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

* itasser_mtg2_model4 *

CA strain for 2407102126523076348

--- normal mode 24 ---

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 ALA 2 -0.0001

ALA 2 GLU 3 -0.0000

GLU 3 GLU 4 -0.0003

GLU 4 LEU 5 -0.1552

LEU 5 LEU 6 0.0002

LEU 6 LEU 7 -0.0003

LEU 7 GLU 8 0.0002

GLU 8 ARG 9 -0.4415

ARG 9 CYS 10 0.0001

CYS 10 ASP 11 -0.0003

ASP 11 LEU 12 0.0001

LEU 12 GLU 13 -0.1921

GLU 13 ILE 14 0.0001

ILE 14 GLN 15 0.0001

GLN 15 ALA 16 -0.0001

ALA 16 ASN 17 -0.0022

ASN 17 GLY 18 -0.0002

GLY 18 ARG 19 0.0002

ARG 19 ASP 20 0.0001

ASP 20 HIS 21 0.0376

HIS 21 HIS 22 -0.0001

HIS 22 THR 23 0.0001

THR 23 ALA 24 -0.0001

ALA 24 ASP 25 -0.0121

ASP 25 LEU 26 -0.0001

LEU 26 CYS 27 -0.0001

CYS 27 GLN 28 0.0000

GLN 28 GLU 29 0.0023

GLU 29 LYS 30 0.0000

LYS 30 LEU 31 0.0001

LEU 31 VAL 32 -0.0001

VAL 32 LEU 33 -0.0063

LEU 33 ARG 34 -0.0001

ARG 34 ARG 35 0.0002

ARG 35 GLY 36 -0.0001

GLY 36 GLN 37 0.2822

GLN 37 ARG 38 0.0001

ARG 38 PHE 39 -0.0002

PHE 39 ARG 40 0.0002

ARG 40 LEU 41 -0.1230

LEU 41 THR 42 -0.0000

THR 42 LEU 43 0.0001

LEU 43 TYR 44 -0.0004

TYR 44 PHE 45 -0.0460

PHE 45 GLU 46 -0.0001

GLU 46 GLY 47 -0.0002

GLY 47 ARG 48 0.0002

ARG 48 GLY 49 0.2193

GLY 49 TYR 50 -0.0001

TYR 50 GLU 51 -0.0001

GLU 51 ALA 52 0.0002

ALA 52 SER 53 0.4235

SER 53 VAL 54 -0.0001

VAL 54 ASP 55 -0.0001

ASP 55 SER 56 0.0001

SER 56 LEU 57 0.0526

LEU 57 THR 58 0.0000

THR 58 PHE 59 -0.0002

PHE 59 GLY 60 -0.0002

GLY 60 ALA 61 0.0304

ALA 61 VAL 62 0.0003

VAL 62 THR 63 -0.0001

THR 63 GLY 64 0.0001

GLY 64 PRO 65 -0.1460

PRO 65 ASP 66 -0.0001

ASP 66 PRO 67 -0.0001

PRO 67 SER 68 -0.0001

SER 68 GLU 69 0.2259

GLU 69 GLU 70 0.0000

GLU 70 ALA 71 -0.0001

ALA 71 GLY 72 -0.0003

GLY 72 THR 73 -0.1426

THR 73 LYS 74 -0.0002

LYS 74 ALA 75 0.0000

ALA 75 ARG 76 0.0000

ARG 76 PHE 77 0.2274

PHE 77 SER 78 0.0003

SER 78 LEU 79 0.0004

LEU 79 SER 80 -0.0003

SER 80 ASP 81 0.1871

ASP 81 ASN 82 0.0003

ASN 82 VAL 83 -0.0004

VAL 83 GLU 84 -0.0001

GLU 84 GLU 85 -0.0296

GLU 85 GLY 86 -0.0003

GLY 86 SER 87 -0.0000

SER 87 TRP 88 0.0003

TRP 88 SER 89 0.0562

SER 89 ALA 90 0.0002

ALA 90 SER 91 -0.0002

SER 91 VAL 92 0.0005

VAL 92 LEU 93 -0.0392

LEU 93 ASP 94 0.0000

ASP 94 GLN 95 -0.0001

GLN 95 GLN 96 0.0004

GLN 96 ASP 97 -0.0658

ASP 97 ASN 98 -0.0001

ASN 98 VAL 99 0.0005

VAL 99 LEU 100 0.0001

LEU 100 SER 101 0.1605

