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

* HYDROLASE 05-OCT-15 5E3X *

CA strain for 240327160220988694

--- normal mode 29 ---

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 0.0001

GLU 2 GLU 3 -0.0004

GLU 3 LEU 4 0.0748

LEU 4 LYS 5 -0.0001

LYS 5 SER 6 -0.0002

SER 6 TYR 7 -0.4026

TYR 7 TYR 8 0.0001

TYR 8 LYS 9 0.0001

LYS 9 ARG 10 -0.2184

ARG 10 VAL 11 0.0000

VAL 11 ALA 12 -0.0003

ALA 12 LYS 13 -0.1748

LYS 13 TYR 14 -0.0000

TYR 14 TYR 15 -0.0000

TYR 15 SER 16 -0.0831

SER 16 ALA 17 0.0003

ALA 17 ALA 18 -0.0000

ALA 18 ALA 19 -0.1534

ALA 19 LEU 20 -0.0001

LEU 20 LEU 21 -0.0002

LEU 21 TYR 22 -0.0835

TYR 22 TRP 23 0.0002

TRP 23 ASP 24 0.0000

ASP 24 MET 25 -0.0147

MET 25 GLN 26 -0.0001

GLN 26 THR 27 0.0003

THR 27 TYR 28 -0.1779

TYR 28 MET 29 -0.0003

MET 29 PRO 30 0.0002

PRO 30 LYS 31 0.2370

LYS 31 ASP 32 0.0001

ASP 32 ALA 33 -0.0001

ALA 33 GLY 34 0.0285

GLY 34 PRO 35 -0.0001

PRO 35 TYR 36 -0.0001

TYR 36 ARG 37 -0.2475

ARG 37 ALA 38 -0.0001

ALA 38 GLU 39 0.0001

GLU 39 VAL 40 -0.0410

VAL 40 LEU 41 0.0003

LEU 41 SER 42 -0.0002

SER 42 GLU 43 0.0748

GLU 43 ILE 44 0.0000

ILE 44 GLY 45 0.0002

GLY 45 THR 46 0.0277

THR 46 TYR 47 -0.0002

TYR 47 ALA 48 0.0004

ALA 48 PHE 49 -0.1900

PHE 49 LYS 50 -0.0000

LYS 50 GLN 51 -0.0003

GLN 51 ILE 52 -0.0310

ILE 52 THR 53 0.0001

THR 53 ASP 54 0.0001

ASP 54 ASP 55 0.0520

ASP 55 ALA 56 0.0002

ALA 56 LEU 57 0.0000

LEU 57 GLY 58 0.2203

GLY 58 LYS 59 -0.0000

LYS 59 LEU 60 0.0002

LEU 60 LEU 61 -0.0191

LEU 61 GLU 62 0.0002

GLU 62 THR 63 -0.0001

THR 63 ALA 64 0.0184

ALA 64 GLN 65 -0.0000

GLN 65 PRO 66 -0.0002

PRO 66 GLN 67 0.0130

GLN 67 SER 68 -0.0001

SER 68 GLU 69 0.0000

GLU 69 ILE 70 -0.3616

ILE 70 ASP 71 0.0001

ASP 71 GLU 72 -0.0003

GLU 72 LYS 73 -0.0525

LYS 73 LEU 74 -0.0003

LEU 74 VAL 75 -0.0001

VAL 75 TYR 76 -0.0239

TYR 76 VAL 77 0.0003

VAL 77 GLY 78 -0.0003

GLY 78 LYS 79 -0.0653

LYS 79 LYS 80 0.0003

LYS 80 GLU 81 0.0002

GLU 81 TYR 82 0.0694

TYR 82 TYR 83 0.0004

TYR 83 LYS 84 0.0003

LYS 84 TYR 85 -0.0768

TYR 85 LYS 86 0.0000

LYS 86 LYS 87 -0.0002

LYS 87 VAL 88 -0.0820

VAL 88 PRO 89 -0.0000

PRO 89 PRO 90 -0.0001

PRO 90 GLU 91 -0.0016

GLU 91 LEU 92 0.0004

LEU 92 PHE 93 -0.0001

PHE 93 GLN 94 -0.0406

GLN 94 GLU 95 -0.0002

GLU 95 ILE 96 -0.0001

ILE 96 MET 97 -0.1452

MET 97 ILE 98 0.0001

ILE 98 THR 99 -0.0000

THR 99 SER 100 0.0563

