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

* 3NT1_ENZIMA_NEMO *

CA strain for 22030921275826620

--- normal mode 8 ---

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
ALA 33 ASN 34 -0.0001

ASN 34 PRO 35 -0.0002

PRO 35 CYS 36 0.0076

CYS 36 CYS 37 0.0001

CYS 37 SER 38 0.0003

SER 38 ASN 39 -0.0287

ASN 39 PRO 40 0.0001

PRO 40 CYS 41 0.0001

CYS 41 GLN 42 0.0389

GLN 42 ASN 43 -0.0001

ASN 43 ARG 44 -0.0000

ARG 44 GLY 45 0.0701

GLY 45 GLU 46 0.0002

GLU 46 CYS 47 -0.0001

CYS 47 MET 48 -0.0591

MET 48 SER 49 0.0001

SER 49 THR 50 0.0001

THR 50 GLY 51 -0.0920

GLY 51 PHE 52 -0.0002

PHE 52 ASP 53 -0.0001

ASP 53 GLN 54 0.0675

GLN 54 TYR 55 0.0001

TYR 55 LYS 56 0.0001

LYS 56 CYS 57 0.0405

CYS 57 ASP 58 -0.0000

ASP 58 CYS 59 -0.0000

CYS 59 THR 60 0.0442

THR 60 ARG 61 -0.0000

ARG 61 THR 62 -0.0003

THR 62 GLY 63 -0.0511

GLY 63 PHE 64 0.0000

PHE 64 TYR 65 -0.0002

TYR 65 GLY 66 0.0456

GLY 66 GLU 67 0.0003

GLU 67 ASN 68 0.0002

ASN 68 CYS 69 0.0116

CYS 69 THR 70 0.0000

THR 70 THR 71 -0.0003

THR 71 PRO 72 0.0268

PRO 72 GLU 73 0.0001

GLU 73 PHE 74 -0.0000

PHE 74 LEU 75 0.0118

LEU 75 THR 76 0.0000

THR 76 ARG 77 0.0002

ARG 77 ILE 78 0.0032

ILE 78 LYS 79 0.0002

LYS 79 LEU 80 0.0003

LEU 80 LEU 81 -0.0304

LEU 81 LEU 82 0.0001

LEU 82 LYS 83 0.0001

LYS 83 PRO 84 0.2049

PRO 84 THR 85 0.0002

THR 85 PRO 86 0.0001

PRO 86 ASN 87 0.0372

ASN 87 THR 88 -0.0001

THR 88 VAL 89 0.0001

VAL 89 HIS 90 0.0865

HIS 90 TYR 91 -0.0000

TYR 91 ILE 92 -0.0000

ILE 92 LEU 93 0.0334

LEU 93 THR 94 0.0003

THR 94 HIS 95 -0.0004

HIS 95 PHE 96 -0.0270

PHE 96 LYS 97 0.0002

LYS 97 GLY 98 0.0003

GLY 98 VAL 99 -0.0129

VAL 99 TRP 100 0.0001

TRP 100 ASN 101 -0.0004

ASN 101 ILE 102 -0.0059

ILE 102 VAL 103 -0.0001

VAL 103 ASN 104 -0.0003

ASN 104 ASN 105 -0.0168

ASN 105 ILE 105 -0.0002

ILE 105 PRO 106 -0.0003

PRO 106 PHE 107 0.0001

PHE 107 LEU 108 -0.0042

LEU 108 ARG 109 0.0000

ARG 109 SER 110 0.0004

SER 110 LEU 111 0.0042

LEU 111 ILE 112 0.0004

ILE 112 MET 113 0.0001

MET 113 LYS 114 0.0026

LYS 114 TYR 115 -0.0001

TYR 115 VAL 116 -0.0001

VAL 116 LEU 117 -0.0141

LEU 117 THR 118 0.0001

THR 118 SER 119 0.0002

SER 119 ARG 120 -0.0242

ARG 120 SER 121 -0.0001

SER 121 TYR 122 0.0000

TYR 122 LEU 123 0.0057

LEU 123 ILE 124 0.0000

