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

* *

CA strain for 2405291039413992221

--- normal mode 9 ---

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
PRO 5 PRO 6 -0.0002

PRO 6 LEU 7 0.0003

LEU 7 THR 8 -0.1981

THR 8 ALA 9 -0.0000

ALA 9 HIS 10 0.0000

HIS 10 ALA 11 -0.0675

ALA 11 THR 12 0.0000

THR 12 ALA 13 -0.0000

ALA 13 ALA 14 0.0714

ALA 14 ALA 15 -0.0004

ALA 15 ILE 16 0.0000

ILE 16 ARG 17 0.0411

ARG 17 ALA 18 0.0000

ALA 18 GLY 19 0.0001

GLY 19 THR 20 0.0076

THR 20 THR 21 0.0001

THR 21 THR 22 -0.0001

THR 22 ALA 23 0.0721

ALA 23 ARG 24 -0.0003

ARG 24 GLU 25 -0.0002

GLU 25 GLN 26 -0.0807

GLN 26 ALA 27 -0.0000

ALA 27 LEU 28 -0.0002

LEU 28 ALA 29 -0.0854

ALA 29 ALA 30 0.0000

ALA 30 ILE 31 -0.0003

ILE 31 ALA 32 -0.0189

ALA 32 ARG 33 0.0000

ARG 33 ILE 34 0.0004

ILE 34 GLU 35 -0.0374

GLU 35 THR 36 0.0001

THR 36 LEU 37 0.0002

LEU 37 ASP 38 0.0171

ASP 38 PRO 39 0.0001

PRO 39 GLU 40 0.0000

GLU 40 ILE 41 -0.0023

ILE 41 ASN 42 0.0002

ASN 42 ALA 43 0.0003

ALA 43 VAL 44 0.0144

VAL 44 PRO 45 0.0002

PRO 45 VAL 46 0.0002

VAL 46 ARG 47 0.2038

ARG 47 ASP 48 0.0002

ASP 48 PHE 49 -0.0000

PHE 49 ASP 50 0.0586

ASP 50 ARG 51 -0.0001

ARG 51 ALA 52 -0.0002

ALA 52 LEU 53 0.1036

LEU 53 ALA 54 0.0001

ALA 54 ALA 55 0.0000

ALA 55 ALA 56 0.0042

ALA 56 ASP 57 0.0002

ASP 57 ALA 58 0.0001

ALA 58 ALA 59 -0.0472

ALA 59 ASP 60 0.0003

ASP 60 ALA 61 0.0000

ALA 61 ARG 62 0.0127

ARG 62 LEU 63 0.0001

LEU 63 ALA 64 0.0001

ALA 64 ALA 65 -0.0396

ALA 65 GLY 66 -0.0000

GLY 66 ASP 67 0.0000

ASP 67 THR 68 -0.0964

THR 68 ALA 69 -0.0002

ALA 69 PRO 70 0.0002

PRO 70 LEU 71 -0.0453

LEU 71 LEU 72 0.0003

LEU 72 GLY 73 0.0000

GLY 73 VAL 74 0.0333

VAL 74 PRO 75 -0.0002

PRO 75 MET 76 -0.0000

MET 76 THR 77 0.1429

THR 77 VAL 78 -0.0002

VAL 78 LYS 79 0.0002

LYS 79 GLU 80 -0.0076

GLU 80 ALA 81 -0.0003

ALA 81 PHE 82 0.0003

PHE 82 ASP 83 -0.0157

ASP 83 ILE 84 -0.0001

ILE 84 ALA 85 0.0003

ALA 85 GLY 86 0.0210

GLY 86 LEU 87 -0.0002

LEU 87 PRO 88 0.0002

PRO 88 THR 89 0.1701

THR 89 HIS 90 0.0000

HIS 90 TRP 91 0.0001

TRP 91 GLY 92 -0.0208

GLY 92 PHE 93 -0.0004

PHE 93 ALA 94 0.0002

ALA 94 GLU 95 0.0103

GLU 95 HIS 96 0.0003

HIS 96 ARG 97 -0.0000

ARG 97 ASN 98 0.0074

ASN 98 ASN 99 -0.0002

ASN 99 VAL 100 -0.0000

VAL 100 ALA 101 -0.0991

ALA 101 THR 102 0.0003

THR 102 THR 103 -0.0004

THR 103 ASP 104 -0.0075

ASP 104 ALA 105 -0.0001

ALA 105 HIS 106 -0.0002

HIS 106 ALA 107 -0.0361

ALA 107 VAL 108 -0.0001

VAL 108 ALA 109 0.0003

ALA 109 ARG 110 -0.0384

ARG 110 LEU 111 -0.0000

LEU 111 LYS 112 0.0000

LYS 112 ALA 113 -0.0204

ALA 113 ALA 114 0.0001

ALA 114 GLY 115 0.0001

GLY 115 ALA 116 -0.0232

ALA 116 ILE 117 -0.0001

ILE 117 ILE 118 0.0002