SER 100 THR 101 0.0004

THR 101 MET 102 -0.0001

MET 102 LEU 103 0.0480

LEU 103 GLU 104 0.0000

GLU 104 GLN 105 -0.0001

GLN 105 LYS 106 -0.0418

LYS 106 TRP 107 0.0001

TRP 107 GLU 108 -0.0002

GLU 108 ILE 109 -0.0158

ILE 109 ALA 110 -0.0000

ALA 110 LYS 111 -0.0002

LYS 111 PRO 112 -0.0016

PRO 112 ARG 113 0.0001

ARG 113 GLY 114 0.0001

GLY 114 ASP 115 0.0320

ASP 115 PHE 116 -0.0000

PHE 116 GLU 117 -0.0000

GLU 117 GLU 118 0.0127

GLU 118 VAL 119 -0.0002

VAL 119 ARG 120 0.0002

ARG 120 PRO 121 0.0234

PRO 121 LEU 122 0.0003

LEU 122 LEU 123 -0.0003

LEU 123 GLU 124 -0.0193

GLU 124 LYS 125 0.0003

LYS 125 ILE 126 0.0002

ILE 126 VAL 127 -0.1346

VAL 127 ASP 128 0.0000

ASP 128 LEU 129 -0.0001

LEU 129 SER 130 0.0368

SER 130 ARG 131 0.0000

ARG 131 LYS 132 -0.0003

LYS 132 TYR 133 0.0502

TYR 133 ALA 134 -0.0002

ALA 134 ASP 135 0.0003

ASP 135 ILE 136 -0.1924

ILE 136 LEU 137 0.0000

LEU 137 GLY 138 -0.0001

GLY 138 TYR 139 -0.4007

TYR 139 GLU 140 -0.0000

GLU 140 GLY 141 0.0002

GLY 141 GLU 142 0.3062

GLU 142 PRO 143 -0.0001

PRO 143 TYR 144 0.0001

TYR 144 ASN 145 -0.1044

ASN 145 ALA 146 -0.0001

ALA 146 LEU 147 -0.0004

LEU 147 LEU 148 -0.0050

LEU 148 ASP 149 -0.0004

ASP 149 LEU 150 -0.0000

LEU 150 TYR 151 -0.1386

TYR 151 GLU 152 -0.0002

GLU 152 PRO 153 0.0002

PRO 153 GLY 154 -0.2709

GLY 154 MET 155 -0.0003

MET 155 LYS 156 -0.0001

LYS 156 ALA 157 -0.0323

ALA 157 GLU 158 -0.0002

GLU 158 GLU 159 0.0002

GLU 159 VAL 160 0.0336

VAL 160 ASP 161 -0.0001

ASP 161 GLN 162 0.0000

GLN 162 ILE 163 -0.0045

ILE 163 PHE 164 0.0005

PHE 164 SER 165 -0.0002

SER 165 LYS 166 0.0224

LYS 166 VAL 167 -0.0000

VAL 167 ARG 168 0.0002

ARG 168 ASP 169 0.0131

ASP 169 PHE 170 -0.0001

PHE 170 ILE 171 0.0001

ILE 171 VAL 172 -0.0199

VAL 172 GLU 173 -0.0003

GLU 173 VAL 174 -0.0004

VAL 174 LEU 175 -0.0168

LEU 175 GLU 176 -0.0004

GLU 176 LYS 177 0.0003

LYS 177 ILE 178 0.1079

ILE 178 GLU 179 0.0000

GLU 179 ARG 180 0.0002

ARG 180 LEU 181 0.0396

LEU 181 PRO 182 -0.0001

PRO 182 LYS 183 0.0001

LYS 183 SER 184 -0.0643

SER 184 GLU 185 0.0002

GLU 185 ASP 186 -0.0003

ASP 186 PRO 187 0.1745

PRO 187 PHE 188 -0.0001

PHE 188 ASN 189 -0.0004

ASN 189 ARG 190 0.1146

ARG 190 GLU 191 -0.0001

GLU 191 ILE 192 0.0001

ILE 192 GLY 193 0.1119

GLY 193 VAL 194 0.0000

VAL 194 ASP 195 -0.0000

ASP 195 LYS 196 -0.0100

LYS 196 GLN 197 0.0000

GLN 197 LYS 198 -0.0000

LYS 198 GLU 199 -0.0995