ILE 124 ASP 125 0.0000

ASP 125 SER 126 -0.0448

SER 126 PRO 127 0.0001

PRO 127 PRO 128 -0.0005

PRO 128 THR 129 0.0211

THR 129 TYR 130 0.0002

TYR 130 ASN 131 0.0001

ASN 131 VAL 132 0.0249

VAL 132 HIS 133 0.0002

HIS 133 TYR 134 0.0001

TYR 134 GLY 135 -0.1037

GLY 135 TYR 136 -0.0000

TYR 136 LYS 137 -0.0003

LYS 137 SER 138 -0.1600

SER 138 TRP 139 0.0001

TRP 139 GLU 140 -0.0001

GLU 140 ALA 141 0.0354

ALA 141 PHE 142 0.0004

PHE 142 SER 143 0.0001

SER 143 ASN 144 -0.0021

ASN 144 LEU 145 -0.0003

LEU 145 SER 146 0.0001

SER 146 TYR 147 -0.0558

TYR 147 TYR 148 0.0001

TYR 148 THR 149 -0.0000

THR 149 ARG 150 -0.0502

ARG 150 ALA 151 0.0005

ALA 151 LEU 152 0.0001

LEU 152 PRO 153 0.0331

PRO 153 PRO 154 0.0001

PRO 154 VAL 155 -0.0002

VAL 155 ALA 156 0.0580

ALA 156 ASP 157 -0.0001

ASP 157 ASP 158 0.0002

ASP 158 CYS 159 0.0602

CYS 159 PRO 160 0.0002

PRO 160 THR 161 -0.0002

THR 161 PRO 162 0.0047

PRO 162 MET 163 -0.0002

MET 163 GLY 164 0.0001

GLY 164 VAL 165 -0.0454

VAL 165 LYS 166 0.0002

LYS 166 GLY 167 -0.0003

GLY 167 ASN 168 0.0083

ASN 168 LYS 169 -0.0004

LYS 169 GLU 170 -0.0001

GLU 170 LEU 171 -0.0160

LEU 171 PRO 172 -0.0004

PRO 172 ASP 173 0.0002

ASP 173 SER 174 -0.0160

SER 174 LYS 175 -0.0001

LYS 175 GLU 176 0.0002

GLU 176 VAL 177 0.0058

VAL 177 LEU 178 -0.0000

LEU 178 GLU 179 0.0003

GLU 179 LYS 180 -0.0002

LYS 180 VAL 181 -0.0000

VAL 181 LEU 182 0.0000

LEU 182 LEU 183 0.0074

LEU 183 ARG 184 -0.0002

ARG 184 ARG 185 0.0003

ARG 185 GLU 186 -0.0340

GLU 186 PHE 187 -0.0002

PHE 187 ILE 188 0.0001

ILE 188 PRO 189 -0.0465

PRO 189 ASP 190 0.0000

ASP 190 PRO 191 -0.0001

PRO 191 GLN 192 -0.0844

GLN 192 GLY 193 0.0003

GLY 193 SER 194 -0.0002

SER 194 ASN 195 0.0810

ASN 195 MET 196 -0.0005

MET 196 MET 197 -0.0002

MET 197 PHE 198 0.0032

PHE 198 ALA 199 -0.0002

ALA 199 PHE 200 0.0003

PHE 200 PHE 201 -0.0032

PHE 201 ALA 202 -0.0002

ALA 202 GLN 203 -0.0003

GLN 203 HIS 204 0.0329

HIS 204 PHE 205 -0.0001

PHE 205 THR 206 0.0002

THR 206 HIS 207 0.0083

HIS 207 GLN 208 0.0003

GLN 208 PHE 209 0.0002

PHE 209 PHE 210 0.0277

PHE 210 LYS 211 -0.0001

LYS 211 THR 212 0.0004

THR 212 ASP 213 -0.0006

ASP 213 HIS 214 -0.0001

HIS 214 LYS 215 0.0003

LYS 215 ARG 216 -0.0077

ARG 216 GLY 217 0.0002

GLY 217 PRO 218 0.0000