ILE 118 LEU 119 -0.0059

LEU 119 GLY 120 0.0003

GLY 120 LYS 121 0.0000

LYS 121 SER 122 -0.0213

SER 122 ASN 123 -0.0003

ASN 123 VAL 124 0.0002

VAL 124 PRO 125 0.0230

PRO 125 LYS 126 0.0001

LYS 126 GLY 127 -0.0002

GLY 127 LEU 128 0.0857

LEU 128 GLY 129 0.0001

GLY 129 ASP 130 0.0001

ASP 130 TRP 131 0.0059

TRP 131 GLN 132 -0.0002

GLN 132 SER 133 0.0000

SER 133 VAL 134 -0.0082

VAL 134 ASN 135 -0.0002

ASN 135 SER 136 0.0001

SER 136 ILE 137 0.0508

ILE 137 HIS 138 -0.0002

HIS 138 GLY 139 -0.0002

GLY 139 ARG 140 -0.1349

ARG 140 THR 141 0.0003

THR 141 ASN 142 -0.0000

ASN 142 HIS 143 -0.1736

HIS 143 PRO 144 -0.0000

PRO 144 LEU 145 -0.0003

LEU 145 ASP 146 0.0399

ASP 146 PRO 147 0.0001

PRO 147 ALA 148 0.0002

ALA 148 ARG 149 -0.0084

ARG 149 THR 150 0.0001

THR 150 SER 151 0.0002

SER 151 GLY 152 0.0174

GLY 152 GLY 153 -0.0001

GLY 153 SER 154 -0.0000

SER 154 SER 155 0.0145

SER 155 GLY 156 -0.0001

GLY 156 GLY 157 -0.0001

GLY 157 GLY 158 -0.0024

GLY 158 ALA 159 0.0000

ALA 159 ALA 160 0.0002

ALA 160 ALA 161 0.0560

ALA 161 VAL 162 -0.0004

VAL 162 ALA 163 -0.0001

ALA 163 ALA 164 -0.1476

ALA 164 GLY 165 0.0001

GLY 165 MET 166 0.0003

MET 166 VAL 167 -0.0266

VAL 167 PRO 168 0.0002

PRO 168 ILE 169 0.0002

ILE 169 GLU 170 0.0545

GLU 170 LEU 171 -0.0002

LEU 171 GLY 172 -0.0001

GLY 172 SER 173 0.1030

SER 173 ASP 174 -0.0001

ASP 174 VAL 175 0.0002

VAL 175 GLY 176 -0.0430

GLY 176 GLY 177 -0.0000

GLY 177 SER 178 -0.0003

SER 178 ILE 179 -0.0162

ILE 179 ARG 180 -0.0003

ARG 180 VAL 181 0.0000

VAL 181 PRO 182 0.0038

PRO 182 ALA 183 0.0003

ALA 183 HIS 184 0.0003

HIS 184 PHE 185 -0.0050

PHE 185 CYS 186 0.0001

CYS 186 GLY 187 -0.0004

GLY 187 ILE 188 0.0406

ILE 188 TRP 189 0.0003

TRP 189 GLY 190 -0.0005

GLY 190 HIS 191 0.0290

HIS 191 LYS 192 -0.0002

LYS 192 PRO 193 -0.0000

PRO 193 SER 194 -0.0000

SER 194 TRP 195 0.0001

TRP 195 ASN 196 -0.0000

ASN 196 ALA 197 -0.1615

ALA 197 ILE 198 0.0000

ILE 198 SER 199 -0.0002

SER 199 SER 200 0.0378

SER 200 ASP 201 0.0003

ASP 201 GLY 202 -0.0002

GLY 202 HIS 203 -0.0168

HIS 203 ARG 204 -0.0002

ARG 204 TYR 205 0.0000

TYR 205 PRO 206 0.0906

PRO 206 GLY 207 0.0001

GLY 207 THR 208 -0.0004

THR 208 ASP 209 0.0884

ASP 209 GLY 210 -0.0005

GLY 210 THR 211 0.0001

THR 211 GLU 212 0.1885

GLU 212 THR 213 0.0004

THR 213 VAL 214 -0.0001

VAL 214 LEU 215 0.1391

LEU 215 GLY 216 -0.0000

GLY 216 VAL 217 0.0002

VAL 217 ILE 218 0.0151

ILE 218 GLY 219 0.0003

GLY 219 PRO 220 -0.0005

PRO 220 LEU 221 0.0404

LEU 221 ALA 222 0.0001

ALA 222 ARG 223 0.0001

ARG 223 ASP 224 -0.0813

ASP 224 PRO 225 0.0002

PRO 225 GLN 226 -0.0000

GLN 226 ASP 227 -0.0573

ASP 227 LEU 228 0.0001

LEU 228 ALA 229 -0.0004

ALA 229 LEU 230 -0.1832