SER 101 LEU 102 -0.0003

LEU 102 GLN 103 0.0003

GLN 103 LEU 104 0.0000

LEU 104 CYS 105 0.1416

CYS 105 THR 106 0.0002

THR 106 PRO 107 -0.0003

PRO 107 ALA 108 -0.0001

ALA 108 ASN 109 0.1046

ASN 109 ALA 110 -0.0004

ALA 110 PRO 111 0.0003

PRO 111 ILE 112 0.0000

ILE 112 GLY 113 -0.0930

GLY 113 LEU 114 -0.0002

LEU 114 TYR 115 0.0000

TYR 115 ARG 116 -0.0001

ARG 116 LEU 117 0.1077

LEU 117 SER 118 0.0002

SER 118 LEU 119 0.0001

LEU 119 GLU 120 0.0000

GLU 120 ALA 121 -0.0833

ALA 121 SER 122 -0.0002

SER 122 THR 123 0.0002

THR 123 GLY 124 -0.0002

GLY 124 TYR 125 0.4132

TYR 125 GLN 126 -0.0002

GLN 126 GLY 127 -0.0001

GLY 127 SER 128 -0.0000

SER 128 SER 129 -0.8271

SER 129 PHE 130 0.0004

PHE 130 VAL 131 -0.0002

VAL 131 LEU 132 0.0004

LEU 132 GLY 133 -0.1626

GLY 133 HIS 134 0.0000

HIS 134 PHE 135 -0.0002

PHE 135 ILE 136 -0.0002

ILE 136 LEU 137 -0.1389

LEU 137 LEU 138 -0.0001

LEU 138 TYR 139 0.0000

TYR 139 ASN 140 0.0005

ASN 140 ALA 141 -0.1534

ALA 141 TRP 142 -0.0000

TRP 142 CYS 143 -0.0002

CYS 143 PRO 144 -0.0005

PRO 144 ALA 145 -0.0284

ALA 145 ASP 146 0.0001

ASP 146 ASP 147 -0.0000

ASP 147 VAL 148 -0.0001

VAL 148 TYR 149 0.0908

TYR 149 LEU 150 0.0000

LEU 150 ASP 151 -0.0000

ASP 151 SER 152 -0.0001

SER 152 GLU 153 0.0217

GLU 153 GLU 154 0.0002

GLU 154 GLU 155 0.0001

GLU 155 ARG 156 -0.0001

ARG 156 ARG 157 -0.0026

ARG 157 GLU 158 0.0002

GLU 158 TYR 159 -0.0002

TYR 159 VAL 160 0.0002

VAL 160 LEU 161 -0.0037

LEU 161 THR 162 -0.0003

THR 162 GLN 163 -0.0001

GLN 163 GLN 164 0.0000

GLN 164 GLY 165 0.0170

GLY 165 PHE 166 0.0002

PHE 166 ILE 167 0.0002

ILE 167 TYR 168 -0.0002

TYR 168 GLN 169 -0.0384

GLN 169 GLY 170 0.0002

GLY 170 SER 171 -0.0003

SER 171 VAL 172 -0.0000

VAL 172 LYS 173 -0.0403

LYS 173 PHE 174 0.0002

PHE 174 ILE 175 -0.0001

ILE 175 LYS 176 0.0004

LYS 176 SER 177 0.0454

SER 177 VAL 178 0.0003

VAL 178 PRO 179 -0.0002

PRO 179 TRP 180 0.0001

TRP 180 ASN 181 0.0480

ASN 181 PHE 182 -0.0002

PHE 182 GLY 183 -0.0000

GLY 183 GLN 184 0.0000

GLN 184 PHE 185 0.0183

PHE 185 GLU 186 0.0000

GLU 186 ASP 187 0.0002

ASP 187 GLY 188 -0.0001

GLY 188 ILE 189 -0.0326

ILE 189 LEU 190 -0.0001

LEU 190 ASP 191 -0.0001

ASP 191 THR 192 -0.0001

THR 192 CYS 193 0.0218

CYS 193 LEU 194 -0.0004

LEU 194 MET 195 -0.0002

MET 195 LEU 196 -0.0003

LEU 196 LEU 197 0.0881

LEU 197 ASP 198 0.0003

ASP 198 MET 199 0.0002

MET 199 ASN 200 -0.0000