PRO 218 GLY 219 0.0185

GLY 219 PHE 220 -0.0000

PHE 220 THR 221 0.0004

THR 221 ARG 222 -0.1156

ARG 222 GLY 223 -0.0003

GLY 223 LEU 224 0.0003

LEU 224 GLY 225 0.0527

GLY 225 HIS 226 -0.0003

HIS 226 GLY 227 -0.0003

GLY 227 VAL 228 0.0070

VAL 228 ASP 229 -0.0003

ASP 229 LEU 230 0.0002

LEU 230 ASN 231 -0.0003

ASN 231 HIS 232 0.0001

HIS 232 ILE 233 -0.0005

ILE 233 TYR 234 0.0185

TYR 234 GLY 235 0.0004

GLY 235 GLU 236 -0.0002

GLU 236 THR 237 -0.0386

THR 237 LEU 238 0.0000

LEU 238 ASP 239 -0.0002

ASP 239 ARG 240 0.0344

ARG 240 GLN 241 -0.0001

GLN 241 HIS 242 -0.0002

HIS 242 LYS 243 -0.0019

LYS 243 LEU 244 -0.0005

LEU 244 ARG 245 0.0000

ARG 245 LEU 246 -0.0221

LEU 246 PHE 247 -0.0002

PHE 247 LYS 248 0.0002

LYS 248 ASP 249 0.0049

ASP 249 GLY 250 0.0001

GLY 250 LYS 251 0.0004

LYS 251 LEU 252 0.0069

LEU 252 LYS 253 0.0001

LYS 253 TYR 254 0.0002

TYR 254 GLN 255 0.0130

GLN 255 VAL 256 0.0002

VAL 256 ILE 257 0.0001

ILE 257 GLY 258 -0.0033

GLY 258 GLY 259 0.0001

GLY 259 GLU 260 0.0001

GLU 260 VAL 261 -0.0139

VAL 261 TYR 262 0.0000

TYR 262 PRO 263 -0.0000

PRO 263 PRO 264 0.0272

PRO 264 THR 265 0.0003

THR 265 VAL 266 -0.0000

VAL 266 LYS 267 -0.0128

LYS 267 ASP 268 -0.0002

ASP 268 THR 269 0.0001

THR 269 GLN 270 -0.0030

GLN 270 VAL 271 0.0002

VAL 271 GLU 272 0.0002

GLU 272 MET 273 0.0563

MET 273 ILE 274 0.0000

ILE 274 TYR 275 0.0004

TYR 275 PRO 276 -0.0280

PRO 276 PRO 277 -0.0001

PRO 277 HIS 278 -0.0002

HIS 278 ILE 279 0.0232

ILE 279 PRO 280 -0.0001

PRO 280 GLU 281 0.0003

GLU 281 ASN 282 0.0277

ASN 282 LEU 283 -0.0002

LEU 283 GLN 284 -0.0000

GLN 284 PHE 285 -0.0041

PHE 285 ALA 286 -0.0000

ALA 286 VAL 287 0.0002

VAL 287 GLY 288 -0.0919

GLY 288 GLN 289 0.0005

GLN 289 GLU 290 -0.0002

GLU 290 VAL 291 0.0338

VAL 291 PHE 292 0.0001

PHE 292 GLY 293 -0.0001

GLY 293 LEU 294 0.0430

LEU 294 VAL 295 0.0005

VAL 295 PRO 296 -0.0002

PRO 296 GLY 297 -0.0227

GLY 297 LEU 298 -0.0003

LEU 298 MET 299 -0.0003

MET 299 MET 300 0.0048

MET 300 TYR 301 -0.0000

TYR 301 ALA 302 0.0001

ALA 302 THR 303 -0.0383

THR 303 ILE 304 0.0002

ILE 304 TRP 305 0.0001

TRP 305 LEU 306 0.0240

LEU 306 ARG 307 -0.0000

ARG 307 GLU 308 -0.0002

GLU 308 HIS 309 0.0050

HIS 309 ASN 310 0.0002

ASN 310 ARG 311 0.0001

ARG 311 VAL 312 0.0058