GLU 199 PHE 200 0.0001

PHE 200 SER 201 0.0001

SER 201 ASN 202 0.0221

ASN 202 TRP 203 0.0001

TRP 203 LEU 204 -0.0000

LEU 204 LEU 205 -0.0088

LEU 205 HIS 206 -0.0003

HIS 206 TYR 207 0.0003

TYR 207 LEU 208 -0.0109

LEU 208 LYS 209 -0.0002

LYS 209 TYR 210 0.0000

TYR 210 ASP 211 -0.1465

ASP 211 PHE 212 0.0001

PHE 212 THR 213 -0.0004

THR 213 LYS 214 0.0258

LYS 214 GLY 215 -0.0002

GLY 215 ARG 216 -0.0000

ARG 216 LEU 217 0.1261

LEU 217 ASP 218 -0.0002

ASP 218 VAL 219 -0.0001

VAL 219 SER 220 0.0958

SER 220 ALA 221 -0.0001

ALA 221 HIS 222 0.0002

HIS 222 PRO 223 0.0316

PRO 223 PHE 224 0.0005

PHE 224 THR 225 -0.0002

THR 225 ASN 226 -0.1175

ASN 226 PRO 227 -0.0001

PRO 227 ILE 228 0.0001

ILE 228 GLY 229 -0.0122

GLY 229 LEU 230 -0.0001

LEU 230 ASN 231 -0.0000

ASN 231 ASP 232 0.0941

ASP 232 VAL 233 0.0001

VAL 233 ARG 234 -0.0000

ARG 234 ILE 235 0.0172

ILE 235 THR 236 -0.0001

THR 236 THR 237 -0.0002

THR 237 ARG 238 0.1211

ARG 238 TYR 239 -0.0001

TYR 239 ILE 240 0.0001

ILE 240 VAL 241 -0.1148

VAL 241 ASN 242 0.0000

ASN 242 ASP 243 -0.0004

ASP 243 ILE 244 -0.0944

ILE 244 ARG 245 0.0001

ARG 245 ASN 246 -0.0000

ASN 246 SER 247 -0.0970

SER 247 ILE 248 0.0000

ILE 248 TYR 249 -0.0002

TYR 249 SER 250 -0.3105

SER 250 THR 251 0.0003

THR 251 ILE 252 -0.0000

ILE 252 HIS 253 0.0143

HIS 253 GLU 254 -0.0003

GLU 254 PHE 255 -0.0000

PHE 255 GLY 256 0.1890

GLY 256 HIS 257 -0.0002

HIS 257 ALA 258 0.0001

ALA 258 LEU 259 -0.2015

LEU 259 TYR 260 -0.0000

TYR 260 ALA 261 -0.0000

ALA 261 LEU 262 0.1158

LEU 262 SER 263 -0.0000

SER 263 ILE 264 -0.0004

ILE 264 PRO 265 0.0062

PRO 265 THR 266 0.0001

THR 266 GLU 267 -0.0002

GLU 267 PHE 268 0.0323

PHE 268 TYR 269 0.0000

TYR 269 GLY 270 -0.0003

GLY 270 LEU 271 -0.1820

LEU 271 PRO 272 0.0000

PRO 272 ILE 273 0.0000

ILE 273 GLY 274 -0.2102

GLY 274 SER 275 -0.0000

SER 275 SER 276 -0.0004

SER 276 ALA 277 0.0008

ALA 277 SER 278 -0.0003

SER 278 TYR 279 0.0003

TYR 279 GLY 280 0.0283

GLY 280 PHE 281 -0.0002

PHE 281 ASP 282 -0.0002

ASP 282 GLU 283 0.0526

GLU 283 SER 284 -0.0003

SER 284 GLN 285 -0.0002

GLN 285 SER 286 0.0954

SER 286 ARG 287 -0.0004

ARG 287 PHE 288 0.0000

PHE 288 TRP 289 0.1304

TRP 289 GLU 290 -0.0001

GLU 290 ASN 291 0.0001

ASN 291 VAL 292 0.0558

VAL 292 VAL 293 0.0001

VAL 293 GLY 294 0.0003

GLY 294 ARG 295 -0.1126

ARG 295 SER 296 -0.0001

SER 296 LEU 297 0.0002

