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

* HYDROLASE 05-OCT-15 5E3X *

CA strain for 240327160220988694

--- normal mode 27 ---

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
MET 1 GLU 2 -0.0003

GLU 2 GLU 3 0.0002

GLU 3 LEU 4 0.0978

LEU 4 LYS 5 -0.0001

LYS 5 SER 6 0.0001

SER 6 TYR 7 -0.1126

TYR 7 TYR 8 0.0002

TYR 8 LYS 9 -0.0000

LYS 9 ARG 10 0.0042

ARG 10 VAL 11 0.0000

VAL 11 ALA 12 -0.0003

ALA 12 LYS 13 -0.1323

LYS 13 TYR 14 0.0003

TYR 14 TYR 15 0.0002

TYR 15 SER 16 0.0680

SER 16 ALA 17 -0.0003

ALA 17 ALA 18 -0.0003

ALA 18 ALA 19 0.0466

ALA 19 LEU 20 -0.0003

LEU 20 LEU 21 -0.0001

LEU 21 TYR 22 0.1308

TYR 22 TRP 23 -0.0002

TRP 23 ASP 24 0.0000

ASP 24 MET 25 -0.0375

MET 25 GLN 26 -0.0003

GLN 26 THR 27 -0.0000

THR 27 TYR 28 0.1020

TYR 28 MET 29 0.0001

MET 29 PRO 30 0.0002

PRO 30 LYS 31 -0.3084

LYS 31 ASP 32 0.0000

ASP 32 ALA 33 -0.0001

ALA 33 GLY 34 0.0024

GLY 34 PRO 35 -0.0002

PRO 35 TYR 36 0.0001

TYR 36 ARG 37 0.1020

ARG 37 ALA 38 0.0000

ALA 38 GLU 39 0.0002

GLU 39 VAL 40 0.2681

VAL 40 LEU 41 -0.0000

LEU 41 SER 42 -0.0003

SER 42 GLU 43 0.1236

GLU 43 ILE 44 -0.0000

ILE 44 GLY 45 -0.0001

GLY 45 THR 46 -0.0715

THR 46 TYR 47 0.0003

TYR 47 ALA 48 0.0003

ALA 48 PHE 49 0.1502

PHE 49 LYS 50 -0.0003

LYS 50 GLN 51 0.0001

GLN 51 ILE 52 0.1255

ILE 52 THR 53 -0.0000

THR 53 ASP 54 -0.0000

ASP 54 ASP 55 0.0395

ASP 55 ALA 56 0.0001

ALA 56 LEU 57 0.0002

LEU 57 GLY 58 -0.0302

GLY 58 LYS 59 0.0000

LYS 59 LEU 60 -0.0002

LEU 60 LEU 61 -0.0050

LEU 61 GLU 62 0.0001

GLU 62 THR 63 0.0002

THR 63 ALA 64 0.0165

ALA 64 GLN 65 -0.0003

GLN 65 PRO 66 0.0002

PRO 66 GLN 67 0.0631

GLN 67 SER 68 -0.0000

SER 68 GLU 69 0.0001

GLU 69 ILE 70 -0.1048

ILE 70 ASP 71 0.0001

ASP 71 GLU 72 0.0002

GLU 72 LYS 73 -0.1757

LYS 73 LEU 74 0.0001

LEU 74 VAL 75 0.0002

VAL 75 TYR 76 0.0160

TYR 76 VAL 77 0.0002

VAL 77 GLY 78 0.0002

GLY 78 LYS 79 0.0947

LYS 79 LYS 80 0.0001

LYS 80 GLU 81 0.0000

GLU 81 TYR 82 0.0402

TYR 82 TYR 83 -0.0003

TYR 83 LYS 84 -0.0000

LYS 84 TYR 85 0.0478

TYR 85 LYS 86 -0.0001

LYS 86 LYS 87 0.0000

LYS 87 VAL 88 -0.0101

VAL 88 PRO 89 -0.0003

PRO 89 PRO 90 0.0001

PRO 90 GLU 91 -0.1225

GLU 91 LEU 92 -0.0005

LEU 92 PHE 93 -0.0001

PHE 93 GLN 94 -0.1214

GLN 94 GLU 95 -0.0001

GLU 95 ILE 96 -0.0000

ILE 96 MET 97 -0.0903

MET 97 ILE 98 -0.0001

ILE 98 THR 99 0.0003

THR 99 SER 100 -0.2180

SER 100 THR 101 0.0003

THR 101 MET 102 0.0001

