V/S 4FDO MP *

CA strain for 20122622073737765

--- 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 0.0004

THR 9 ALA 10 0.0430

ALA 10 THR 11 -0.0002

THR 11 ARG 12 -0.0000

ARG 12 LEU 13 0.0152

LEU 13 THR 14 0.0001

THR 14 GLY 15 -0.0003

GLY 15 TRP 16 0.0889

TRP 16 GLY 17 -0.0003

GLY 17 ARG 18 0.0001

ARG 18 THR 19 0.0619

THR 19 ALA 20 0.0004

ALA 20 PRO 21 0.0004

PRO 21 SER 22 0.0857

SER 22 VAL 23 0.0002

VAL 23 ALA 24 -0.0000

ALA 24 ASN 25 0.0237

ASN 25 VAL 26 -0.0000

VAL 26 LEU 27 -0.0001

LEU 27 ARG 28 -0.0028

ARG 28 THR 29 -0.0002

THR 29 PRO 30 -0.0000

PRO 30 ASP 31 0.0222

ASP 31 ALA 32 0.0001

ALA 32 GLU 33 -0.0000

GLU 33 MET 34 -0.0077

MET 34 ILE 35 -0.0001

ILE 35 VAL 36 -0.0000

VAL 36 LYS 37 0.0031

LYS 37 ALA 38 0.0002

ALA 38 VAL 39 -0.0001

VAL 39 ALA 40 0.0003

ALA 40 ARG 41 -0.0001

ARG 41 VAL 42 -0.0002

VAL 42 ALA 43 0.0155

ALA 43 GLU 44 -0.0003

GLU 44 SER 45 0.0003

SER 45 GLY 46 -0.0351

GLY 46 GLY 47 0.0001

GLY 47 GLY 48 -0.0004

GLY 48 ARG 49 0.0537

ARG 49 GLY 50 0.0001

GLY 50 ALA 51 0.0000

ALA 51 ILE 52 0.0385

ILE 52 ALA 53 0.0002

ALA 53 ARG 54 -0.0002

ARG 54 GLY 55 0.1578

GLY 55 LEU 56 0.0002

LEU 56 GLY 57 0.0002

GLY 57 ARG 58 0.0418

ARG 58 SER 59 0.0003

SER 59 TYR 60 -0.0001

TYR 60 GLY 61 0.0598

GLY 61 ASP 62 -0.0003

ASP 62 ASN 63 0.0003

ASN 63 ALA 64 -0.0330

ALA 64 GLN 65 -0.0001

GLN 65 ASN 66 -0.0002

ASN 66 GLY 67 0.0213

GLY 67 GLY 68 -0.0000

GLY 68 GLY 69 0.0003

GLY 69 LEU 70 0.0197

LEU 70 VAL 71 0.0000

VAL 71 ILE 72 0.0001

ILE 72 ASP 73 0.0559

ASP 73 MET 74 -0.0000

MET 74 THR 75 0.0002

THR 75 PRO 76 -0.0449

PRO 76 LEU 77 0.0000

LEU 77 ASN 78 0.0004

ASN 78 THR 79 -0.0234

THR 79 ILE 80 -0.0002

ILE 80 HIS 81 -0.0002

HIS 81 SER 82 -0.0817

SER 82 ILE 83 -0.0003

ILE 83 ASP 84 -0.0001

ASP 84 ALA 85 -0.0350

ALA 85 ASP 86 -0.0001

ASP 86 THR 87 -0.0000

THR 87 LYS 88 -0.0177

LYS 88 LEU 89 -0.0002

LEU 89 VAL 90 -0.0002

VAL 90 ASP 91 -0.0643

ASP 91 ILE 92 0.0000

ILE 92 ASP 93 -0.0000

ASP 93 ALA 94 -0.0449

ALA 94 GLY 95 -0.0000

GLY 95 VAL 96 0.0000

VAL 96 ASN 97 0.0624

ASN 97 LEU 98 -0.0001

LEU 98 ASP 99 0.0003

ASP 99 GLN 100 -0.0945

GLN 100 LEU 101 0.0002

LEU 101 MET 102 -0.0001

MET 102 LYS 103 -0.0288

LYS 103 ALA 104 0.0000

ALA 104 ALA 105 -0.0001

ALA 105 LEU 106 0.0713

LEU 106 PRO 107 0.0001

PRO 107 PHE 108 -0.0001

PHE 108 GLY 109 0.0384

GLY 109 LEU 110 0.0001

LEU 110 TRP 111 0.0003

TRP 111 VAL 112 0.0101

VAL 112 PRO 113 0.0004

PRO 113 VAL 114 0.0002

VAL 114 LEU 115 -0.0302

LEU 115 PRO 116 -0.0002

PRO 116 GLY 117 -0.0000

GLY 117 THR 118 0.0272

THR 118 ARG 119 -0.0003

ARG 119 GLN 120 -0.0002