LEU 297 ALA 298 0.1915

ALA 298 PHE 299 0.0000

PHE 299 TRP 300 -0.0004

TRP 300 LYS 301 -0.0029

LYS 301 GLY 302 -0.0003

GLY 302 ILE 303 0.0004

ILE 303 TYR 304 0.0211

TYR 304 SER 305 0.0000

SER 305 LYS 306 -0.0004

LYS 306 PHE 307 0.0299

PHE 307 ILE 308 0.0001

ILE 308 GLU 309 0.0003

GLU 309 ILE 310 -0.0840

ILE 310 VAL 311 -0.0002

VAL 311 PRO 312 0.0001

PRO 312 GLU 313 0.0163

GLU 313 MET 314 0.0001

MET 314 ARG 315 -0.0000

ARG 315 GLY 316 -0.0322

GLY 316 TYR 317 0.0001

TYR 317 SER 318 0.0000

SER 318 VAL 319 -0.0840

VAL 319 GLU 320 -0.0000

GLU 320 GLU 321 0.0001

GLU 321 LEU 322 -0.0740

LEU 322 TRP 323 0.0001

TRP 323 ARG 324 -0.0000

ARG 324 ALA 325 0.0940

ALA 325 VAL 326 -0.0002

VAL 326 ASN 327 -0.0004

ASN 327 ARG 328 0.0614

ARG 328 VAL 329 0.0001

VAL 329 GLN 330 0.0002

GLN 330 ARG 331 -0.3184

ARG 331 SER 332 -0.0000

SER 332 PHE 333 0.0001

PHE 333 ILE 334 -0.1067

ILE 334 ARG 335 0.0002

ARG 335 THR 336 -0.0001

THR 336 GLU 337 0.0222

GLU 337 ALA 338 0.0005

ALA 338 ASP 339 -0.0003

ASP 339 GLU 340 -0.2758

GLU 340 VAL 341 -0.0000

VAL 341 THR 342 -0.0001

THR 342 TYR 343 -0.1095

TYR 343 ASN 344 -0.0001

ASN 344 LEU 345 0.0002

LEU 345 HIS 346 0.0750

HIS 346 ILE 347 -0.0003

ILE 347 ILE 348 -0.0001

ILE 348 ILE 349 -0.1065

ILE 349 ARG 350 0.0004

ARG 350 PHE 351 -0.0001

PHE 351 GLU 352 -0.0430

GLU 352 ILE 353 -0.0002

ILE 353 GLU 354 0.0000

GLU 354 ARG 355 0.1525

ARG 355 GLU 356 0.0001

GLU 356 LEU 357 -0.0000

LEU 357 ILE 358 0.0994

ILE 358 ASN 359 0.0000

ASN 359 GLY 360 0.0001

GLY 360 GLU 361 0.0329

GLU 361 LEU 362 0.0003

LEU 362 SER 363 -0.0003

SER 363 VAL 364 -0.0567

VAL 364 LYS 365 0.0001

LYS 365 ASP 366 0.0004

ASP 366 VAL 367 -0.0878

VAL 367 PRO 368 -0.0005

PRO 368 ASP 369 -0.0000

ASP 369 LYS 370 -0.0005

LYS 370 TRP 371 0.0002

TRP 371 ASN 372 -0.0000

ASN 372 GLU 373 0.0209

GLU 373 LEU 374 -0.0001

LEU 374 TYR 375 0.0001

TYR 375 LYS 376 0.0103

LYS 376 LYS 377 -0.0000

LYS 377 TYR 378 0.0002

TYR 378 LEU 379 0.0007

LEU 379 GLY 380 0.0002

GLY 380 LEU 381 -0.0001

LEU 381 ASP 382 -0.0778

ASP 382 VAL 383 0.0001

VAL 383 PRO 384 -0.0002

PRO 384 ASN 385 -0.0985

ASN 385 ASN 386 -0.0001

ASN 386 THR 387 -0.0001

THR 387 LEU 388 0.1231

LEU 388 GLY 389 0.0001

GLY 389 CYS 390 0.0006

CYS 390 MET 391 -0.0256

MET 391 GLN 392 0.0002

GLN 392 ASP 393 0.0003

ASP 393 PRO 394 0.0327

PRO 394 HIS 395 0.0001

HIS 395 TRP 396 -0.0004