VAL 312 CYS 313 0.0000

CYS 313 ASP 314 -0.0002

ASP 314 ILE 315 0.0118

ILE 315 LEU 316 0.0001

LEU 316 LYS 317 -0.0002

LYS 317 GLN 318 0.0013

GLN 318 GLU 319 -0.0002

GLU 319 GLU 319 0.0000

GLU 319 HIS 320 -0.0001

HIS 320 PRO 321 0.0036

PRO 321 GLU 322 -0.0000

GLU 322 TRP 323 0.0002

TRP 323 GLY 324 0.0133

GLY 324 ASP 325 0.0003

ASP 325 GLU 326 -0.0003

GLU 326 GLN 327 0.0021

GLN 327 LEU 328 -0.0000

LEU 328 PHE 329 0.0002

PHE 329 GLN 330 -0.0018

GLN 330 THR 331 0.0001

THR 331 SER 332 -0.0001

SER 332 ARG 333 -0.0164

ARG 333 LEU 334 -0.0006

LEU 334 ILE 335 -0.0000

ILE 335 LEU 336 -0.0037

LEU 336 ILE 337 -0.0001

ILE 337 GLY 338 0.0003

GLY 338 GLU 339 -0.0143

GLU 339 THR 340 0.0002

THR 340 ILE 341 -0.0002

ILE 341 LYS 342 0.0050

LYS 342 ILE 343 -0.0001

ILE 343 VAL 344 0.0002

VAL 344 ILE 345 0.0057

ILE 345 GLU 346 -0.0001

GLU 346 ASP 347 0.0001

ASP 347 TYR 348 -0.0077

TYR 348 VAL 349 0.0003

VAL 349 GLN 350 0.0003

GLN 350 HIS 351 -0.0542

HIS 351 LEU 352 -0.0001

LEU 352 SER 353 0.0001

SER 353 GLY 354 -0.0919

GLY 354 TYR 355 0.0001

TYR 355 HIS 356 0.0001

HIS 356 PHE 357 -0.0295

PHE 357 LYS 358 0.0001

LYS 358 LEU 359 0.0002

LEU 359 LYS 360 -0.0250

LYS 360 PHE 361 -0.0001

PHE 361 ASP 362 0.0001

ASP 362 PRO 363 0.0038

PRO 363 GLU 364 -0.0003

GLU 364 LEU 365 -0.0005

LEU 365 LEU 366 0.0222

LEU 366 PHE 367 0.0004

PHE 367 ASN 368 0.0000

ASN 368 GLN 369 0.0041

GLN 369 GLN 370 0.0003

GLN 370 PHE 371 -0.0000

PHE 371 GLN 372 0.0490

GLN 372 TYR 373 0.0004

TYR 373 GLN 374 0.0003

GLN 374 ASN 375 0.0636

ASN 375 ARG 376 -0.0000

ARG 376 ILE 377 0.0002

ILE 377 ALA 378 -0.0373

ALA 378 SER 379 0.0003

SER 379 GLU 380 0.0001

GLU 380 PHE 381 -0.0182

PHE 381 ASN 382 -0.0002

ASN 382 THR 383 0.0003

THR 383 LEU 384 -0.0098

LEU 384 TYR 385 0.0003

TYR 385 HIS 386 -0.0004

HIS 386 TRP 387 -0.0355

TRP 387 HIS 388 0.0003

HIS 388 PRO 389 0.0001

PRO 389 LEU 390 0.0015

LEU 390 LEU 391 -0.0003

LEU 391 PRO 392 0.0001

PRO 392 ASP 393 -0.0290

ASP 393 THR 394 -0.0000

THR 394 PHE 395 0.0000

PHE 395 ASN 396 -0.0181

ASN 396 ILE 397 -0.0002

ILE 397 GLU 398 -0.0003

GLU 398 ASP 399 0.0040

ASP 399 GLN 400 0.0000

GLN 400 GLU 401 -0.0001

GLU 401 TYR 402 -0.0135

TYR 402 SER 403 0.0002

SER 403 PHE 404 0.0000

PHE 404 LYS 405 0.0295

LYS 405 GLN 406 0.0004