ASN 200 PRO 201 -0.1247

PRO 201 LYS 202 0.0001

LYS 202 PHE 203 0.0001

PHE 203 LEU 204 0.0001

LEU 204 LYS 205 -0.0183

LYS 205 ASN 206 0.0002

ASN 206 ARG 207 0.0000

ARG 207 SER 208 0.0004

SER 208 ARG 209 -0.1093

ARG 209 ASP 210 -0.0001

ASP 210 CYS 211 -0.0000

CYS 211 SER 212 0.0001

SER 212 ARG 213 -0.1820

ARG 213 ARG 214 0.0001

ARG 214 SER 215 0.0003

SER 215 SER 216 -0.0003

SER 216 PRO 217 -0.1698

PRO 217 ILE 218 0.0002

ILE 218 TYR 219 0.0004

TYR 219 VAL 220 0.0004

VAL 220 GLY 221 0.0152

GLY 221 ARG 222 -0.0000

ARG 222 VAL 223 0.0000

VAL 223 VAL 224 0.0003

VAL 224 SER 225 0.0531

SER 225 ALA 226 -0.0000

ALA 226 MET 227 -0.0002

MET 227 VAL 228 0.0000

VAL 228 ASN 229 0.0105

ASN 229 CYS 230 0.0001

CYS 230 ASN 231 -0.0003

ASN 231 ASP 232 -0.0002

ASP 232 ASP 233 -0.1108

ASP 233 GLN 234 -0.0002

GLN 234 GLY 235 0.0000

GLY 235 VAL 236 0.0004

VAL 236 LEU 237 0.2420

LEU 237 LEU 238 -0.0002

LEU 238 GLY 239 -0.0001

GLY 239 ARG 240 -0.0002

ARG 240 TRP 241 -0.2309

TRP 241 ASP 242 0.0001

ASP 242 ASN 243 0.0000

ASN 243 ASN 244 -0.0001

ASN 244 TYR 245 -0.0966

TYR 245 GLY 246 -0.0003

GLY 246 ASP 247 0.0001

ASP 247 GLY 248 -0.0001

GLY 248 ILE 249 -0.1030

ILE 249 SER 250 -0.0000

SER 250 PRO 251 -0.0001

PRO 251 MET 252 0.0001

MET 252 ALA 253 -0.0112

ALA 253 TRP 254 0.0002

TRP 254 ILE 255 0.0000

ILE 255 GLY 256 -0.0002

GLY 256 SER 257 0.0514

SER 257 VAL 258 -0.0002

VAL 258 ASP 259 -0.0001

ASP 259 ILE 260 0.0002

ILE 260 LEU 261 0.1019

LEU 261 ARG 262 -0.0001

ARG 262 ARG 263 -0.0000

ARG 263 TRP 264 -0.0004

TRP 264 LYS 265 -0.0532

LYS 265 GLU 266 -0.0000

GLU 266 HIS 267 -0.0003

HIS 267 GLY 268 -0.0001

GLY 268 CYS 269 0.0135

CYS 269 GLN 270 -0.0002

GLN 270 GLN 271 0.0003

GLN 271 VAL 272 -0.0001

VAL 272 LYS 273 0.1753

LYS 273 TYR 274 0.0002

TYR 274 GLY 275 0.0001

GLY 275 GLN 276 -0.0001

GLN 276 CYS 277 -0.1121

CYS 277 TRP 278 0.0002

TRP 278 VAL 279 0.0005

VAL 279 PHE 280 0.0001

PHE 280 ALA 281 0.0041

ALA 281 ALA 282 0.0000

ALA 282 VAL 283 0.0001

VAL 283 ALA 284 -0.0000

ALA 284 CYS 285 0.0065

CYS 285 THR 286 0.0002

THR 286 VAL 287 0.0000

VAL 287 LEU 288 -0.0001

LEU 288 ARG 289 0.0278

ARG 289 CYS 290 -0.0000

CYS 290 LEU 291 0.0002

LEU 291 GLY 292 -0.0000

GLY 292 ILE 293 0.0203

ILE 293 PRO 294 -0.0002

PRO 294 THR 295 -0.0002

THR 295 ARG 296 -0.0001

ARG 296 VAL 297 -0.0998

VAL 297 VAL 298 0.0002

VAL 298 THR 299 -0.0002

