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

* 4P8L V/S 4FDO MP *

CA strain for 20122622073737765

--- normal mode 11 ---

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 -0.0001

THR 8 THR 9 0.0002

THR 9 ALA 10 -0.0495

ALA 10 THR 11 0.0001

THR 11 ARG 12 -0.0003

ARG 12 LEU 13 0.0104

LEU 13 THR 14 -0.0000

THR 14 GLY 15 0.0002

GLY 15 TRP 16 -0.0186

TRP 16 GLY 17 0.0002

GLY 17 ARG 18 0.0003

ARG 18 THR 19 0.0069

THR 19 ALA 20 0.0002

ALA 20 PRO 21 0.0004

PRO 21 SER 22 -0.1622

SER 22 VAL 23 -0.0003

VAL 23 ALA 24 -0.0001

ALA 24 ASN 25 -0.0650

ASN 25 VAL 26 -0.0002

VAL 26 LEU 27 0.0002

LEU 27 ARG 28 0.0246

ARG 28 THR 29 -0.0005

THR 29 PRO 30 0.0004

PRO 30 ASP 31 0.0343

ASP 31 ALA 32 -0.0000

ALA 32 GLU 33 0.0001

GLU 33 MET 34 -0.0026

MET 34 ILE 35 -0.0000

ILE 35 VAL 36 0.0000

VAL 36 LYS 37 0.0828

LYS 37 ALA 38 -0.0003

ALA 38 VAL 39 -0.0001

VAL 39 ALA 40 0.0249

ALA 40 ARG 41 -0.0003

ARG 41 VAL 42 -0.0000

VAL 42 ALA 43 -0.0307

ALA 43 GLU 44 -0.0002

GLU 44 SER 45 0.0003

SER 45 GLY 46 0.0177

GLY 46 GLY 47 -0.0000

GLY 47 GLY 48 0.0002

GLY 48 ARG 49 -0.1280

ARG 49 GLY 50 -0.0003

GLY 50 ALA 51 0.0002

ALA 51 ILE 52 0.0121

ILE 52 ALA 53 -0.0000

ALA 53 ARG 54 -0.0000

ARG 54 GLY 55 0.0611

GLY 55 LEU 56 0.0000

LEU 56 GLY 57 0.0001

GLY 57 ARG 58 0.0343

ARG 58 SER 59 0.0003

SER 59 TYR 60 0.0001

TYR 60 GLY 61 -0.0590

GLY 61 ASP 62 -0.0001

ASP 62 ASN 63 0.0001

ASN 63 ALA 64 -0.0022

ALA 64 GLN 65 -0.0001

GLN 65 ASN 66 0.0005

ASN 66 GLY 67 0.0004

GLY 67 GLY 68 -0.0002

GLY 68 GLY 69 -0.0000

GLY 69 LEU 70 0.0069

LEU 70 VAL 71 0.0001

VAL 71 ILE 72 -0.0001

ILE 72 ASP 73 0.0404

ASP 73 MET 74 -0.0002

MET 74 THR 75 0.0004

THR 75 PRO 76 0.0299

PRO 76 LEU 77 -0.0002

LEU 77 ASN 78 0.0004

ASN 78 THR 79 0.0275

THR 79 ILE 80 0.0002

ILE 80 HIS 81 0.0000

HIS 81 SER 82 0.1566

SER 82 ILE 83 0.0003

ILE 83 ASP 84 -0.0001

ASP 84 ALA 85 0.0679

ALA 85 ASP 86 0.0001

ASP 86 THR 87 -0.0001

THR 87 LYS 88 0.0220

LYS 88 LEU 89 0.0001

LEU 89 VAL 90 0.0001

VAL 90 ASP 91 0.1547

ASP 91 ILE 92 0.0003

ILE 92 ASP 93 -0.0002

ASP 93 ALA 94 0.0089

ALA 94 GLY 95 0.0002

GLY 95 VAL 96 -0.0001

VAL 96 ASN 97 0.0778

ASN 97 LEU 98 0.0001

LEU 98 ASP 99 -0.0002

ASP 99 GLN 100 -0.0082

GLN 100 LEU 101 0.0001

LEU 101 MET 102 0.0003

MET 102 LYS 103 -0.0105

LYS 103 ALA 104 -0.0004

ALA 104 ALA 105 0.0000

ALA 105 LEU 106 0.1029

LEU 106 PRO 107 -0.0003

PRO 107 PHE 108 -0.0000

PHE 108 GLY 109 -0.0280

GLY 109 LEU 110 -0.0000

LEU 110 TRP 111 -0.0003

TRP 111 VAL 112 -0.0386

VAL 112 PRO 113 -0.0001

PRO 113 VAL 114 0.0003

VAL 114 LEU 115 0.0263