GLN 406 PHE 407 0.0001

PHE 407 LEU 408 0.0204

LEU 408 TYR 409 -0.0001

TYR 409 ASN 410 -0.0003

ASN 410 ASN 411 0.0199

ASN 411 SER 412 0.0001

SER 412 ILE 413 0.0001

ILE 413 LEU 414 0.0089

LEU 414 LEU 415 -0.0002

LEU 415 GLU 416 0.0000

GLU 416 HIS 417 0.0302

HIS 417 GLY 418 0.0001

GLY 418 LEU 419 0.0001

LEU 419 THR 420 0.0019

THR 420 GLN 421 -0.0002

GLN 421 PHE 422 0.0002

PHE 422 VAL 423 0.0150

VAL 423 GLU 424 -0.0000

GLU 424 SER 425 0.0001

SER 425 PHE 426 0.0101

PHE 426 THR 427 0.0002

THR 427 ARG 428 0.0002

ARG 428 GLN 429 -0.0375

GLN 429 ILE 430 0.0002

ILE 430 ALA 431 -0.0005

ALA 431 GLY 432 0.0356

GLY 432 ARG 433 0.0002

ARG 433 ARG 433 0.0000

ARG 433 VAL 434 -0.0003

VAL 434 ALA 435 0.0270

ALA 435 GLY 436 -0.0000

GLY 436 GLY 437 -0.0002

GLY 437 ARG 438 -0.0262

ARG 438 ASN 439 0.0000

ASN 439 VAL 440 -0.0001

VAL 440 PRO 441 -0.0163

PRO 441 ILE 442 -0.0001

ILE 442 ALA 443 0.0002

ALA 443 VAL 444 -0.0420

VAL 444 GLN 445 -0.0004

GLN 445 ALA 446 -0.0002

ALA 446 VAL 447 0.0773

VAL 447 ALA 448 -0.0000

ALA 448 LYS 449 -0.0001

LYS 449 ALA 450 0.0196

ALA 450 SER 451 -0.0001

SER 451 ILE 452 -0.0002

ILE 452 ASP 453 0.0100

ASP 453 GLN 454 -0.0001

GLN 454 SER 455 -0.0002

SER 455 ARG 456 0.0058

ARG 456 GLU 457 0.0001

GLU 457 MET 458 0.0003

MET 458 LYS 459 -0.0758

LYS 459 TYR 460 0.0003

TYR 460 GLN 461 -0.0002

GLN 461 SER 462 0.0058

SER 462 LEU 463 -0.0000

LEU 463 ASN 464 0.0002

ASN 464 GLU 465 0.0020

GLU 465 TYR 466 0.0002

TYR 466 ARG 467 -0.0004

ARG 467 LYS 468 0.0726

LYS 468 ARG 469 -0.0002

ARG 469 PHE 470 0.0000

PHE 470 SER 471 -0.0737

SER 471 LEU 472 0.0000

LEU 472 LYS 473 0.0002

LYS 473 PRO 474 -0.0258

PRO 474 TYR 475 -0.0001

TYR 475 THR 476 -0.0002

THR 476 SER 477 -0.0370

SER 477 PHE 478 -0.0001

PHE 478 GLU 479 -0.0001

GLU 479 GLU 480 -0.0194

GLU 480 LEU 481 -0.0001

LEU 481 THR 482 0.0002

THR 482 GLY 483 0.0031

GLY 483 GLU 484 -0.0005

GLU 484 LYS 485 0.0000

LYS 485 GLU 486 0.0042

GLU 486 MET 487 0.0002

MET 487 ALA 488 -0.0000

ALA 488 ALA 489 -0.0011

ALA 489 GLU 490 -0.0004

GLU 490 LEU 491 -0.0004

LEU 491 LYS 492 0.0075

LYS 492 ALA 493 -0.0001

ALA 493 LEU 494 0.0001

LEU 494 TYR 495 -0.0040

TYR 495 SER 496 -0.0003

SER 496 ASP 497 0.0002

ASP 497 ILE 498 -0.0182

ILE 498 ASP 499 0.0003