MET 102 LEU 103 -0.0969

LEU 103 GLU 104 -0.0001

GLU 104 GLN 105 0.0001

GLN 105 LYS 106 0.1251

LYS 106 TRP 107 0.0001

TRP 107 GLU 108 -0.0002

GLU 108 ILE 109 0.1560

ILE 109 ALA 110 0.0002

ALA 110 LYS 111 0.0001

LYS 111 PRO 112 0.1537

PRO 112 ARG 113 0.0001

ARG 113 GLY 114 0.0004

GLY 114 ASP 115 0.0655

ASP 115 PHE 116 -0.0005

PHE 116 GLU 117 -0.0000

GLU 117 GLU 118 0.0833

GLU 118 VAL 119 0.0001

VAL 119 ARG 120 -0.0000

ARG 120 PRO 121 0.0156

PRO 121 LEU 122 0.0000

LEU 122 LEU 123 0.0002

LEU 123 GLU 124 0.0863

GLU 124 LYS 125 -0.0003

LYS 125 ILE 126 -0.0004

ILE 126 VAL 127 0.1809

VAL 127 ASP 128 0.0002

ASP 128 LEU 129 0.0002

LEU 129 SER 130 -0.1274

SER 130 ARG 131 0.0001

ARG 131 LYS 132 0.0001

LYS 132 TYR 133 -0.1682

TYR 133 ALA 134 0.0003

ALA 134 ASP 135 0.0002

ASP 135 ILE 136 0.0157

ILE 136 LEU 137 -0.0001

LEU 137 GLY 138 -0.0002

GLY 138 TYR 139 0.2379

TYR 139 GLU 140 -0.0000

GLU 140 GLY 141 -0.0000

GLY 141 GLU 142 -0.0948

GLU 142 PRO 143 -0.0000

PRO 143 TYR 144 0.0001

TYR 144 ASN 145 0.0237

ASN 145 ALA 146 -0.0002

ALA 146 LEU 147 -0.0000

LEU 147 LEU 148 -0.1396

LEU 148 ASP 149 -0.0000

ASP 149 LEU 150 0.0000

LEU 150 TYR 151 -0.0042

TYR 151 GLU 152 -0.0004

GLU 152 PRO 153 -0.0000

PRO 153 GLY 154 0.0769

GLY 154 MET 155 0.0000

MET 155 LYS 156 0.0001

LYS 156 ALA 157 0.0230

ALA 157 GLU 158 -0.0000

GLU 158 GLU 159 0.0000

GLU 159 VAL 160 0.1090

VAL 160 ASP 161 0.0002

ASP 161 GLN 162 -0.0000

GLN 162 ILE 163 -0.0002

ILE 163 PHE 164 -0.0002

PHE 164 SER 165 0.0005

SER 165 LYS 166 -0.0887

LYS 166 VAL 167 -0.0004

VAL 167 ARG 168 0.0003

ARG 168 ASP 169 -0.1548

ASP 169 PHE 170 -0.0001

PHE 170 ILE 171 0.0002

ILE 171 VAL 172 -0.0031

VAL 172 GLU 173 -0.0001

GLU 173 VAL 174 0.0001

VAL 174 LEU 175 0.1004

LEU 175 GLU 176 -0.0001

GLU 176 LYS 177 -0.0000

LYS 177 ILE 178 0.1096

ILE 178 GLU 179 -0.0001

GLU 179 ARG 180 -0.0002

ARG 180 LEU 181 0.0656

LEU 181 PRO 182 0.0003

PRO 182 LYS 183 -0.0001

LYS 183 SER 184 0.2669

SER 184 GLU 185 -0.0001

GLU 185 ASP 186 -0.0002

ASP 186 PRO 187 0.1604

PRO 187 PHE 188 0.0001

PHE 188 ASN 189 -0.0001

ASN 189 ARG 190 0.0625

ARG 190 GLU 191 0.0000

GLU 191 ILE 192 -0.0000

ILE 192 GLY 193 0.1511

GLY 193 VAL 194 -0.0001

VAL 194 ASP 195 -0.0001

ASP 195 LYS 196 0.0693

LYS 196 GLN 197 -0.0000

GLN 197 LYS 198 -0.0003

LYS 198 GLU 199 0.0151

GLU 199 PHE 200 -0.0001

PHE 200 SER 201 0.0002

SER 201 ASN 202 -0.0342