LEU 115 PRO 116 -0.0001

PRO 116 GLY 117 -0.0002

GLY 117 THR 118 0.0272

THR 118 ARG 119 -0.0002

ARG 119 GLN 120 -0.0001

GLN 120 VAL 121 0.0248

VAL 121 THR 122 0.0002

THR 122 VAL 123 0.0000

VAL 123 GLY 124 0.0089

GLY 124 GLY 125 -0.0001

GLY 125 ALA 126 0.0005

ALA 126 ILE 127 0.0340

ILE 127 ALA 128 0.0002

ALA 128 CYS 129 -0.0000

CYS 129 ASP 130 0.0109

ASP 130 ILE 131 0.0000

ILE 131 HIS 132 0.0000

HIS 132 GLY 133 0.0733

GLY 133 LYS 134 0.0005

LYS 134 ASN 135 0.0002

ASN 135 HIS 136 -0.0701

HIS 136 HIS 137 -0.0003

HIS 137 SER 138 0.0002

SER 138 ALA 139 0.1083

ALA 139 GLY 140 -0.0003

GLY 140 SER 141 0.0000

SER 141 PHE 142 0.0274

PHE 142 GLY 143 0.0001

GLY 143 ASN 144 -0.0001

ASN 144 HIS 145 -0.1413

HIS 145 VAL 146 -0.0004

VAL 146 ARG 147 -0.0002

ARG 147 SER 148 0.2127

SER 148 MET 149 0.0002

MET 149 ASP 150 -0.0003

ASP 150 LEU 151 0.1130

LEU 151 LEU 152 0.0000

LEU 152 THR 153 0.0002

THR 153 ALA 154 0.1219

ALA 154 ASP 155 0.0000

ASP 155 GLY 156 0.0002

GLY 156 GLU 157 0.1052

GLU 157 ILE 158 -0.0001

ILE 158 ARG 159 -0.0004

ARG 159 HIS 160 0.1056

HIS 160 LEU 161 0.0002

LEU 161 THR 162 -0.0002

THR 162 PRO 163 -0.0092

PRO 163 THR 164 -0.0003

THR 164 GLY 165 0.0003

GLY 165 GLU 166 0.0210

GLU 166 ASP 167 -0.0001

ASP 167 ALA 168 0.0002

ALA 168 GLU 169 -0.0191

GLU 169 LEU 170 -0.0003

LEU 170 PHE 171 0.0000

PHE 171 TRP 172 -0.0310

TRP 172 ALA 173 0.0003

ALA 173 THR 174 0.0002

THR 174 VAL 175 0.0453

VAL 175 GLY 176 0.0001

GLY 176 GLY 177 -0.0003

GLY 177 ASN 178 -0.0056

ASN 178 GLY 179 0.0003

GLY 179 LEU 180 0.0001

LEU 180 THR 181 -0.0419

THR 181 GLY 182 -0.0000

GLY 182 ILE 183 -0.0000

ILE 183 ILE 184 0.0789

ILE 184 MET 185 -0.0000

MET 185 ARG 186 0.0001

ARG 186 ALA 187 0.1346

ALA 187 THR 188 -0.0001

THR 188 ILE 189 -0.0002

ILE 189 GLU 190 0.0941

GLU 190 MET 191 0.0002

MET 191 THR 192 0.0003

THR 192 PRO 193 0.0565

PRO 193 THR 194 -0.0003

THR 194 SER 195 -0.0001

SER 195 THR 196 0.0557

THR 196 ALA 197 0.0005

ALA 197 TYR 198 -0.0001

TYR 198 PHE 199 -0.0085

PHE 199 ILE 200 0.0001

ILE 200 ALA 201 -0.0000

ALA 201 ASP 202 0.0926

ASP 202 GLY 203 0.0001

GLY 203 ASP 204 0.0001

ASP 204 VAL 205 0.1470

VAL 205 THR 206 0.0003

THR 206 ALA 207 0.0001

ALA 207 SER 208 -0.0251

SER 208 LEU 209 -0.0002

LEU 209 ASP 210 -0.0002

ASP 210 GLU 211 -0.0272

GLU 211 THR 212 -0.0001

THR 212 ILE 213 -0.0001

ILE 213 ALA 214 -0.0374

ALA 214 LEU 215 -0.0000

LEU 215 HIS 216 -0.0003

HIS 216 SER 217 0.0022

SER 217 ASP 218 -0.0001

ASP 218 GLY 219 -0.0004

GLY 219 SER 220 -0.0406

SER 220 GLU 221 -0.0000

GLU 221 ALA 222 -0.0004

ALA 222 ARG 223 -0.0341