ASP 499 VAL 500 -0.0002

VAL 500 MET 501 0.0188

MET 501 GLU 502 0.0002

GLU 502 LEU 503 0.0000

LEU 503 TYR 504 -0.0098

TYR 504 PRO 505 -0.0002

PRO 505 ALA 506 -0.0002

ALA 506 LEU 507 -0.0004

LEU 507 LEU 508 0.0000

LEU 508 VAL 509 -0.0002

VAL 509 GLU 510 -0.0210

GLU 510 LYS 511 0.0001

LYS 511 PRO 512 -0.0001

PRO 512 ARG 513 -0.0505

ARG 513 PRO 514 -0.0002

PRO 514 ASP 515 -0.0002

ASP 515 ALA 516 -0.1106

ALA 516 ILE 517 0.0003

ILE 517 PHE 518 -0.0003

PHE 518 GLY 519 0.1280

GLY 519 GLU 520 -0.0003

GLU 520 THR 521 0.0000

THR 521 MET 522 0.0156

MET 522 VAL 523 -0.0001

VAL 523 GLU 524 -0.0001

GLU 524 LEU 525 -0.0199

LEU 525 GLY 526 0.0003

GLY 526 ALA 527 0.0003

ALA 527 PRO 528 0.0050

PRO 528 PHE 529 0.0003

PHE 529 SER 530 -0.0004

SER 530 LEU 531 -0.0062

LEU 531 LYS 532 -0.0001

LYS 532 GLY 533 0.0004

GLY 533 LEU 534 0.0218

LEU 534 MET 535 -0.0003

MET 535 GLY 536 -0.0003

GLY 536 ASN 537 -0.0245

ASN 537 PRO 538 -0.0000

PRO 538 ILE 539 -0.0001

ILE 539 CYS 540 -0.0127

CYS 540 SER 541 0.0000

SER 541 PRO 542 -0.0001

PRO 542 GLN 543 -0.0287

GLN 543 TYR 544 -0.0001

TYR 544 TRP 545 -0.0001

TRP 545 LYS 546 0.0081

LYS 546 PRO 547 -0.0001

PRO 547 SER 548 0.0003

SER 548 THR 549 0.0087

THR 549 PHE 550 -0.0001

PHE 550 GLY 551 -0.0002

GLY 551 GLY 552 -0.0072

GLY 552 GLU 553 -0.0001

GLU 553 VAL 554 0.0001

VAL 554 GLY 555 -0.0070

GLY 555 PHE 556 -0.0001

PHE 556 LYS 557 0.0002

LYS 557 ILE 558 -0.0088

ILE 558 ILE 559 -0.0000

ILE 559 ASN 560 -0.0001

ASN 560 THR 561 0.0014

THR 561 ALA 562 -0.0001

ALA 562 SER 563 -0.0002

SER 563 ILE 564 -0.0421

ILE 564 GLN 565 0.0003

GLN 565 SER 566 0.0001

SER 566 LEU 567 -0.0123

LEU 567 ILE 568 -0.0002

ILE 568 CYS 569 0.0002

CYS 569 ASN 570 -0.0081

ASN 570 ASN 571 0.0000

ASN 571 VAL 572 0.0002

VAL 572 LYS 573 -0.0243

LYS 573 GLY 574 0.0001

GLY 574 CYS 575 -0.0002

CYS 575 PRO 576 0.0038

PRO 576 PHE 577 0.0000

PHE 577 THR 578 0.0001

THR 578 SER 579 0.0681

SER 579 PHE 580 0.0002

PHE 580 ASN 581 -0.0001

ASN 581 ASN 581 0.0082

ASN 581 VAL 582 -0.0047

VAL 582 GLN 583 -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.

*** 3NT1_ENZIMA_NEMO ***

CA strain for 22030921275826620

--- normal mode 8 ---

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

* 3NT1_ENZIMA_NEMO *