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

* *

CA strain for 20122711390853324

--- 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 -0.0397

ALA 10 THR 11 0.0003

THR 11 ARG 12 -0.0005

ARG 12 LEU 13 -0.0436

LEU 13 THR 14 -0.0002

THR 14 GLY 15 0.0003

GLY 15 TRP 16 -0.0719

TRP 16 GLY 17 0.0000

GLY 17 ARG 18 -0.0001

ARG 18 THR 19 -0.0284

THR 19 ALA 20 0.0002

ALA 20 PRO 21 0.0002

PRO 21 SER 22 -0.0349

SER 22 VAL 23 -0.0003

VAL 23 ALA 24 0.0003

ALA 24 ASN 25 -0.0099

ASN 25 VAL 26 0.0001

VAL 26 LEU 27 -0.0002

LEU 27 ARG 28 -0.0286

ARG 28 THR 29 -0.0000

THR 29 PRO 30 -0.0001

PRO 30 ASP 31 -0.0297

ASP 31 ALA 32 0.0000

ALA 32 GLU 33 0.0002

GLU 33 MET 34 0.0283

MET 34 ILE 35 -0.0001

ILE 35 VAL 36 0.0002

VAL 36 LYS 37 0.0039

LYS 37 ALA 38 0.0000

ALA 38 VAL 39 -0.0001

VAL 39 ALA 40 0.0003

ALA 40 ARG 41 -0.0000

ARG 41 VAL 42 -0.0002

VAL 42 ALA 43 -0.0048

ALA 43 GLU 44 -0.0001

GLU 44 SER 45 -0.0003

SER 45 GLY 46 0.0359

GLY 46 GLY 47 -0.0004

GLY 47 GLY 48 0.0002

GLY 48 ARG 49 -0.0412

ARG 49 GLY 50 0.0004

GLY 50 ALA 51 -0.0001

ALA 51 ILE 52 -0.0543

ILE 52 ALA 53 0.0003

ALA 53 ARG 54 0.0001

ARG 54 GLY 55 -0.2288

GLY 55 LEU 56 0.0002

LEU 56 GLY 57 -0.0001

GLY 57 ARG 58 0.0029

ARG 58 SER 59 -0.0000

SER 59 TYR 60 -0.0003

TYR 60 GLY 61 -0.0483

GLY 61 ASP 62 -0.0002

ASP 62 ASN 63 0.0002

ASN 63 ALA 64 0.0265

ALA 64 GLN 65 -0.0001

GLN 65 ASN 66 -0.0002

ASN 66 GLY 67 -0.0385

GLY 67 GLY 68 -0.0001

GLY 68 GLY 69 0.0001

GLY 69 LEU 70 -0.0404

LEU 70 VAL 71 0.0000

VAL 71 ILE 72 0.0001

ILE 72 ASP 73 -0.0805

ASP 73 MET 74 0.0001

MET 74 THR 75 -0.0001

THR 75 PRO 76 0.0338

PRO 76 LEU 77 -0.0001

LEU 77 ASN 78 -0.0003

ASN 78 THR 79 -0.0367

THR 79 ILE 80 0.0002

ILE 80 HIS 81 -0.0005

HIS 81 SER 82 0.0273

SER 82 ILE 83 0.0001

ILE 83 ASP 84 0.0000

ASP 84 ALA 85 0.0015

ALA 85 ASP 86 0.0002

ASP 86 THR 87 0.0003

THR 87 LYS 88 -0.0134

LYS 88 LEU 89 -0.0001

LEU 89 VAL 90 0.0001

VAL 90 ASP 91 0.0392

ASP 91 ILE 92 -0.0000

ILE 92 ASP 93 0.0002

ASP 93 ALA 94 0.0349

ALA 94 GLY 95 0.0001

GLY 95 VAL 96 0.0003

VAL 96 ASN 97 -0.0825

ASN 97 LEU 98 0.0002

LEU 98 ASP 99 0.0003

ASP 99 GLN 100 0.0846

GLN 100 LEU 101 -0.0002

LEU 101 MET 102 -0.0001

MET 102 LYS 103 0.0493

LYS 103 ALA 104 -0.0001

ALA 104 ALA 105 0.0003

ALA 105 LEU 106 -0.0827

LEU 106 PRO 107 -0.0003

PRO 107 PHE 108 -0.0002

PHE 108 GLY 109 -0.0698

GLY 109 LEU 110 0.0003

LEU 110 TRP 111 0.0003

TRP 111 VAL 112 -0.0091

VAL 112 PRO 113 0.0002

PRO 113 VAL 114 -0.0003

VAL 114 LEU 115 -0.0064

LEU 115 PRO 116 -0.0000

PRO 116 GLY 117 0.0002