ARG 223 TYR 224 -0.0001

TYR 224 THR 225 0.0003

THR 225 TYR 226 0.0161

TYR 226 SER 227 0.0003

SER 227 SER 228 -0.0001

SER 228 ALA 229 0.0798

ALA 229 TRP 230 -0.0002

TRP 230 PHE 231 -0.0003

PHE 231 ASP 232 0.0882

ASP 232 ALA 233 0.0000

ALA 233 ILE 234 0.0001

ILE 234 SER 235 0.0004

SER 235 ALA 236 0.0003

ALA 236 PRO 237 -0.0002

PRO 237 PRO 238 0.0086

PRO 238 LYS 239 -0.0000

LYS 239 LEU 240 -0.0000

LEU 240 GLY 241 0.0422

GLY 241 ARG 242 0.0002

ARG 242 ALA 243 0.0001

ALA 243 ALA 244 0.1258

ALA 244 VAL 245 -0.0001

VAL 245 SER 246 -0.0001

SER 246 ARG 247 0.0995

ARG 247 GLY 248 0.0001

GLY 248 ARG 249 -0.0002

ARG 249 LEU 250 -0.0647

LEU 250 ALA 251 0.0001

ALA 251 THR 252 0.0001

THR 252 VAL 253 -0.0656

VAL 253 GLU 254 -0.0003

GLU 254 GLN 255 -0.0003

GLN 255 LEU 256 0.0023

LEU 256 PRO 257 0.0001

PRO 257 ALA 258 0.0000

ALA 258 LYS 259 0.0034

LYS 259 LEU 260 0.0004

LEU 260 ARG 261 -0.0002

ARG 261 SER 262 -0.0258

SER 262 GLU 263 -0.0001

GLU 263 PRO 264 0.0000

PRO 264 LEU 265 0.0778

LEU 265 LYS 266 0.0000

LYS 266 PHE 267 0.0002

PHE 267 ASP 268 0.0498

ASP 268 ARG 298 0.8793

ARG 298 LYS 299 -0.0001

LYS 299 SER 300 -0.0003

SER 300 GLY 301 0.3910

GLY 301 THR 302 -0.0001

THR 302 TYR 303 0.0002

TYR 303 ARG 304 -0.3205

ARG 304 GLY 305 0.0000

GLY 305 LYS 306 -0.0000

LYS 306 VAL 307 0.0889

VAL 307 GLN 308 -0.0000

GLN 308 ASN 309 0.0001

ASN 309 LEU 310 -0.0258

LEU 310 THR 311 -0.0002

THR 311 GLN 312 -0.0002

GLN 312 PHE 313 -0.0244

PHE 313 TYR 314 -0.0002

TYR 314 HIS 315 0.0001

HIS 315 PRO 316 -0.0694

PRO 316 LEU 317 0.0004

LEU 317 ASP 318 0.0000

ASP 318 MET 319 0.0984

MET 319 PHE 320 0.0000

PHE 320 GLY 321 -0.0003

GLY 321 GLU 322 -0.0643

GLU 322 TRP 323 -0.0001

TRP 323 ASN 324 -0.0003

ASN 324 ARG 325 0.0004

ARG 325 ALA 326 0.0002

ALA 326 TYR 327 -0.0000

TYR 327 GLY 328 -0.1069

GLY 328 PRO 329 -0.0002

PRO 329 ALA 330 0.0003

ALA 330 GLY 331 -0.1682

GLY 331 PHE 332 -0.0003

PHE 332 LEU 333 0.0003

LEU 333 GLN 334 -0.0015

GLN 334 TYR 335 0.0002

TYR 335 GLN 336 -0.0001

GLN 336 PHE 337 0.0066

PHE 337 VAL 338 -0.0002

VAL 338 ILE 339 0.0000

ILE 339 PRO 340 0.0184

PRO 340 THR 341 0.0003

THR 341 GLU 342 -0.0003

GLU 342 ALA 343 0.0009

ALA 343 VAL 344 0.0004

VAL 344 ASP 345 -0.0004

ASP 345 GLU 346 -0.0061

GLU 346 PHE 347 0.0000

PHE 347 LYS 348 0.0001

LYS 348 LYS 349 -0.0428

LYS 349 ILE 350 -0.0000

ILE 350 ILE 351 0.0001

ILE 351 GLY 352 0.0099

GLY 352 VAL 353 0.0000

VAL 353 ILE 354 -0.0002

ILE 354 GLN 355 -0.0587

GLN 355 ALA 356 0.0003

ALA 356 SER 357 -0.0001

SER 357 GLY 358 0.0021

GLY 358 HIS 359 0.0002