ASN 202 TRP 203 -0.0001

TRP 203 LEU 204 -0.0000

LEU 204 LEU 205 -0.1218

LEU 205 HIS 206 0.0001

HIS 206 TYR 207 0.0001

TYR 207 LEU 208 -0.0519

LEU 208 LYS 209 0.0000

LYS 209 TYR 210 -0.0005

TYR 210 ASP 211 -0.1152

ASP 211 PHE 212 0.0001

PHE 212 THR 213 0.0001

THR 213 LYS 214 -0.0118

LYS 214 GLY 215 0.0003

GLY 215 ARG 216 -0.0003

ARG 216 LEU 217 -0.0154

LEU 217 ASP 218 0.0003

ASP 218 VAL 219 -0.0003

VAL 219 SER 220 -0.1046

SER 220 ALA 221 -0.0000

ALA 221 HIS 222 0.0001

HIS 222 PRO 223 0.1039

PRO 223 PHE 224 -0.0000

PHE 224 THR 225 -0.0002

THR 225 ASN 226 0.0686

ASN 226 PRO 227 -0.0004

PRO 227 ILE 228 -0.0000

ILE 228 GLY 229 -0.1639

GLY 229 LEU 230 0.0001

LEU 230 ASN 231 -0.0001

ASN 231 ASP 232 -0.0425

ASP 232 VAL 233 -0.0000

VAL 233 ARG 234 0.0001

ARG 234 ILE 235 -0.0054

ILE 235 THR 236 -0.0001

THR 236 THR 237 -0.0001

THR 237 ARG 238 0.0979

ARG 238 TYR 239 0.0000

TYR 239 ILE 240 0.0002

ILE 240 VAL 241 0.1366

VAL 241 ASN 242 0.0001

ASN 242 ASP 243 -0.0002

ASP 243 ILE 244 -0.0104

ILE 244 ARG 245 -0.0003

ARG 245 ASN 246 0.0002

ASN 246 SER 247 -0.1197

SER 247 ILE 248 -0.0000

ILE 248 TYR 249 0.0002

TYR 249 SER 250 -0.1262

SER 250 THR 251 0.0002

THR 251 ILE 252 -0.0003

ILE 252 HIS 253 0.0237

HIS 253 GLU 254 -0.0001

GLU 254 PHE 255 -0.0002

PHE 255 GLY 256 0.0327

GLY 256 HIS 257 0.0002

HIS 257 ALA 258 -0.0002

ALA 258 LEU 259 -0.0133

LEU 259 TYR 260 -0.0001

TYR 260 ALA 261 0.0004

ALA 261 LEU 262 -0.0418

LEU 262 SER 263 0.0001

SER 263 ILE 264 0.0003

ILE 264 PRO 265 -0.1128

PRO 265 THR 266 -0.0000

THR 266 GLU 267 0.0001

GLU 267 PHE 268 -0.0455

PHE 268 TYR 269 0.0000

TYR 269 GLY 270 -0.0000

GLY 270 LEU 271 -0.0400

LEU 271 PRO 272 0.0001

PRO 272 ILE 273 -0.0002

ILE 273 GLY 274 0.0124

GLY 274 SER 275 0.0001

SER 275 SER 276 -0.0002

SER 276 ALA 277 0.2473

ALA 277 SER 278 -0.0003

SER 278 TYR 279 0.0002

TYR 279 GLY 280 0.0258

GLY 280 PHE 281 -0.0000

PHE 281 ASP 282 -0.0000

ASP 282 GLU 283 -0.1301

GLU 283 SER 284 0.0001

SER 284 GLN 285 -0.0003

GLN 285 SER 286 -0.0056

SER 286 ARG 287 0.0003

ARG 287 PHE 288 -0.0000

PHE 288 TRP 289 0.0921

TRP 289 GLU 290 -0.0002

GLU 290 ASN 291 -0.0000

ASN 291 VAL 292 0.0846

VAL 292 VAL 293 0.0001

VAL 293 GLY 294 -0.0002

GLY 294 ARG 295 -0.0976

ARG 295 SER 296 -0.0000

SER 296 LEU 297 -0.0002

LEU 297 ALA 298 -0.1172

ALA 298 PHE 299 0.0004

PHE 299 TRP 300 0.0000

TRP 300 LYS 301 -0.0461