GLY 117 THR 118 -0.0797

THR 118 ARG 119 -0.0003

ARG 119 GLN 120 -0.0000

GLN 120 VAL 121 -0.0589

VAL 121 THR 122 0.0002

THR 122 VAL 123 0.0002

VAL 123 GLY 124 -0.0162

GLY 124 GLY 125 -0.0001

GLY 125 ALA 126 -0.0005

ALA 126 ILE 127 -0.0214

ILE 127 ALA 128 0.0001

ALA 128 CYS 129 0.0000

CYS 129 ASP 130 -0.0023

ASP 130 ILE 131 -0.0001

ILE 131 HIS 132 0.0002

HIS 132 GLY 133 -0.0524

GLY 133 LYS 134 0.0000

LYS 134 ASN 135 0.0004

ASN 135 HIS 136 0.0273

HIS 136 HIS 137 0.0005

HIS 137 SER 138 0.0002

SER 138 ALA 139 -0.0305

ALA 139 GLY 140 0.0002

GLY 140 SER 141 0.0003

SER 141 PHE 142 -0.0282

PHE 142 GLY 143 0.0000

GLY 143 ASN 144 -0.0001

ASN 144 HIS 145 -0.0135

HIS 145 VAL 146 0.0004

VAL 146 ARG 147 -0.0003

ARG 147 SER 148 0.1262

SER 148 MET 149 0.0001

MET 149 ASP 150 -0.0001

ASP 150 LEU 151 0.0290

LEU 151 LEU 152 -0.0000

LEU 152 THR 153 -0.0000

THR 153 ALA 154 0.0214

ALA 154 ASP 155 -0.0001

ASP 155 GLY 156 -0.0002

GLY 156 GLU 157 0.0613

GLU 157 ILE 158 -0.0003

ILE 158 ARG 159 -0.0003

ARG 159 HIS 160 0.0754

HIS 160 LEU 161 0.0003

LEU 161 THR 162 -0.0005

THR 162 PRO 163 -0.0257

PRO 163 THR 164 -0.0001

THR 164 GLY 165 -0.0002

GLY 165 GLU 166 0.0020

GLU 166 ASP 167 -0.0001

ASP 167 ALA 168 -0.0004

ALA 168 GLU 169 -0.0231

GLU 169 LEU 170 0.0001

LEU 170 PHE 171 0.0004

PHE 171 TRP 172 -0.0145

TRP 172 ALA 173 -0.0003

ALA 173 THR 174 0.0002

THR 174 VAL 175 0.0242

VAL 175 GLY 176 0.0003

GLY 176 GLY 177 0.0000

GLY 177 ASN 178 0.0198

ASN 178 GLY 179 -0.0000

GLY 179 LEU 180 -0.0001

LEU 180 THR 181 0.0006

THR 181 GLY 182 0.0004

GLY 182 ILE 183 -0.0002

ILE 183 ILE 184 -0.0179

ILE 184 MET 185 0.0002

MET 185 ARG 186 0.0003

ARG 186 ALA 187 0.0474

ALA 187 THR 188 -0.0003

THR 188 ILE 189 -0.0000

ILE 189 GLU 190 0.0793

GLU 190 MET 191 0.0001

MET 191 THR 192 0.0001

THR 192 PRO 193 0.2379

PRO 193 THR 194 -0.0002

THR 194 SER 195 -0.0000

SER 195 THR 196 0.1020

THR 196 ALA 197 -0.0001

ALA 197 TYR 198 0.0006

TYR 198 PHE 199 0.0127

PHE 199 ILE 200 0.0001

ILE 200 ALA 201 -0.0002

ALA 201 ASP 202 -0.0515

ASP 202 GLY 203 -0.0001

GLY 203 ASP 204 0.0003

ASP 204 VAL 205 0.0279

VAL 205 THR 206 0.0004

THR 206 ALA 207 0.0001

ALA 207 SER 208 0.0942

SER 208 LEU 209 0.0001

LEU 209 ASP 210 0.0001

ASP 210 GLU 211 0.0057

GLU 211 THR 212 0.0000

THR 212 ILE 213 0.0004

ILE 213 ALA 214 0.0050

ALA 214 LEU 215 -0.0003

LEU 215 HIS 216 -0.0001

HIS 216 SER 217 -0.0219

SER 217 ASP 218 0.0004

ASP 218 GLY 219 -0.0003

GLY 219 SER 220 0.0150

SER 220 GLU 221 -0.0001

GLU 221 ALA 222 0.0002

ALA 222 ARG 223 0.0050

ARG 223 TYR 224 -0.0005

