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

* 4P8L V/S 4FDO MP *

CA strain for 20122622073737765

--- 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
THR 7 THR 8 0.0000

THR 8 THR 9 -0.0000

THR 9 ALA 10 -0.0071

ALA 10 THR 11 0.0002

THR 11 ARG 12 -0.0000

ARG 12 LEU 13 0.0243

LEU 13 THR 14 -0.0001

THR 14 GLY 15 -0.0001

GLY 15 TRP 16 -0.0016

TRP 16 GLY 17 0.0000

GLY 17 ARG 18 0.0001

ARG 18 THR 19 0.1288

THR 19 ALA 20 0.0000

ALA 20 PRO 21 -0.0002

PRO 21 SER 22 -0.0901

SER 22 VAL 23 0.0002

VAL 23 ALA 24 0.0003

ALA 24 ASN 25 -0.0166

ASN 25 VAL 26 0.0001

VAL 26 LEU 27 -0.0002

LEU 27 ARG 28 0.0426

ARG 28 THR 29 0.0001

THR 29 PRO 30 0.0003

PRO 30 ASP 31 0.0003

ASP 31 ALA 32 0.0002

ALA 32 GLU 33 0.0000

GLU 33 MET 34 -0.0240

MET 34 ILE 35 0.0001

ILE 35 VAL 36 -0.0001

VAL 36 LYS 37 0.0023

LYS 37 ALA 38 0.0004

ALA 38 VAL 39 0.0002

VAL 39 ALA 40 0.0001

ALA 40 ARG 41 0.0000

ARG 41 VAL 42 0.0000

VAL 42 ALA 43 -0.0069

ALA 43 GLU 44 0.0002

GLU 44 SER 45 -0.0001

SER 45 GLY 46 0.0153

GLY 46 GLY 47 0.0001

GLY 47 GLY 48 0.0002

GLY 48 ARG 49 -0.0192

ARG 49 GLY 50 -0.0000

GLY 50 ALA 51 0.0003

ALA 51 ILE 52 0.0100

ILE 52 ALA 53 0.0000

ALA 53 ARG 54 -0.0001

ARG 54 GLY 55 0.1227

GLY 55 LEU 56 0.0004

LEU 56 GLY 57 -0.0001

GLY 57 ARG 58 -0.0407

ARG 58 SER 59 0.0000

SER 59 TYR 60 -0.0001

TYR 60 GLY 61 0.0477

GLY 61 ASP 62 -0.0003

ASP 62 ASN 63 0.0001

ASN 63 ALA 64 -0.0022

ALA 64 GLN 65 -0.0003

GLN 65 ASN 66 -0.0003

ASN 66 GLY 67 0.0118

GLY 67 GLY 68 -0.0004

GLY 68 GLY 69 -0.0000

GLY 69 LEU 70 0.0282

LEU 70 VAL 71 -0.0002

VAL 71 ILE 72 -0.0000

ILE 72 ASP 73 0.0643

ASP 73 MET 74 -0.0003

MET 74 THR 75 0.0002

THR 75 PRO 76 -0.0550

PRO 76 LEU 77 0.0003

LEU 77 ASN 78 0.0000

ASN 78 THR 79 0.0890

THR 79 ILE 80 -0.0003

ILE 80 HIS 81 -0.0000

HIS 81 SER 82 0.0804

SER 82 ILE 83 0.0002

ILE 83 ASP 84 -0.0003

ASP 84 ALA 85 0.0553

ALA 85 ASP 86 -0.0001

ASP 86 THR 87 0.0001

THR 87 LYS 88 0.0455

LYS 88 LEU 89 -0.0003

LEU 89 VAL 90 0.0001

VAL 90 ASP 91 0.0182

ASP 91 ILE 92 0.0002

ILE 92 ASP 93 0.0000

ASP 93 ALA 94 -0.0110

ALA 94 GLY 95 -0.0000

GLY 95 VAL 96 -0.0002

VAL 96 ASN 97 -0.0385

ASN 97 LEU 98 -0.0001

LEU 98 ASP 99 -0.0001

ASP 99 GLN 100 -0.0930

GLN 100 LEU 101 0.0001

LEU 101 MET 102 -0.0000

MET 102 LYS 103 -0.0424

LYS 103 ALA 104 0.0001

ALA 104 ALA 105 -0.0000

ALA 105 LEU 106 0.0174

LEU 106 PRO 107 -0.0000

PRO 107 PHE 108 0.0001

PHE 108 GLY 109 0.0849

GLY 109 LEU 110 -0.0003

LEU 110 TRP 111 0.0000

TRP 111 VAL 112 -0.0276

VAL 112 PRO 113 0.0003

PRO 113 VAL 114 -0.0002

VAL 114 LEU 115 0.0012

LEU 115 PRO 116 0.0004