THR 299 ASN 300 0.0000

ASN 300 TYR 301 0.0598

TYR 301 ASN 302 0.0003

ASN 302 SER 303 -0.0003

SER 303 ALA 304 0.0000

ALA 304 HIS 305 0.0746

HIS 305 ASP 306 -0.0001

ASP 306 GLN 307 0.0002

GLN 307 ASN 308 -0.0002

ASN 308 SER 309 -0.0819

SER 309 ASN 310 -0.0000

ASN 310 LEU 311 -0.0001

LEU 311 LEU 312 -0.0000

LEU 312 ILE 313 -0.0060

ILE 313 GLU 314 -0.0000

GLU 314 TYR 315 -0.0003

TYR 315 PHE 316 0.0002

PHE 316 ARG 317 -0.0482

ARG 317 ASN 318 0.0001

ASN 318 GLU 319 -0.0001

GLU 319 PHE 320 0.0002

PHE 320 GLY 321 0.0382

GLY 321 GLU 322 0.0001

GLU 322 LEU 323 -0.0001

LEU 323 GLU 324 0.0000

GLU 324 SER 325 0.0615

SER 325 ASN 326 -0.0000

ASN 326 LYS 327 0.0003

LYS 327 SER 328 0.0001

SER 328 GLU 329 0.0240

GLU 329 MET 330 -0.0002

MET 330 ILE 331 0.0001

ILE 331 TRP 332 -0.0001

TRP 332 ASN 333 0.2399

ASN 333 PHE 334 0.0000

PHE 334 HIS 335 -0.0000

HIS 335 CYS 336 0.0001

CYS 336 TRP 337 -0.0065

TRP 337 VAL 338 0.0002

VAL 338 GLU 339 0.0001

GLU 339 SER 340 -0.0001

SER 340 TRP 341 -0.0300

TRP 341 MET 342 0.0001

MET 342 THR 343 -0.0004

THR 343 ARG 344 -0.0001

ARG 344 PRO 345 0.0279

PRO 345 ASP 346 -0.0003

ASP 346 LEU 347 0.0002

LEU 347 GLN 348 -0.0003

GLN 348 PRO 349 -0.0291

PRO 349 GLY 350 -0.0002

GLY 350 TYR 351 -0.0004

TYR 351 GLU 352 0.0001

GLU 352 GLY 353 0.0117

GLY 353 TRP 354 0.0003

TRP 354 GLN 355 0.0001

GLN 355 ALA 356 0.0001

ALA 356 ILE 357 -0.0244

ILE 357 ASP 358 -0.0005

ASP 358 PRO 359 0.0002

PRO 359 THR 360 0.0003

THR 360 PRO 361 -0.0244

PRO 361 GLN 362 0.0003

GLN 362 GLU 363 -0.0004

GLU 363 LYS 364 -0.0001

LYS 364 SER 365 -0.0428

SER 365 GLU 366 -0.0001

GLU 366 GLY 367 -0.0001

GLY 367 THR 368 0.0003

THR 368 TYR 369 -0.0091

TYR 369 CYS 370 -0.0001

CYS 370 CYS 371 -0.0000

CYS 371 GLY 372 0.0001

GLY 372 PRO 373 0.0050

PRO 373 VAL 374 0.0001

VAL 374 SER 375 -0.0003

SER 375 VAL 376 0.0003

VAL 376 ARG 377 -0.0226

ARG 377 ALA 378 -0.0002

ALA 378 ILE 379 -0.0003

ILE 379 LYS 380 -0.0002

LYS 380 GLU 381 -0.1588

GLU 381 GLY 382 0.0001

GLY 382 ASP 383 0.0002

ASP 383 LEU 384 0.0000

LEU 384 SER 385 -0.0089

SER 385 THR 386 0.0001

THR 386 LYS 387 -0.0004

LYS 387 TYR 388 0.0004

TYR 388 ASP 389 -0.0955

ASP 389 ALA 390 0.0002

ALA 390 PRO 391 0.0001

PRO 391 PHE 392 -0.0002

PHE 392 VAL 393 0.0229

VAL 393 PHE 394 -0.0002

PHE 394 ALA 395 -0.0003

ALA 395 GLU 396 -0.0002

GLU 396 VAL 397 -0.0663

VAL 397 ASN 398 -0.0003