TYR 224 THR 225 -0.0003

THR 225 TYR 226 -0.0326

TYR 226 SER 227 -0.0004

SER 227 SER 228 0.0001

SER 228 ALA 229 0.0941

ALA 229 TRP 230 0.0001

TRP 230 PHE 231 0.0000

PHE 231 ASP 232 0.0681

ASP 232 ALA 233 0.0001

ALA 233 ILE 234 0.0001

ILE 234 SER 235 -0.0233

SER 235 ALA 236 -0.0005

ALA 236 PRO 237 -0.0002

PRO 237 PRO 238 0.0213

PRO 238 LYS 239 -0.0004

LYS 239 LEU 240 0.0003

LEU 240 GLY 241 -0.1115

GLY 241 ARG 242 -0.0001

ARG 242 ALA 243 0.0001

ALA 243 ALA 244 -0.0182

ALA 244 VAL 245 0.0005

VAL 245 SER 246 -0.0004

SER 246 ARG 247 0.0096

ARG 247 GLY 248 0.0000

GLY 248 ARG 249 -0.0004

ARG 249 LEU 250 -0.0603

LEU 250 ALA 251 0.0004

ALA 251 THR 252 -0.0004

THR 252 VAL 253 0.0765

VAL 253 GLU 254 0.0001

GLU 254 GLN 255 -0.0000

GLN 255 LEU 256 0.0198

LEU 256 PRO 257 -0.0000

PRO 257 ALA 258 0.0001

ALA 258 LYS 259 -0.0456

LYS 259 LEU 260 -0.0002

LEU 260 ARG 261 0.0000

ARG 261 SER 262 -0.0011

SER 262 GLU 263 0.0003

GLU 263 PRO 264 -0.0001

PRO 264 LEU 265 -0.1119

LEU 265 LYS 266 -0.0001

LYS 266 PHE 267 -0.0001

PHE 267 ASP 268 0.0642

ASP 268 ALA 284 0.1682

ALA 284 ASN 285 -0.0001

ASN 285 LYS 286 -0.0000

LYS 286 TYR 287 0.0270

TYR 287 THR 288 0.0001

THR 288 PHE 289 0.0001

PHE 289 GLY 290 -0.1935

GLY 290 PRO 291 -0.0001

PRO 291 ILE 292 0.0002

ILE 292 GLY 293 0.1121

GLY 293 GLU 294 0.0000

GLU 294 LEU 295 -0.0000

LEU 295 TRP 296 0.0426

TRP 296 TYR 297 0.0003

TYR 297 ARG 298 -0.0001

ARG 298 LYS 299 0.1365

LYS 299 SER 300 0.0001

SER 300 GLY 301 -0.0002

GLY 301 THR 302 0.0039

THR 302 TYR 303 -0.0002

TYR 303 ARG 304 0.0003

ARG 304 GLY 305 -0.1167

GLY 305 LYS 306 0.0002

LYS 306 VAL 307 -0.0002

VAL 307 GLN 308 -0.1097

GLN 308 ASN 309 -0.0002

ASN 309 LEU 310 0.0003

LEU 310 THR 311 0.0392

THR 311 GLN 312 0.0002

GLN 312 PHE 313 -0.0004

PHE 313 TYR 314 -0.0730

TYR 314 HIS 315 0.0003

HIS 315 GLY 331 -0.0965

GLY 331 PHE 332 0.0002

PHE 332 LEU 333 -0.0005

LEU 333 GLN 334 0.0772

GLN 334 TYR 335 -0.0000

TYR 335 GLN 336 -0.0002

GLN 336 PHE 337 0.0023

PHE 337 VAL 338 0.0003

VAL 338 ILE 339 0.0004

ILE 339 PRO 340 -0.0091

PRO 340 THR 341 -0.0001

THR 341 GLU 342 0.0002

GLU 342 ALA 343 -0.0342

ALA 343 VAL 344 -0.0003

VAL 344 ASP 345 0.0002

ASP 345 GLU 346 0.0145

GLU 346 PHE 347 0.0001

PHE 347 LYS 348 0.0002

LYS 348 LYS 349 0.0172

LYS 349 ILE 350 -0.0001

ILE 350 ILE 351 -0.0003

ILE 351 GLY 352 -0.0040

GLY 352 VAL 353 0.0001

VAL 353 ILE 354 0.0000

ILE 354 GLN 355 0.0103

GLN 355 ALA 356 -0.0001

ALA 356 SER 357 0.0000

SER 357 GLY 358 0.0002

GLY 358 HIS 359 0.0003

HIS 359 TYR 360 -0.0002

TYR 360 SER 361 0.0315