PRO 116 GLY 117 -0.0001

GLY 117 THR 118 -0.0703

THR 118 ARG 119 -0.0000

ARG 119 GLN 120 -0.0005

GLN 120 VAL 121 0.0031

VAL 121 THR 122 0.0003

THR 122 VAL 123 0.0003

VAL 123 GLY 124 0.0104

GLY 124 GLY 125 -0.0003

GLY 125 ALA 126 -0.0002

ALA 126 ILE 127 0.0010

ILE 127 ALA 128 -0.0003

ALA 128 CYS 129 -0.0001

CYS 129 ASP 130 0.0027

ASP 130 ILE 131 0.0002

ILE 131 HIS 132 -0.0001

HIS 132 GLY 133 -0.0070

GLY 133 LYS 134 -0.0002

LYS 134 ASN 135 -0.0002

ASN 135 HIS 136 -0.0644

HIS 136 HIS 137 -0.0002

HIS 137 SER 138 0.0002

SER 138 ALA 139 0.1763

ALA 139 GLY 140 0.0000

GLY 140 SER 141 0.0001

SER 141 PHE 142 0.0640

PHE 142 GLY 143 0.0000

GLY 143 ASN 144 0.0002

ASN 144 HIS 145 -0.0358

HIS 145 VAL 146 0.0000

VAL 146 ARG 147 0.0001

ARG 147 SER 148 -0.0197

SER 148 MET 149 -0.0000

MET 149 ASP 150 -0.0000

ASP 150 LEU 151 -0.0513

LEU 151 LEU 152 -0.0001

LEU 152 THR 153 -0.0003

THR 153 ALA 154 -0.0249

ALA 154 ASP 155 0.0001

ASP 155 GLY 156 0.0001

GLY 156 GLU 157 -0.0113

GLU 157 ILE 158 -0.0001

ILE 158 ARG 159 -0.0000

ARG 159 HIS 160 -0.0349

HIS 160 LEU 161 -0.0001

LEU 161 THR 162 0.0003

THR 162 PRO 163 0.0573

PRO 163 THR 164 0.0000

THR 164 GLY 165 0.0002

GLY 165 GLU 166 -0.0229

GLU 166 ASP 167 0.0002

ASP 167 ALA 168 0.0001

ALA 168 GLU 169 -0.0255

GLU 169 LEU 170 -0.0002

LEU 170 PHE 171 -0.0004

PHE 171 TRP 172 0.0372

TRP 172 ALA 173 0.0003

ALA 173 THR 174 0.0002

THR 174 VAL 175 0.0091

VAL 175 GLY 176 0.0003

GLY 176 GLY 177 -0.0003

GLY 177 ASN 178 -0.0137

ASN 178 GLY 179 0.0001

GLY 179 LEU 180 -0.0004

LEU 180 THR 181 -0.0339

THR 181 GLY 182 -0.0001

GLY 182 ILE 183 0.0002

ILE 183 ILE 184 -0.0111

ILE 184 MET 185 0.0002

MET 185 ARG 186 -0.0004

ARG 186 ALA 187 0.0006

ALA 187 THR 188 0.0000

THR 188 ILE 189 -0.0003

ILE 189 GLU 190 -0.0332

GLU 190 MET 191 -0.0002

MET 191 THR 192 -0.0001

THR 192 PRO 193 -0.1950

PRO 193 THR 194 0.0000

THR 194 SER 195 0.0001

SER 195 THR 196 -0.0458

THR 196 ALA 197 -0.0000

ALA 197 TYR 198 -0.0003

TYR 198 PHE 199 -0.0694

PHE 199 ILE 200 -0.0005

ILE 200 ALA 201 -0.0001

ALA 201 ASP 202 -0.0049

ASP 202 GLY 203 0.0001

GLY 203 ASP 204 -0.0003

ASP 204 VAL 205 0.0242

VAL 205 THR 206 -0.0005

THR 206 ALA 207 0.0000

ALA 207 SER 208 0.0753

SER 208 LEU 209 0.0000

LEU 209 ASP 210 -0.0003

ASP 210 GLU 211 -0.0462

GLU 211 THR 212 -0.0001

THR 212 ILE 213 -0.0001

ILE 213 ALA 214 -0.0555

ALA 214 LEU 215 -0.0002

LEU 215 HIS 216 0.0000

HIS 216 SER 217 0.0224

SER 217 ASP 218 0.0004

ASP 218 GLY 219 0.0003

GLY 219 SER 220 -0.0493

SER 220 GLU 221 -0.0003

GLU 221 ALA 222 -0.0002

ALA 222 ARG 223 -0.0192

ARG 223 TYR 224 0.0000