GLN 120 VAL 121 0.0558

VAL 121 THR 122 -0.0002

THR 122 VAL 123 0.0001

VAL 123 GLY 124 0.0196

GLY 124 GLY 125 0.0003

GLY 125 ALA 126 0.0001

ALA 126 ILE 127 -0.0081

ILE 127 ALA 128 0.0002

ALA 128 CYS 129 0.0000

CYS 129 ASP 130 -0.0152

ASP 130 ILE 131 -0.0001

ILE 131 HIS 132 -0.0001

HIS 132 GLY 133 -0.0291

GLY 133 LYS 134 0.0002

LYS 134 ASN 135 -0.0004

ASN 135 HIS 136 -0.0126

HIS 136 HIS 137 0.0004

HIS 137 SER 138 -0.0000

SER 138 ALA 139 -0.0393

ALA 139 GLY 140 -0.0004

GLY 140 SER 141 0.0004

SER 141 PHE 142 0.0232

PHE 142 GLY 143 0.0003

GLY 143 ASN 144 -0.0001

ASN 144 HIS 145 0.1011

HIS 145 VAL 146 0.0004

VAL 146 ARG 147 0.0000

ARG 147 SER 148 -0.1434

SER 148 MET 149 -0.0001

MET 149 ASP 150 0.0000

ASP 150 LEU 151 -0.0209

LEU 151 LEU 152 -0.0002

LEU 152 THR 153 -0.0001

THR 153 ALA 154 -0.0127

ALA 154 ASP 155 -0.0001

ASP 155 GLY 156 0.0001

GLY 156 GLU 157 -0.0449

GLU 157 ILE 158 0.0003

ILE 158 ARG 159 -0.0003

ARG 159 HIS 160 -0.0586

HIS 160 LEU 161 -0.0004

LEU 161 THR 162 0.0001

THR 162 PRO 163 0.0146

PRO 163 THR 164 -0.0002

THR 164 GLY 165 0.0001

GLY 165 GLU 166 -0.0193

GLU 166 ASP 167 0.0001

ASP 167 ALA 168 0.0002

ALA 168 GLU 169 0.0347

GLU 169 LEU 170 -0.0001

LEU 170 PHE 171 -0.0002

PHE 171 TRP 172 0.0105

TRP 172 ALA 173 0.0001

ALA 173 THR 174 -0.0001

THR 174 VAL 175 -0.0395

VAL 175 GLY 176 -0.0003

GLY 176 GLY 177 -0.0004

GLY 177 ASN 178 -0.0063

ASN 178 GLY 179 0.0000

GLY 179 LEU 180 -0.0001

LEU 180 THR 181 0.0200

THR 181 GLY 182 0.0004

GLY 182 ILE 183 0.0000

ILE 183 ILE 184 0.0132

ILE 184 MET 185 -0.0001

MET 185 ARG 186 -0.0001

ARG 186 ALA 187 -0.0476

ALA 187 THR 188 0.0001

THR 188 ILE 189 0.0001

ILE 189 GLU 190 -0.0727

GLU 190 MET 191 -0.0001

MET 191 THR 192 -0.0001

THR 192 PRO 193 -0.1119

PRO 193 THR 194 0.0002

THR 194 SER 195 -0.0001

SER 195 THR 196 -0.0801

THR 196 ALA 197 0.0003

ALA 197 TYR 198 0.0003

TYR 198 PHE 199 -0.0099

PHE 199 ILE 200 0.0001

ILE 200 ALA 201 -0.0000

ALA 201 ASP 202 0.0215

ASP 202 GLY 203 0.0001

GLY 203 ASP 204 -0.0001

ASP 204 VAL 205 0.0226

VAL 205 THR 206 -0.0003

THR 206 ALA 207 0.0002

ALA 207 SER 208 -0.0758

SER 208 LEU 209 -0.0003

LEU 209 ASP 210 0.0001

ASP 210 GLU 211 -0.0006

GLU 211 THR 212 -0.0000

THR 212 ILE 213 -0.0000

ILE 213 ALA 214 -0.0016

ALA 214 LEU 215 0.0001

LEU 215 HIS 216 -0.0002

HIS 216 SER 217 -0.0035

SER 217 ASP 218 -0.0004

ASP 218 GLY 219 0.0004

GLY 219 SER 220 0.0101

SER 220 GLU 221 0.0000

GLU 221 ALA 222 0.0002

ALA 222 ARG 223 0.0256

ARG 223 TYR 224 0.0001

TYR 224 THR 225 -0.0000

THR 225 TYR 226 0.0336

TYR 226 SER 227 -0.0001