SER 361 PHE 362 -0.0001

PHE 362 LEU 363 -0.0000

LEU 363 ASN 364 0.0261

ASN 364 VAL 365 0.0001

VAL 365 PHE 366 0.0001

PHE 366 LYS 367 0.0709

LYS 367 LEU 368 -0.0001

LEU 368 PHE 369 -0.0001

PHE 369 GLY 370 0.0284

GLY 370 PRO 371 0.0002

PRO 371 ARG 372 0.0001

ARG 372 ASN 373 -0.0022

ASN 373 GLN 374 -0.0002

GLN 374 ALA 375 -0.0002

ALA 375 PRO 376 -0.0189

PRO 376 LEU 377 0.0001

LEU 377 SER 378 -0.0002

SER 378 PHE 379 0.0198

PHE 379 PRO 380 -0.0002

PRO 380 ILE 381 0.0001

ILE 381 PRO 382 0.0423

PRO 382 GLY 383 -0.0001

GLY 383 TRP 384 0.0000

TRP 384 ASN 385 -0.0133

ASN 385 ILE 386 -0.0001

ILE 386 CYS 387 -0.0001

CYS 387 VAL 388 0.0371

VAL 388 ASP 389 -0.0001

ASP 389 PHE 390 -0.0001

PHE 390 PRO 391 -0.0135

PRO 391 ILE 392 -0.0000

ILE 392 LYS 393 -0.0003

LYS 393 ASP 394 0.0321

ASP 394 GLY 395 0.0001

GLY 395 LEU 396 -0.0001

LEU 396 GLY 397 -0.0465

GLY 397 LYS 398 0.0001

LYS 398 PHE 399 -0.0001

PHE 399 VAL 400 0.0052

VAL 400 SER 401 -0.0002

SER 401 GLU 402 -0.0001

GLU 402 LEU 403 0.0086

LEU 403 ASP 404 -0.0004

ASP 404 ARG 405 -0.0000

ARG 405 ARG 406 0.0365

ARG 406 VAL 407 -0.0002

VAL 407 LEU 408 -0.0000

LEU 408 GLU 409 0.0726

GLU 409 PHE 410 -0.0004

PHE 410 GLY 411 0.0000

GLY 411 GLY 412 -0.0334

GLY 412 ARG 413 -0.0000

ARG 413 LEU 414 -0.0002

LEU 414 TYR 415 0.0272

TYR 415 THR 416 0.0002

THR 416 ALA 417 -0.0002

ALA 417 LYS 418 0.0350

LYS 418 ASP 419 -0.0001

ASP 419 SER 420 -0.0003

SER 420 ARG 421 0.1008

ARG 421 THR 422 0.0001

THR 422 THR 423 0.0002

THR 423 ALA 424 -0.1153

ALA 424 GLU 425 0.0002

GLU 425 THR 426 -0.0002

THR 426 PHE 427 -0.0054

PHE 427 HIS 428 0.0001

HIS 428 ALA 429 -0.0003

ALA 429 MET 430 0.0143

MET 430 TYR 431 -0.0004

TYR 431 PRO 432 0.0000

PRO 432 ARG 433 -0.0854

ARG 433 VAL 434 0.0001

VAL 434 ASP 435 0.0001

ASP 435 GLU 436 -0.0863

GLU 436 TRP 437 -0.0003

TRP 437 ILE 438 -0.0001

ILE 438 SER 439 -0.0344

SER 439 VAL 440 -0.0004

VAL 440 ARG 441 0.0000

ARG 441 ARG 442 0.0117

ARG 442 LYS 443 0.0000

LYS 443 VAL 444 -0.0001

VAL 444 ASP 445 0.0237

ASP 445 PRO 446 -0.0002

PRO 446 LEU 447 -0.0001

LEU 447 ARG 448 -0.0256

ARG 448 VAL 449 -0.0001

VAL 449 PHE 450 -0.0002

PHE 450 ALA 451 0.0095

ALA 451 SER 452 -0.0002

SER 452 ASP 453 -0.0001

ASP 453 MET 454 0.0521

MET 454 ALA 455 -0.0002

ALA 455 ARG 456 -0.0002

ARG 456 ARG 457 0.0379

ARG 457 LEU 458 0.0002

LEU 458 GLU 459 0.0003

GLU 459 LEU 460 -0.0481

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.

*** ***

CA strain for 20122711390853324

--- normal mode 11 ---

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

* *