TYR 224 THR 225 0.0005

THR 225 TYR 226 0.0401

TYR 226 SER 227 0.0001

SER 227 SER 228 -0.0001

SER 228 ALA 229 0.0449

ALA 229 TRP 230 0.0001

TRP 230 PHE 231 0.0002

PHE 231 ASP 232 0.0702

ASP 232 ALA 233 -0.0001

ALA 233 ILE 234 0.0000

ILE 234 SER 235 -0.0913

SER 235 ALA 236 -0.0003

ALA 236 PRO 237 0.0000

PRO 237 PRO 238 -0.0283

PRO 238 LYS 239 -0.0001

LYS 239 LEU 240 -0.0002

LEU 240 GLY 241 0.0000

GLY 241 ARG 242 -0.0001

ARG 242 ALA 243 0.0003

ALA 243 ALA 244 0.0816

ALA 244 VAL 245 0.0002

VAL 245 SER 246 -0.0004

SER 246 ARG 247 0.0638

ARG 247 GLY 248 0.0000

GLY 248 ARG 249 -0.0003

ARG 249 LEU 250 -0.0266

LEU 250 ALA 251 -0.0000

ALA 251 THR 252 0.0000

THR 252 VAL 253 -0.1157

VAL 253 GLU 254 -0.0001

GLU 254 GLN 255 -0.0003

GLN 255 LEU 256 -0.0727

LEU 256 PRO 257 -0.0002

PRO 257 ALA 258 -0.0002

ALA 258 LYS 259 0.0462

LYS 259 LEU 260 -0.0000

LEU 260 ARG 261 -0.0001

ARG 261 SER 262 0.0426

SER 262 GLU 263 0.0000

GLU 263 PRO 264 0.0002

PRO 264 LEU 265 0.0423

LEU 265 LYS 266 0.0000

LYS 266 PHE 267 0.0004

PHE 267 ASP 268 0.0115

ASP 268 ARG 298 -0.1840

ARG 298 LYS 299 0.0002

LYS 299 SER 300 -0.0002

SER 300 GLY 301 -0.2250

GLY 301 THR 302 0.0001

THR 302 TYR 303 0.0003

TYR 303 ARG 304 0.1467

ARG 304 GLY 305 -0.0001

GLY 305 LYS 306 -0.0001

LYS 306 VAL 307 -0.0165

VAL 307 GLN 308 -0.0003

GLN 308 ASN 309 -0.0000

ASN 309 LEU 310 0.0969

LEU 310 THR 311 0.0002

THR 311 GLN 312 -0.0000

GLN 312 PHE 313 -0.0854

PHE 313 TYR 314 0.0001

TYR 314 HIS 315 0.0004

HIS 315 PRO 316 0.2881

PRO 316 LEU 317 0.0001

LEU 317 ASP 318 0.0002

ASP 318 MET 319 -0.0010

MET 319 PHE 320 -0.0001

PHE 320 GLY 321 -0.0001

GLY 321 GLU 322 0.0574

GLU 322 TRP 323 0.0001

TRP 323 ASN 324 -0.0002

ASN 324 ARG 325 -0.0681

ARG 325 ALA 326 0.0004

ALA 326 TYR 327 -0.0001

TYR 327 GLY 328 -0.0042

GLY 328 PRO 329 -0.0002

PRO 329 ALA 330 0.0005

ALA 330 GLY 331 -0.1426

GLY 331 PHE 332 0.0004

PHE 332 LEU 333 -0.0002

LEU 333 GLN 334 0.0079

GLN 334 TYR 335 -0.0001

TYR 335 GLN 336 0.0001

GLN 336 PHE 337 -0.0210

PHE 337 VAL 338 0.0003

VAL 338 ILE 339 0.0002

ILE 339 PRO 340 -0.0028

PRO 340 THR 341 -0.0001

THR 341 GLU 342 0.0004

GLU 342 ALA 343 -0.0294

ALA 343 VAL 344 -0.0000

VAL 344 ASP 345 0.0003

ASP 345 GLU 346 -0.0224

GLU 346 PHE 347 -0.0001

PHE 347 LYS 348 -0.0002

LYS 348 LYS 349 -0.0360

LYS 349 ILE 350 -0.0002

ILE 350 ILE 351 0.0003

ILE 351 GLY 352 0.0369

GLY 352 VAL 353 0.0004

VAL 353 ILE 354 0.0002

ILE 354 GLN 355 0.0056

GLN 355 ALA 356 0.0000

ALA 356 SER 357 0.0001

SER 357 GLY 358 0.0147

GLY 358 HIS 359 -0.0000

HIS 359 TYR 360 0.0002

TYR 360 SER 361 0.1360