LEU 230 MET 231 -0.0001

MET 231 ILE 232 -0.0000

ILE 232 ASP 233 0.0345

ASP 233 LEU 234 0.0003

LEU 234 LEU 235 -0.0001

LEU 235 ALA 236 -0.0183

ALA 236 THR 237 -0.0002

THR 237 LEU 238 -0.0000

LEU 238 PRO 239 0.0135

PRO 239 LEU 240 -0.0004

LEU 240 PRO 241 -0.0001

PRO 241 ARG 242 0.0791

ARG 242 PRO 243 -0.0000

PRO 243 ALA 244 0.0004

ALA 244 ALA 245 0.0634

ALA 245 ARG 246 -0.0000

ARG 246 THR 247 -0.0002

THR 247 ARG 248 -0.0712

ARG 248 ARG 249 -0.0002

ARG 249 VAL 250 -0.0001

VAL 250 LEU 251 0.0423

LEU 251 VAL 252 -0.0000

VAL 252 LEU 253 -0.0002

LEU 253 ALA 254 -0.0111

ALA 254 GLN 255 -0.0002

GLN 255 HIS 256 0.0001

HIS 256 PRO 257 -0.0333

PRO 257 GLU 258 -0.0001

GLU 258 THR 259 -0.0005

THR 259 ARG 260 -0.1027

ARG 260 THR 261 0.0003

THR 261 ALA 262 -0.0000

ALA 262 HIS 263 0.0329

HIS 263 ALA 264 0.0004

ALA 264 VAL 265 0.0001

VAL 265 VAL 266 -0.0239

VAL 266 GLU 267 0.0002

GLU 267 GLY 268 0.0002

GLY 268 VAL 269 -0.0368

VAL 269 GLU 270 0.0003

GLU 270 ARG 271 0.0000

ARG 271 ALA 272 0.0104

ALA 272 ALA 273 0.0004

ALA 273 ALA 274 -0.0002

ALA 274 ALA 275 0.0012

ALA 275 LEU 276 -0.0001

LEU 276 ALA 277 0.0002

ALA 277 ARG 278 -0.0139

ARG 278 ALA 279 -0.0003

ALA 279 GLY 280 -0.0001

GLY 280 VAL 281 0.0320

VAL 281 GLU 282 0.0001

GLU 282 VAL 283 -0.0003

VAL 283 VAL 284 -0.0365

VAL 284 ARG 285 0.0001

ARG 285 HIS 286 -0.0000

HIS 286 SER 287 -0.0394

SER 287 ASP 288 0.0005

ASP 288 LEU 289 0.0002

LEU 289 LEU 290 0.0408

LEU 290 PRO 291 -0.0002

PRO 291 ASP 292 0.0004

ASP 292 LEU 293 0.0149

LEU 293 SER 294 -0.0002

SER 294 ARG 295 0.0004

ARG 295 GLN 296 -0.0186

GLN 296 HIS 297 -0.0001

HIS 297 SER 298 -0.0004

SER 298 ALA 299 -0.0518

ALA 299 TYR 300 -0.0001

TYR 300 GLY 301 -0.0002

GLY 301 ASP 302 -0.1015

ASP 302 LEU 303 0.0002

LEU 303 LEU 304 0.0000

LEU 304 ASN 305 -0.0747

ASN 305 VAL 306 -0.0003

VAL 306 THR 307 0.0001

THR 307 PHE 308 0.0748

PHE 308 ALA 309 0.0003

ALA 309 ARG 310 -0.0003

ARG 310 SER 311 0.0312

SER 311 ASN 312 0.0001

ASN 312 PRO 313 -0.0001

PRO 313 ALA 314 0.0584

ALA 314 LEU 315 -0.0002

LEU 315 HIS 316 0.0001

HIS 316 HIS 317 0.0713

HIS 317 THR 318 -0.0001

THR 318 LEU 319 0.0003

LEU 319 PRO 320 0.0537

PRO 320 SER 321 -0.0003

SER 321 LEU 322 -0.0001

LEU 322 LEU 323 -0.0548

LEU 323 LYS 324 -0.0002

LYS 324 TRP 325 0.0000

TRP 325 LEU 326 0.0191

LEU 326 SER 327 -0.0003

SER 327 MET 328 -0.0001

MET 328 LEU 329 -0.0301

LEU 329 ASP 330 0.0001

ASP 330 ALA 331 0.0003

ALA 331 GLN 332 -0.0146

GLN 332 ALA 333 -0.0000

ALA 333 ARG 334 0.0001

ARG 334 SER 335 -0.0721

SER 335 THR 336 0.0002

THR 336 ARG 337 0.0004

ARG 337 ALA 338 0.0275

ALA 338 TRP 339 0.0001

TRP 339 GLY 340 -0.0002

GLY 340 ALA 341 0.0133

ALA 341 LEU 342 0.0000