TRP 396 PHE 397 0.0237

PHE 397 GLY 398 0.0006

GLY 398 GLY 399 -0.0003

GLY 399 ASN 400 0.0139

ASN 400 PHE 401 0.0003

PHE 401 GLY 402 -0.0003

GLY 402 TYR 403 -0.0734

TYR 403 PHE 404 -0.0000

PHE 404 PRO 405 0.0003

PRO 405 THR 406 -0.0926

THR 406 TYR 407 -0.0000

TYR 407 ALA 408 0.0002

ALA 408 LEU 409 -0.0680

LEU 409 GLY 410 0.0003

GLY 410 ASN 411 0.0002

ASN 411 LEU 412 0.0375

LEU 412 TYR 413 -0.0002

TYR 413 ALA 414 0.0002

ALA 414 ALA 415 -0.0119

ALA 415 GLN 416 0.0006

GLN 416 ILE 417 0.0000

ILE 417 PHE 418 0.0296

PHE 418 GLU 419 0.0002

GLU 419 LYS 420 -0.0000

LYS 420 LEU 421 0.1543

LEU 421 LYS 422 0.0000

LYS 422 GLU 423 0.0001

GLU 423 GLU 424 0.1003

GLU 424 ILE 425 0.0000

ILE 425 ASN 426 -0.0000

ASN 426 PHE 427 0.0259

PHE 427 GLU 428 0.0003

GLU 428 GLU 429 -0.0000

GLU 429 VAL 430 -0.3332

VAL 430 VAL 431 -0.0001

VAL 431 SER 432 -0.0001

SER 432 ALA 433 0.2170

ALA 433 GLY 434 -0.0001

GLY 434 ASN 435 -0.0001

ASN 435 PHE 436 -0.0849

PHE 436 GLU 437 0.0001

GLU 437 ILE 438 0.0001

ILE 438 ILE 439 0.0239

ILE 439 LYS 440 0.0003

LYS 440 ASN 441 -0.0000

ASN 441 PHE 442 0.2853

PHE 442 LEU 443 -0.0001

LEU 443 LYS 444 -0.0001

LYS 444 GLU 445 0.0403

GLU 445 LYS 446 -0.0001

LYS 446 ILE 447 0.0004

ILE 447 HIS 448 0.0837

HIS 448 SER 449 -0.0000

SER 449 LYS 450 -0.0001

LYS 450 GLY 451 -0.0114

GLY 451 LYS 452 0.0004

LYS 452 MET 453 0.0002

MET 453 TYR 454 0.1246

TYR 454 GLU 455 0.0003

GLU 455 PRO 456 0.0002

PRO 456 SER 457 0.1600

SER 457 ASP 458 -0.0002

ASP 458 LEU 459 0.0001

LEU 459 ILE 460 0.0888

ILE 460 LYS 461 0.0002

LYS 461 ILE 462 0.0001

ILE 462 VAL 463 0.0306

VAL 463 THR 464 0.0001

THR 464 GLY 465 -0.0003

GLY 465 LYS 466 -0.0827

LYS 466 PRO 467 -0.0002

PRO 467 LEU 468 0.0001

LEU 468 SER 469 -0.0700

SER 469 TYR 470 0.0002

TYR 470 GLU 471 -0.0003

GLU 471 SER 472 0.1778

SER 472 PHE 473 0.0002

PHE 473 VAL 474 -0.0000

VAL 474 ARG 475 0.0278

ARG 475 TYR 476 0.0000

TYR 476 ILE 477 -0.0002

ILE 477 LYS 478 -0.0886

LYS 478 ASP 479 0.0000

ASP 479 LYS 480 -0.0002

LYS 480 TYR 481 -0.0287

TYR 481 SER 482 -0.0003

SER 482 LYS 483 0.0002

LYS 483 VAL 484 0.1008

VAL 484 TYR 485 0.0000

TYR 485 GLU 486 0.0000

GLU 486 ILE 487 0.1582

ILE 487 GLU 488 -0.0002

GLU 488 LEU 489 0.0005

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 29 ---

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

* HYDROLASE 05-OCT-15 5E3X *