SER 361 PHE 362 -0.0000

PHE 362 LEU 363 0.0001

LEU 363 ASN 364 -0.0729

ASN 364 VAL 365 0.0003

VAL 365 PHE 366 0.0001

PHE 366 LYS 367 0.0297

LYS 367 LEU 368 -0.0000

LEU 368 PHE 369 0.0002

PHE 369 GLY 370 0.0515

GLY 370 PRO 371 -0.0002

PRO 371 ARG 372 0.0004

ARG 372 ASN 373 0.2219

ASN 373 GLN 374 0.0002

GLN 374 ALA 375 0.0002

ALA 375 PRO 376 -0.0350

PRO 376 LEU 377 -0.0002

LEU 377 SER 378 0.0005

SER 378 PHE 379 0.0624

PHE 379 PRO 380 -0.0001

PRO 380 ILE 381 -0.0004

ILE 381 PRO 382 0.0652

PRO 382 GLY 383 0.0000

GLY 383 TRP 384 0.0002

TRP 384 ASN 385 -0.0154

ASN 385 ILE 386 0.0002

ILE 386 CYS 387 -0.0001

CYS 387 VAL 388 0.0355

VAL 388 ASP 389 0.0001

ASP 389 PHE 390 -0.0000

PHE 390 PRO 391 0.0432

PRO 391 ILE 392 0.0002

ILE 392 LYS 393 0.0003

LYS 393 ASP 394 0.0299

ASP 394 GLY 395 0.0002

GLY 395 LEU 396 -0.0004

LEU 396 GLY 397 -0.0013

GLY 397 LYS 398 0.0000

LYS 398 PHE 399 -0.0004

PHE 399 VAL 400 -0.0212

VAL 400 SER 401 -0.0001

SER 401 GLU 402 0.0001

GLU 402 LEU 403 -0.0069

LEU 403 ASP 404 0.0001

ASP 404 ARG 405 -0.0004

ARG 405 ARG 406 -0.0299

ARG 406 VAL 407 0.0003

VAL 407 LEU 408 -0.0000

LEU 408 GLU 409 0.0196

GLU 409 PHE 410 0.0000

PHE 410 GLY 411 0.0005

GLY 411 GLY 412 -0.0201

GLY 412 ARG 413 0.0002

ARG 413 LEU 414 -0.0002

LEU 414 TYR 415 0.0029

TYR 415 THR 416 0.0000

THR 416 ALA 417 0.0002

ALA 417 LYS 418 -0.0203

LYS 418 ASP 419 -0.0002

ASP 419 SER 420 0.0002

SER 420 ARG 421 -0.0444

ARG 421 THR 422 -0.0001

THR 422 THR 423 0.0002

THR 423 ALA 424 -0.0102

ALA 424 GLU 425 -0.0001

GLU 425 THR 426 0.0004

THR 426 PHE 427 0.0001

PHE 427 HIS 428 -0.0001

HIS 428 ALA 429 0.0002

ALA 429 MET 430 -0.0293

MET 430 TYR 431 0.0001

TYR 431 PRO 432 0.0003

PRO 432 ARG 433 0.0776

ARG 433 VAL 434 0.0003

VAL 434 ASP 435 -0.0001

ASP 435 GLU 436 0.0103

GLU 436 TRP 437 -0.0001

TRP 437 ILE 438 -0.0001

ILE 438 SER 439 -0.0120

SER 439 VAL 440 -0.0001

VAL 440 ARG 441 0.0001

ARG 441 ARG 442 0.0006

ARG 442 LYS 443 -0.0000

LYS 443 VAL 444 -0.0001

VAL 444 ASP 445 -0.0211

ASP 445 PRO 446 0.0002

PRO 446 LEU 447 0.0003

LEU 447 ARG 448 -0.0016

ARG 448 VAL 449 0.0004

VAL 449 PHE 450 0.0002

PHE 450 ALA 451 -0.0430

ALA 451 SER 452 0.0000

SER 452 ASP 453 -0.0005

ASP 453 MET 454 0.0007

MET 454 ALA 455 -0.0004

ALA 455 ARG 456 0.0001

ARG 456 ARG 457 -0.0571

ARG 457 LEU 458 0.0000

LEU 458 GLU 459 -0.0001

GLU 459 LEU 460 -0.0220

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.

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

CA strain for 20122622073737765

--- normal mode 7 ---

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

* 4P8L V/S 4FDO MP *