LEU 342 PHE 343 0.0001

PHE 343 GLY 344 0.0052

GLY 344 GLU 345 0.0002

GLU 345 PHE 346 -0.0000

PHE 346 ASP 347 -0.1086

ASP 347 ALA 348 -0.0001

ALA 348 VAL 349 0.0002

VAL 349 ILE 350 0.0117

ILE 350 ALA 351 -0.0003

ALA 351 PRO 352 -0.0002

PRO 352 PRO 353 0.0135

PRO 353 ALA 354 0.0003

ALA 354 ALA 355 -0.0001

ALA 355 THR 356 -0.0324

THR 356 GLN 357 -0.0003

GLN 357 ALA 358 -0.0001

ALA 358 PHE 359 0.0261

PHE 359 ALA 360 0.0001

ALA 360 HIS 361 0.0001

HIS 361 ASP 362 0.0261

ASP 362 HIS 363 -0.0002

HIS 363 SER 364 0.0002

SER 364 PRO 365 -0.0262

PRO 365 LEU 366 -0.0003

LEU 366 ALA 367 0.0003

ALA 367 ASP 368 -0.0152

ASP 368 ARG 369 -0.0000

ARG 369 THR 370 0.0001

THR 370 LEU 371 0.0167

LEU 371 ALA 372 -0.0001

ALA 372 ILE 373 -0.0001

ILE 373 ASP 374 0.0068

ASP 374 GLY 375 -0.0001

GLY 375 THR 376 -0.0000

THR 376 PRO 377 0.0057

PRO 377 GLY 378 0.0001

GLY 378 PRO 379 -0.0001

PRO 379 TYR 380 0.0257

TYR 380 ASP 381 0.0002

ASP 381 ALA 382 0.0002

ALA 382 HIS 383 -0.0354

HIS 383 LEU 384 -0.0002

LEU 384 ALA 385 0.0002

ALA 385 TRP 386 0.0074

TRP 386 ALA 387 0.0005

ALA 387 GLY 388 -0.0001

GLY 388 LEU 389 0.0184

LEU 389 ALA 390 0.0002

ALA 390 THR 391 0.0002

THR 391 TYR 392 0.0190

TYR 392 PRO 393 -0.0004

PRO 393 GLY 394 0.0001

GLY 394 LEU 395 -0.0231

LEU 395 PRO 396 -0.0002

PRO 396 ALA 397 0.0001

ALA 397 THR 398 -0.0862

THR 398 CYS 399 0.0001

CYS 399 MET 400 -0.0001

MET 400 PRO 401 0.0895

PRO 401 VAL 402 0.0003

VAL 402 GLY 403 0.0001

GLY 403 LEU 404 0.0686

LEU 404 ILE 405 0.0001

ILE 405 ASP 406 -0.0003

ASP 406 GLY 407 -0.0575

GLY 407 LEU 408 0.0004

LEU 408 PRO 409 -0.0001

PRO 409 THR 410 -0.0240

THR 410 GLY 411 0.0001

GLY 411 VAL 412 0.0000

VAL 412 GLN 413 0.0475

GLN 413 VAL 414 0.0003

VAL 414 ILE 415 0.0001

ILE 415 THR 416 0.0138

THR 416 GLU 417 0.0002

GLU 417 LEU 418 -0.0001

LEU 418 HIS 419 -0.1144

HIS 419 GLN 420 0.0000

GLN 420 ASP 421 -0.0004

ASP 421 HIS 422 -0.0141

HIS 422 ARG 423 -0.0001

ARG 423 ALA 424 -0.0001

ALA 424 ILE 425 -0.1555

ILE 425 GLU 426 0.0004

GLU 426 ILE 427 0.0002

ILE 427 ALA 428 -0.0791

ALA 428 ALA 429 -0.0001

ALA 429 LEU 430 -0.0001

LEU 430 ILE 431 0.0459

ILE 431 ALA 432 0.0000

ALA 432 GLN 433 -0.0001

GLN 433 HIS 434 -0.0536

HIS 434 LEU 435 -0.0003

LEU 435 SER 436 -0.0004

SER 436 PRO 437 -0.0508

PRO 437 SER 438 0.0002

SER 438 PRO 439 -0.0001

PRO 439 GLN 440 0.0274

GLN 440 GLY 441 0.0001

GLY 441 ALA 442 -0.0004

ALA 442 ILE 443 -0.1578

ILE 443 ALA 444 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: April 25th, 2023.

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

*** ***

CA strain for 2405291039413992221

--- normal mode 9 ---

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

* *