ASN 398 ALA 399 0.0005

ALA 399 ASP 400 0.0000

ASP 400 VAL 401 -0.0813

VAL 401 VAL 402 -0.0002

VAL 402 ASP 403 -0.0000

ASP 403 TRP 404 0.0002

TRP 404 ILE 405 0.0014

ILE 405 ARG 406 -0.0000

ARG 406 GLN 407 0.0003

GLN 407 GLU 408 -0.0004

GLU 408 ASP 409 -0.0647

ASP 409 GLY 410 0.0001

GLY 410 SER 411 0.0001

SER 411 VAL 412 0.0002

VAL 412 LEU 413 0.0456

LEU 413 LYS 414 0.0001

LYS 414 SER 415 -0.0003

SER 415 ILE 416 0.0002

ILE 416 ASN 417 -0.0380

ASN 417 ARG 418 -0.0001

ARG 418 SER 419 0.0001

SER 419 LEU 420 -0.0002

LEU 420 VAL 421 -0.0552

VAL 421 VAL 422 -0.0001

VAL 422 GLY 423 0.0003

GLY 423 GLN 424 0.0002

GLN 424 LYS 425 -0.0051

LYS 425 ILE 426 0.0001

ILE 426 SER 427 -0.0000

SER 427 THR 428 0.0001

THR 428 LYS 429 -0.0528

LYS 429 SER 430 -0.0003

SER 430 VAL 431 -0.0000

VAL 431 GLY 432 0.0003

GLY 432 ARG 433 -0.1214

ARG 433 ASP 434 0.0001

ASP 434 ASP 435 0.0002

ASP 435 ARG 436 -0.0001

ARG 436 GLU 437 -0.0733

GLU 437 ASP 438 -0.0004

ASP 438 ILE 439 0.0003

ILE 439 THR 440 -0.0001

THR 440 HIS 441 -0.1334

HIS 441 THR 442 0.0001

THR 442 TYR 443 -0.0002

TYR 443 LYS 444 -0.0000

LYS 444 TYR 445 -0.0548

TYR 445 PRO 446 0.0002

PRO 446 GLU 447 0.0003

GLU 447 GLY 448 -0.0003

GLY 448 SER 449 -0.0526

SER 449 PRO 450 0.0000

PRO 450 GLU 451 0.0001

GLU 451 GLU 452 -0.0002

GLU 452 ARG 453 -0.1474

ARG 453 GLU 454 0.0001

GLU 454 VAL 455 0.0001

VAL 455 PHE 456 -0.0001

PHE 456 THR 457 -0.1176

THR 457 LYS 458 -0.0002

LYS 458 ALA 459 -0.0001

ALA 459 ASN 460 -0.0003

ASN 460 HIS 461 0.1175

HIS 461 LEU 462 0.0002

LEU 462 ASN 463 -0.0001

ASN 463 LYS 464 0.0001

LYS 464 LEU 465 -0.1444

LEU 465 ALA 466 0.0003

ALA 466 GLU 467 -0.0001

GLU 467 LYS 468 -0.0000

LYS 468 GLU 469 -0.0107

GLU 469 GLU 470 -0.0000

GLU 470 THR 471 -0.0000

THR 471 GLY 472 0.0000

GLY 472 VAL 473 0.0769

VAL 473 ALA 474 -0.0002

ALA 474 MET 475 0.0003

MET 475 ARG 476 0.0002

ARG 476 ILE 477 -0.2438

ILE 477 ARG 478 -0.0002

ARG 478 VAL 479 0.0004

VAL 479 GLY 480 -0.0002

GLY 480 ASP 481 -0.2018

ASP 481 SER 482 0.0002

SER 482 MET 483 -0.0003

MET 483 SER 484 0.0001

SER 484 MET 485 -0.1800

MET 485 GLY 486 -0.0001

GLY 486 ASN 487 0.0000

ASN 487 ASP 488 -0.0000

ASP 488 PHE 489 -0.0762

PHE 489 ASP 490 0.0001

ASP 490 VAL 491 -0.0002

VAL 491 PHE 492 -0.0004

PHE 492 ALA 493 -0.1213

ALA 493 HIS 494 -0.0002

HIS 494 ILE 495 -0.0001

ILE 495 GLY 496 0.0002

GLY 496 ASN 497 -0.2373