HIS 359 TYR 360 -0.0005

TYR 360 SER 361 0.0851

SER 361 PHE 362 0.0003

PHE 362 LEU 363 -0.0001

LEU 363 ASN 364 -0.0308

ASN 364 VAL 365 -0.0002

VAL 365 PHE 366 -0.0003

PHE 366 LYS 367 0.0360

LYS 367 LEU 368 0.0001

LEU 368 PHE 369 -0.0000

PHE 369 GLY 370 0.0622

GLY 370 PRO 371 0.0004

PRO 371 ARG 372 -0.0002

ARG 372 ASN 373 0.1313

ASN 373 GLN 374 0.0000

GLN 374 ALA 375 0.0001

ALA 375 PRO 376 -0.0277

PRO 376 LEU 377 -0.0002

LEU 377 SER 378 0.0002

SER 378 PHE 379 0.0302

PHE 379 PRO 380 -0.0002

PRO 380 ILE 381 -0.0002

ILE 381 PRO 382 0.0456

PRO 382 GLY 383 0.0001

GLY 383 TRP 384 -0.0001

TRP 384 ASN 385 -0.0093

ASN 385 ILE 386 0.0003

ILE 386 CYS 387 -0.0004

CYS 387 VAL 388 0.0096

VAL 388 ASP 389 0.0002

ASP 389 PHE 390 -0.0000

PHE 390 PRO 391 0.0337

PRO 391 ILE 392 -0.0001

ILE 392 LYS 393 -0.0000

LYS 393 ASP 394 0.0467

ASP 394 GLY 395 -0.0003

GLY 395 LEU 396 -0.0004

LEU 396 GLY 397 -0.0785

GLY 397 LYS 398 0.0001

LYS 398 PHE 399 -0.0000

PHE 399 VAL 400 -0.0856

VAL 400 SER 401 0.0000

SER 401 GLU 402 -0.0000

GLU 402 LEU 403 -0.0049

LEU 403 ASP 404 0.0005

ASP 404 ARG 405 -0.0002

ARG 405 ARG 406 -0.0303

ARG 406 VAL 407 0.0002

VAL 407 LEU 408 0.0001

LEU 408 GLU 409 -0.0268

GLU 409 PHE 410 -0.0000

PHE 410 GLY 411 -0.0000

GLY 411 GLY 412 0.0297

GLY 412 ARG 413 0.0003

ARG 413 LEU 414 0.0001

LEU 414 TYR 415 -0.0305

TYR 415 THR 416 -0.0001

THR 416 ALA 417 -0.0001

ALA 417 LYS 418 -0.0251

LYS 418 ASP 419 -0.0001

ASP 419 SER 420 -0.0001

SER 420 ARG 421 -0.0095

ARG 421 THR 422 -0.0002

THR 422 THR 423 -0.0001

THR 423 ALA 424 -0.1022

ALA 424 GLU 425 0.0001

GLU 425 THR 426 -0.0001

THR 426 PHE 427 -0.0695

PHE 427 HIS 428 0.0001

HIS 428 ALA 429 -0.0004

ALA 429 MET 430 0.0088

MET 430 TYR 431 0.0002

TYR 431 PRO 432 -0.0001

PRO 432 ARG 433 -0.1256

ARG 433 VAL 434 -0.0001

VAL 434 ASP 435 0.0004

ASP 435 GLU 436 -0.0973

GLU 436 TRP 437 0.0000

TRP 437 ILE 438 0.0001

ILE 438 SER 439 -0.0474

SER 439 VAL 440 -0.0001

VAL 440 ARG 441 0.0002

ARG 441 ARG 442 0.0277

ARG 442 LYS 443 -0.0002

LYS 443 VAL 444 0.0001

VAL 444 ASP 445 0.0568

ASP 445 PRO 446 -0.0001

PRO 446 LEU 447 0.0001

LEU 447 ARG 448 -0.0675

ARG 448 VAL 449 -0.0003

VAL 449 PHE 450 -0.0001

PHE 450 ALA 451 -0.1003

ALA 451 SER 452 -0.0004

SER 452 ASP 453 -0.0001

ASP 453 MET 454 0.0507

MET 454 ALA 455 -0.0002

ALA 455 ARG 456 0.0003

ARG 456 ARG 457 -0.2263

ARG 457 LEU 458 -0.0002

LEU 458 GLU 459 0.0001

GLU 459 LEU 460 -0.0827

LEU 460 LEU 461 0.0004

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 11 ---

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

* 4P8L V/S 4FDO MP *