SER 227 SER 228 -0.0001

SER 228 ALA 229 -0.0336

ALA 229 TRP 230 -0.0000

TRP 230 PHE 231 0.0001

PHE 231 ASP 232 -0.0818

ASP 232 ALA 233 0.0000

ALA 233 ILE 234 0.0000

ILE 234 SER 235 0.0301

SER 235 ALA 236 0.0002

ALA 236 PRO 237 -0.0002

PRO 237 PRO 238 0.0157

PRO 238 LYS 239 -0.0006

LYS 239 LEU 240 0.0002

LEU 240 GLY 241 -0.0118

GLY 241 ARG 242 -0.0001

ARG 242 ALA 243 -0.0000

ALA 243 ALA 244 -0.0789

ALA 244 VAL 245 -0.0000

VAL 245 SER 246 -0.0000

SER 246 ARG 247 -0.0044

ARG 247 GLY 248 0.0004

GLY 248 ARG 249 -0.0001

ARG 249 LEU 250 0.1072

LEU 250 ALA 251 -0.0000

ALA 251 THR 252 -0.0002

THR 252 VAL 253 0.0238

VAL 253 GLU 254 -0.0000

GLU 254 GLN 255 0.0004

GLN 255 LEU 256 0.0030

LEU 256 PRO 257 0.0002

PRO 257 ALA 258 -0.0001

ALA 258 LYS 259 0.0350

LYS 259 LEU 260 0.0001

LEU 260 ARG 261 -0.0005

ARG 261 SER 262 0.0120

SER 262 GLU 263 -0.0000

GLU 263 PRO 264 -0.0001

PRO 264 LEU 265 0.0866

LEU 265 LYS 266 -0.0001

LYS 266 PHE 267 0.0001

PHE 267 ASP 268 -0.0534

ASP 268 ARG 298 0.1180

ARG 298 LYS 299 0.0002

LYS 299 SER 300 0.0002

SER 300 GLY 301 0.2714

GLY 301 THR 302 -0.0001

THR 302 TYR 303 0.0000

TYR 303 ARG 304 -0.1367

ARG 304 GLY 305 -0.0001

GLY 305 LYS 306 -0.0002

LYS 306 VAL 307 -0.0437

VAL 307 GLN 308 -0.0001

GLN 308 ASN 309 0.0001

ASN 309 LEU 310 0.0567

LEU 310 THR 311 -0.0001

THR 311 GLN 312 0.0001

GLN 312 PHE 313 -0.0833

PHE 313 TYR 314 -0.0001

TYR 314 HIS 315 0.0000

HIS 315 PRO 316 0.0038

PRO 316 LEU 317 -0.0002

LEU 317 ASP 318 0.0002

ASP 318 MET 319 -0.1378

MET 319 PHE 320 -0.0003

PHE 320 GLY 321 -0.0001

GLY 321 GLU 322 0.0739

GLU 322 TRP 323 -0.0000

TRP 323 ASN 324 -0.0001

ASN 324 ARG 325 0.0337

ARG 325 ALA 326 -0.0003

ALA 326 TYR 327 0.0004

TYR 327 GLY 328 0.1059

GLY 328 PRO 329 0.0005

PRO 329 ALA 330 0.0001

ALA 330 GLY 331 0.0951

GLY 331 PHE 332 0.0000

PHE 332 LEU 333 0.0002

LEU 333 GLN 334 -0.0417

GLN 334 TYR 335 0.0002

TYR 335 GLN 336 -0.0002

GLN 336 PHE 337 -0.0065

PHE 337 VAL 338 0.0001

VAL 338 ILE 339 0.0001

ILE 339 PRO 340 0.0114

PRO 340 THR 341 -0.0001

THR 341 GLU 342 -0.0001

GLU 342 ALA 343 0.0502

ALA 343 VAL 344 -0.0002

VAL 344 ASP 345 0.0005

ASP 345 GLU 346 -0.0228

GLU 346 PHE 347 0.0000

PHE 347 LYS 348 -0.0001

LYS 348 LYS 349 -0.0124

LYS 349 ILE 350 0.0004

ILE 350 ILE 351 0.0002

ILE 351 GLY 352 -0.0062

GLY 352 VAL 353 0.0004

VAL 353 ILE 354 -0.0003

ILE 354 GLN 355 0.0164

GLN 355 ALA 356 -0.0001

ALA 356 SER 357 -0.0002

SER 357 GLY 358 -0.0115

GLY 358 HIS 359 0.0002

HIS 359 TYR 360 -0.0004

TYR 360 SER 361 -0.0971

SER 361 PHE 362 0.0002

PHE 362 LEU 363 -0.0001

LEU 363 ASN 364 0.0458