ASN 497 ASP 498 0.0000

ASP 498 THR 499 0.0001

THR 499 SER 500 -0.0000

SER 500 GLU 501 0.1130

GLU 501 THR 502 -0.0002

THR 502 ARG 503 0.0001

ARG 503 GLU 504 -0.0004

GLU 504 CYS 505 0.1316

CYS 505 ARG 506 -0.0001

ARG 506 LEU 507 0.0001

LEU 507 LEU 508 -0.0000

LEU 508 LEU 509 0.1423

LEU 509 CYS 510 0.0000

CYS 510 ALA 511 0.0002

ALA 511 ARG 512 -0.0003

ARG 512 THR 513 0.2694

THR 513 VAL 514 0.0004

VAL 514 SER 515 -0.0002

SER 515 TYR 516 -0.0000

TYR 516 ASN 517 -0.0088

ASN 517 GLY 518 -0.0003

GLY 518 VAL 519 0.0003

VAL 519 LEU 520 0.0001

LEU 520 GLY 521 -0.0678

GLY 521 PRO 522 0.0000

PRO 522 GLU 523 -0.0003

GLU 523 CYS 524 0.0000

CYS 524 GLY 525 0.2518

GLY 525 THR 526 0.0001

THR 526 GLU 527 -0.0001

GLU 527 ASP 528 0.0002

ASP 528 ILE 529 0.2867

ILE 529 ASN 530 0.0002

ASN 530 LEU 531 0.0003

LEU 531 THR 532 -0.0003

THR 532 LEU 533 0.2012

LEU 533 ASP 534 -0.0001

ASP 534 PRO 535 0.0002

PRO 535 TYR 536 0.0000

TYR 536 SER 537 -0.1084

SER 537 GLU 538 -0.0003

GLU 538 ASN 539 0.0002

ASN 539 SER 540 -0.0001

SER 540 ILE 541 0.0132

ILE 541 PRO 542 0.0003

PRO 542 LEU 543 -0.0001

LEU 543 ARG 544 0.0002

ARG 544 ILE 545 -0.0048

ILE 545 LEU 546 -0.0002

LEU 546 TYR 547 -0.0000

TYR 547 GLU 548 -0.0001

GLU 548 LYS 549 0.0254

LYS 549 TYR 550 0.0000

TYR 550 SER 551 0.0004

SER 551 GLY 552 -0.0002

GLY 552 CYS 553 -0.0397

CYS 553 LEU 554 0.0000

LEU 554 THR 555 -0.0000

THR 555 GLU 556 -0.0000

GLU 556 SER 557 -0.0715

SER 557 ASN 558 -0.0000

ASN 558 LEU 559 0.0001

LEU 559 ILE 560 -0.0002

ILE 560 LYS 561 0.1269

LYS 561 VAL 562 -0.0004

VAL 562 ARG 563 0.0004

ARG 563 GLY 564 -0.0002

GLY 564 LEU 565 0.0491

LEU 565 LEU 566 -0.0001

LEU 566 ILE 567 0.0004

ILE 567 GLU 568 -0.0003

GLU 568 PRO 569 0.0013

PRO 569 ALA 570 -0.0002

ALA 570 ALA 571 -0.0005

ALA 571 ASN 572 -0.0001

ASN 572 SER 573 0.1005

SER 573 TYR 574 -0.0002

TYR 574 LEU 575 0.0002

LEU 575 LEU 576 0.0004

LEU 576 ALA 577 -0.1718

ALA 577 GLU 578 0.0001

GLU 578 ARG 579 0.0002

ARG 579 ASP 580 0.0003

ASP 580 LEU 581 0.1062

LEU 581 TYR 582 0.0003

TYR 582 LEU 583 0.0001

LEU 583 GLU 584 0.0002

GLU 584 ASN 585 0.5136

ASN 585 PRO 586 -0.0003

PRO 586 GLU 587 -0.0000

GLU 587 ILE 588 -0.0002

ILE 588 LYS 589 -0.0942

LYS 589 ILE 590 -0.0002

ILE 590 ARG 591 0.0005

ARG 591 VAL 592 -0.0003

VAL 592 LEU 593 0.0754

LEU 593 GLY 594 -0.0001

GLY 594 GLU 595 -0.0000

GLU 595 PRO 596 0.0000