LYS 301 GLY 302 0.0002

GLY 302 ILE 303 0.0003

ILE 303 TYR 304 -0.1392

TYR 304 SER 305 0.0002

SER 305 LYS 306 0.0000

LYS 306 PHE 307 -0.0316

PHE 307 ILE 308 0.0003

ILE 308 GLU 309 -0.0002

GLU 309 ILE 310 -0.0102

ILE 310 VAL 311 -0.0002

VAL 311 PRO 312 -0.0001

PRO 312 GLU 313 -0.0067

GLU 313 MET 314 -0.0005

MET 314 ARG 315 0.0003

ARG 315 GLY 316 0.0359

GLY 316 TYR 317 -0.0000

TYR 317 SER 318 0.0003

SER 318 VAL 319 -0.0120

VAL 319 GLU 320 -0.0001

GLU 320 GLU 321 0.0001

GLU 321 LEU 322 -0.1349

LEU 322 TRP 323 -0.0000

TRP 323 ARG 324 0.0000

ARG 324 ALA 325 -0.1019

ALA 325 VAL 326 0.0000

VAL 326 ASN 327 0.0006

ASN 327 ARG 328 -0.2581

ARG 328 VAL 329 -0.0002

VAL 329 GLN 330 0.0003

GLN 330 ARG 331 -0.2850

ARG 331 SER 332 0.0002

SER 332 PHE 333 -0.0003

PHE 333 ILE 334 -0.1141

ILE 334 ARG 335 -0.0002

ARG 335 THR 336 0.0003

THR 336 GLU 337 -0.0886

GLU 337 ALA 338 -0.0002

ALA 338 ASP 339 0.0001

ASP 339 GLU 340 0.0859

GLU 340 VAL 341 -0.0003

VAL 341 THR 342 0.0004

THR 342 TYR 343 -0.2212

TYR 343 ASN 344 -0.0001

ASN 344 LEU 345 0.0002

LEU 345 HIS 346 -0.0617

HIS 346 ILE 347 -0.0003

ILE 347 ILE 348 0.0001

ILE 348 ILE 349 0.0306

ILE 349 ARG 350 0.0000

ARG 350 PHE 351 -0.0000

PHE 351 GLU 352 0.0120

GLU 352 ILE 353 0.0000

ILE 353 GLU 354 0.0003

GLU 354 ARG 355 0.0982

ARG 355 GLU 356 -0.0005

GLU 356 LEU 357 -0.0002

LEU 357 ILE 358 -0.0473

ILE 358 ASN 359 -0.0000

ASN 359 GLY 360 0.0001

GLY 360 GLU 361 0.0952

GLU 361 LEU 362 0.0002

LEU 362 SER 363 0.0000

SER 363 VAL 364 -0.0111

VAL 364 LYS 365 0.0001

LYS 365 ASP 366 0.0000

ASP 366 VAL 367 -0.0106

VAL 367 PRO 368 -0.0002

PRO 368 ASP 369 -0.0001

ASP 369 LYS 370 -0.0736

LYS 370 TRP 371 0.0003

TRP 371 ASN 372 -0.0002

ASN 372 GLU 373 -0.1227

GLU 373 LEU 374 -0.0003

LEU 374 TYR 375 0.0001

TYR 375 LYS 376 -0.0506

LYS 376 LYS 377 0.0003

LYS 377 TYR 378 -0.0001

TYR 378 LEU 379 0.0522

LEU 379 GLY 380 0.0001

GLY 380 LEU 381 -0.0003

LEU 381 ASP 382 -0.1691

ASP 382 VAL 383 0.0003

VAL 383 PRO 384 -0.0000

PRO 384 ASN 385 0.0012

ASN 385 ASN 386 -0.0001

ASN 386 THR 387 -0.0000

THR 387 LEU 388 0.0995

LEU 388 GLY 389 -0.0002

GLY 389 CYS 390 0.0001

CYS 390 MET 391 -0.1144

MET 391 GLN 392 -0.0001

GLN 392 ASP 393 0.0002

ASP 393 PRO 394 -0.4883

PRO 394 HIS 395 0.0000

HIS 395 TRP 396 0.0003

TRP 396 PHE 397 -0.1041

PHE 397 GLY 398 0.0000

GLY 398 GLY 399 0.0002

GLY 399 ASN 400 -0.2437

ASN 400 PHE 401 0.0002