ASN 364 VAL 365 0.0005

VAL 365 PHE 366 -0.0001

PHE 366 LYS 367 -0.0241

LYS 367 LEU 368 0.0004

LEU 368 PHE 369 -0.0000

PHE 369 GLY 370 -0.0237

GLY 370 PRO 371 0.0001

PRO 371 ARG 372 0.0000

ARG 372 ASN 373 -0.0376

ASN 373 GLN 374 -0.0002

GLN 374 ALA 375 0.0001

ALA 375 PRO 376 0.0289

PRO 376 LEU 377 0.0003

LEU 377 SER 378 -0.0002

SER 378 PHE 379 -0.0205

PHE 379 PRO 380 0.0001

PRO 380 ILE 381 -0.0001

ILE 381 PRO 382 -0.0603

PRO 382 GLY 383 0.0003

GLY 383 TRP 384 -0.0005

TRP 384 ASN 385 0.0192

ASN 385 ILE 386 0.0004

ILE 386 CYS 387 -0.0001

CYS 387 VAL 388 -0.0355

VAL 388 ASP 389 0.0002

ASP 389 PHE 390 -0.0004

PHE 390 PRO 391 -0.0124

PRO 391 ILE 392 -0.0003

ILE 392 LYS 393 0.0001

LYS 393 ASP 394 -0.0544

ASP 394 GLY 395 -0.0004

GLY 395 LEU 396 0.0004

LEU 396 GLY 397 0.0447

GLY 397 LYS 398 -0.0001

LYS 398 PHE 399 0.0001

PHE 399 VAL 400 0.0185

VAL 400 SER 401 0.0003

SER 401 GLU 402 -0.0003

GLU 402 LEU 403 0.0167

LEU 403 ASP 404 -0.0000

ASP 404 ARG 405 -0.0002

ARG 405 ARG 406 -0.0135

ARG 406 VAL 407 0.0004

VAL 407 LEU 408 0.0001

LEU 408 GLU 409 -0.0542

GLU 409 PHE 410 0.0001

PHE 410 GLY 411 -0.0002

GLY 411 GLY 412 0.0269

GLY 412 ARG 413 -0.0002

ARG 413 LEU 414 0.0001

LEU 414 TYR 415 -0.0101

TYR 415 THR 416 0.0003

THR 416 ALA 417 0.0003

ALA 417 LYS 418 -0.0082

LYS 418 ASP 419 0.0004

ASP 419 SER 420 -0.0001

SER 420 ARG 421 -0.0741

ARG 421 THR 422 0.0001

THR 422 THR 423 -0.0002

THR 423 ALA 424 0.1295

ALA 424 GLU 425 0.0003

GLU 425 THR 426 0.0001

THR 426 PHE 427 0.0322

PHE 427 HIS 428 0.0000

HIS 428 ALA 429 0.0001

ALA 429 MET 430 -0.0213

MET 430 TYR 431 0.0001

TYR 431 PRO 432 0.0000

PRO 432 ARG 433 0.1058

ARG 433 VAL 434 0.0002

VAL 434 ASP 435 -0.0001

ASP 435 GLU 436 0.1094

GLU 436 TRP 437 -0.0001

TRP 437 ILE 438 0.0002

ILE 438 SER 439 0.0423

SER 439 VAL 440 0.0002

VAL 440 ARG 441 -0.0002

ARG 441 ARG 442 -0.0137

ARG 442 LYS 443 -0.0001

LYS 443 VAL 444 0.0000

VAL 444 ASP 445 -0.0247

ASP 445 PRO 446 0.0001

PRO 446 LEU 447 0.0001

LEU 447 ARG 448 0.0385

ARG 448 VAL 449 0.0001

VAL 449 PHE 450 -0.0003

PHE 450 ALA 451 0.0330

ALA 451 SER 452 0.0003

SER 452 ASP 453 0.0000

ASP 453 MET 454 -0.0476

MET 454 ALA 455 -0.0001

ALA 455 ARG 456 -0.0003

ARG 456 ARG 457 -0.0226

ARG 457 LEU 458 -0.0001

LEU 458 GLU 459 0.0004

GLU 459 LEU 460 0.0516

LEU 460 LEU 461 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: October 18th, 2018.

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

*** 4P8L V/S 4FDO MP ***

CA strain for 20122622073737765

--- normal mode 8 ---

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

* 4P8L V/S 4FDO MP *