PRO 596 LYS 597 -0.3318

LYS 597 GLN 598 -0.0000

GLN 598 ASN 599 0.0002

ASN 599 ARG 600 0.0001

ARG 600 LYS 601 0.0109

LYS 601 LEU 602 -0.0002

LEU 602 VAL 603 0.0000

VAL 603 ALA 604 -0.0002

ALA 604 GLU 605 -0.3767

GLU 605 VAL 606 -0.0000

VAL 606 SER 607 0.0000

SER 607 LEU 608 -0.0002

LEU 608 LYS 609 -0.0938

LYS 609 ASN 610 -0.0002

ASN 610 PRO 611 0.0001

PRO 611 LEU 612 -0.0003

LEU 612 SER 613 -0.0398

SER 613 ASP 614 -0.0003

ASP 614 PRO 615 0.0004

PRO 615 LEU 616 -0.0000

LEU 616 TYR 617 0.0136

TYR 617 ASP 618 0.0000

ASP 618 CYS 619 -0.0002

CYS 619 ILE 620 0.0002

ILE 620 PHE 621 0.1385

PHE 621 THR 622 0.0001

THR 622 VAL 623 -0.0002

VAL 623 GLU 624 -0.0003

GLU 624 GLY 625 0.5326

GLY 625 ALA 626 -0.0004

ALA 626 GLY 627 0.0001

GLY 627 LEU 628 -0.0003

LEU 628 THR 629 0.2290

THR 629 LYS 630 0.0001

LYS 630 GLU 631 0.0003

GLU 631 GLN 632 0.0000

GLN 632 LYS 633 0.1682

LYS 633 SER 634 -0.0002

SER 634 VAL 635 -0.0001

VAL 635 GLU 636 0.0002

GLU 636 VAL 637 0.3145

VAL 637 SER 638 0.0001

SER 638 ASP 639 0.0003

ASP 639 PRO 640 0.0001

PRO 640 VAL 641 -0.0498

VAL 641 PRO 642 -0.0001

PRO 642 ALA 643 0.0001

ALA 643 GLY 644 0.0001

GLY 644 ASP 645 -0.2086

ASP 645 LEU 646 0.0002

LEU 646 VAL 647 -0.0000

VAL 647 LYS 648 -0.0002

LYS 648 ALA 649 0.1678

ALA 649 ARG 650 -0.0001

ARG 650 VAL 651 -0.0000

VAL 651 ASP 652 -0.0001

ASP 652 LEU 653 0.2694

LEU 653 PHE 654 0.0003

PHE 654 PRO 655 0.0001

PRO 655 THR 656 0.0000

THR 656 ASP 657 -0.0039

ASP 657 ILE 658 0.0003

ILE 658 GLY 659 -0.0000

GLY 659 LEU 660 0.0001

LEU 660 HIS 661 0.2551

HIS 661 LYS 662 -0.0002

LYS 662 LEU 663 0.0001

LEU 663 VAL 664 -0.0002

VAL 664 VAL 665 0.4408

VAL 665 ASN 666 0.0000

ASN 666 PHE 667 0.0000

PHE 667 GLN 668 0.0001

GLN 668 CYS 669 0.2624

CYS 669 ASP 670 0.0000

ASP 670 LYS 671 0.0006

LYS 671 LEU 672 -0.0003

LEU 672 LYS 673 0.0552

LYS 673 SER 674 0.0003

SER 674 VAL 675 0.0003

VAL 675 LYS 676 0.0001

LYS 676 GLY 677 0.0100

GLY 677 TYR 678 -0.0001

TYR 678 ARG 679 0.0002

ARG 679 ASN 680 0.0001

ASN 680 VAL 681 -0.0066

VAL 681 ILE 682 -0.0001

ILE 682 ILE 683 -0.0001

ILE 683 GLY 684 0.0001

GLY 684 PRO 685 -0.2380

PRO 685 ALA 686 0.0001

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.

*** itasser_mtg2_model4 ***

CA strain for 2407102126523076348

--- normal mode 24 ---

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

* itasser_mtg2_model4 *