PHE 401 GLY 402 0.0001

GLY 402 TYR 403 0.0230

TYR 403 PHE 404 0.0003

PHE 404 PRO 405 -0.0002

PRO 405 THR 406 -0.0380

THR 406 TYR 407 0.0002

TYR 407 ALA 408 0.0004

ALA 408 LEU 409 0.0883

LEU 409 GLY 410 0.0004

GLY 410 ASN 411 0.0001

ASN 411 LEU 412 0.0451

LEU 412 TYR 413 -0.0003

TYR 413 ALA 414 -0.0001

ALA 414 ALA 415 -0.0588

ALA 415 GLN 416 0.0001

GLN 416 ILE 417 0.0001

ILE 417 PHE 418 0.0240

PHE 418 GLU 419 -0.0002

GLU 419 LYS 420 -0.0002

LYS 420 LEU 421 0.0370

LEU 421 LYS 422 -0.0004

LYS 422 GLU 423 0.0003

GLU 423 GLU 424 -0.0398

GLU 424 ILE 425 0.0000

ILE 425 ASN 426 0.0000

ASN 426 PHE 427 -0.0369

PHE 427 GLU 428 -0.0000

GLU 428 GLU 429 0.0000

GLU 429 VAL 430 0.0531

VAL 430 VAL 431 -0.0000

VAL 431 SER 432 -0.0003

SER 432 ALA 433 -0.0659

ALA 433 GLY 434 -0.0000

GLY 434 ASN 435 -0.0004

ASN 435 PHE 436 0.0030

PHE 436 GLU 437 0.0002

GLU 437 ILE 438 0.0001

ILE 438 ILE 439 -0.0483

ILE 439 LYS 440 0.0001

LYS 440 ASN 441 0.0000

ASN 441 PHE 442 -0.0771

PHE 442 LEU 443 0.0000

LEU 443 LYS 444 0.0003

LYS 444 GLU 445 -0.0454

GLU 445 LYS 446 -0.0000

LYS 446 ILE 447 -0.0001

ILE 447 HIS 448 -0.0527

HIS 448 SER 449 0.0004

SER 449 LYS 450 -0.0001

LYS 450 GLY 451 0.2079

GLY 451 LYS 452 -0.0001

LYS 452 MET 453 0.0005

MET 453 TYR 454 -0.2142

TYR 454 GLU 455 -0.0001

GLU 455 PRO 456 0.0001

PRO 456 SER 457 -0.0418

SER 457 ASP 458 -0.0000

ASP 458 LEU 459 -0.0003

LEU 459 ILE 460 -0.1471

ILE 460 LYS 461 -0.0001

LYS 461 ILE 462 -0.0002

ILE 462 VAL 463 0.0130

VAL 463 THR 464 0.0000

THR 464 GLY 465 0.0002

GLY 465 LYS 466 0.1197

LYS 466 PRO 467 0.0001

PRO 467 LEU 468 0.0003

LEU 468 SER 469 -0.1082

SER 469 TYR 470 -0.0003

TYR 470 GLU 471 -0.0002

GLU 471 SER 472 0.0561

SER 472 PHE 473 0.0001

PHE 473 VAL 474 -0.0000

VAL 474 ARG 475 -0.0487

ARG 475 TYR 476 -0.0002

TYR 476 ILE 477 0.0004

ILE 477 LYS 478 -0.1565

LYS 478 ASP 479 -0.0001

ASP 479 LYS 480 0.0002

LYS 480 TYR 481 -0.0817

TYR 481 SER 482 -0.0002

SER 482 LYS 483 0.0000

LYS 483 VAL 484 0.0106

VAL 484 TYR 485 0.0002

TYR 485 GLU 486 -0.0003

GLU 486 ILE 487 0.1327

ILE 487 GLU 488 0.0003

GLU 488 LEU 489 -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: April 25th, 2023.

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

*** HYDROLASE 05-OCT-15 5E3X ***

CA strain for 240327160220988694

--- normal mode 27 ---

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

* HYDROLASE 05-OCT-15 5E3X *