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

* erb3MUT *

CA strain for 22042816174173283

--- normal mode 7 ---

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 8 VAL 9 -0.0002

VAL 9 CYS 10 0.0002

CYS 10 PRO 11 -0.0003

PRO 11 GLY 12 0.0063

GLY 12 THR 13 0.0001

THR 13 LEU 14 0.0000

LEU 14 ASN 15 0.0004

ASN 15 GLY 16 -0.0020

GLY 16 LEU 17 -0.0001

LEU 17 SER 18 -0.0002

SER 18 VAL 19 0.0000

VAL 19 ALA 23 0.0002

ALA 23 GLU 24 -0.0005

GLU 24 ASN 25 0.0001

ASN 25 GLN 26 -0.0001

GLN 26 TYR 27 -0.0003

TYR 27 GLN 28 0.0001

GLN 28 THR 29 -0.0001

THR 29 LEU 30 0.0001

LEU 30 TYR 31 0.0004

TYR 31 LYS 32 -0.0000

LYS 32 LEU 33 -0.0003

LEU 33 TYR 34 -0.0001

TYR 34 GLU 35 -0.0007

GLU 35 ARG 36 0.0001

ARG 36 CYS 37 0.0001

CYS 37 GLU 38 -0.0003

GLU 38 VAL 39 -0.0008

VAL 39 VAL 40 0.0001

VAL 40 MET 41 0.0001

MET 41 GLY 42 0.0005

GLY 42 ASN 43 -0.0018

ASN 43 LEU 44 -0.0002

LEU 44 GLU 45 0.0002

GLU 45 ILE 46 -0.0002

ILE 46 VAL 47 0.0005

VAL 47 LEU 48 -0.0003

LEU 48 THR 49 -0.0003

THR 49 GLY 50 0.0003

GLY 50 HIS 51 -0.0008

HIS 51 ASN 52 -0.0001

ASN 52 ALA 53 -0.0004

ALA 53 ASP 54 -0.0002

ASP 54 LEU 55 0.0003

LEU 55 SER 56 0.0002

SER 56 PHE 57 -0.0000

PHE 57 LEU 58 -0.0000

LEU 58 GLN 59 -0.0005

GLN 59 TRP 60 0.0001

TRP 60 ILE 61 0.0002

ILE 61 ARG 62 0.0002

ARG 62 GLU 63 -0.0015

GLU 63 VAL 64 -0.0001

VAL 64 THR 65 -0.0004

THR 65 GLY 66 0.0001

GLY 66 TYR 67 -0.0010

TYR 67 VAL 68 0.0003

VAL 68 LEU 69 -0.0000

LEU 69 VAL 70 0.0001

VAL 70 ALA 71 0.0000

ALA 71 MET 72 -0.0001

MET 72 ASN 73 -0.0001

ASN 73 GLU 74 -0.0003

GLU 74 PHE 75 -0.0004

PHE 75 SER 76 0.0000

SER 76 THR 77 0.0004

THR 77 LEU 78 0.0001

LEU 78 PRO 79 0.0009

PRO 79 LEU 80 0.0002

LEU 80 PRO 81 -0.0003

PRO 81 ASN 82 -0.0000

ASN 82 LEU 83 -0.0013

LEU 83 ARG 84 0.0003

ARG 84 VAL 85 0.0000

VAL 85 VAL 86 -0.0002

VAL 86 ARG 87 -0.0018

ARG 87 GLY 88 0.0004

GLY 88 THR 89 -0.0002

THR 89 GLN 90 0.0001

GLN 90 VAL 91 -0.0011

VAL 91 TYR 92 -0.0001

TYR 92 ASP 93 0.0001

ASP 93 GLY 94 -0.0002

GLY 94 LYS 95 -0.0001

LYS 95 PHE 96 -0.0000

PHE 96 ALA 97 0.0001

ALA 97 ILE 98 -0.0000

ILE 98 PHE 99 -0.0004

PHE 99 VAL 100 -0.0000

VAL 100 MET 101 -0.0002

MET 101 LEU 102 -0.0000

LEU 102 ASN 103 0.0003

ASN 103 TYR 104 -0.0002

TYR 104 ASN 105 -0.0003

ASN 105 THR 106 0.0001

THR 106 ASN 107 -0.0000

ASN 107 SER 108 -0.0000

SER 108 SER 109 0.0000

SER 109 HIS 110 -0.0000

HIS 110 ALA 111 -0.0000

ALA 111 LEU 112 -0.0003

LEU 112 ARG 113 0.0000

ARG 113 GLN 114 -0.0002

GLN 114 LEU 115 -0.0001

LEU 115 ARG 116 0.0002

ARG 116 LEU 117 0.0004

LEU 117 THR 118 -0.0001

THR 118 GLN 119 -0.0004

GLN 119 LEU 120 -0.0002

LEU 120 THR 121 -0.0000

THR 121 GLU 122 0.0002

GLU 122 ILE 123 0.0005

ILE 123 LEU 124 0.0001

LEU 124 SER 125 0.0000

SER 125 GLY 126 -0.0000

GLY 126 GLY 127 -0.0022

GLY 127 VAL 128 0.0001

VAL 128 TYR 129 0.0000

TYR 129 ILE 130 -0.0001

ILE 130 GLU 131 -0.0000

GLU 131 LYS 132 -0.0003

LYS 132 ASN 133 -0.0004

ASN 133 ASP 134 -0.0001

ASP 134 LYS 135 -0.0000

LYS 135 LEU 136 0.0001

LEU 136 CYS 137 0.0001

CYS 137 HIS 138 -0.0001

HIS 138 MET 139 -0.0003

MET 139 ASP 140 -0.0004

ASP 140 THR 141 -0.0001

THR 141 ILE 142 0.0001

ILE 142 ASP 143 -0.0010

ASP 143 TRP 144 0.0002

TRP 144 ARG 145 -0.0004

ARG 145 ASP 146 0.0000

ASP 146 ILE 147 -0.0006

ILE 147 VAL 148 0.0000

VAL 148 ARG 149 -0.0000

ARG 149 ASP 150 0.0001

ASP 150 ARG 151 -0.0007

ARG 151 ASP 152 0.0001

ASP 152 ALA 153 0.0002

ALA 153 GLU 154 -0.0003

GLU 154 ILE 155 0.0000

ILE 155 VAL 156 -0.0000

VAL 156 VAL 157 0.0002

VAL 157 LYS 158 -0.0000

LYS 158 ASP 159 -0.0003

ASP 159 ASN 160 0.0003

ASN 160 GLY 161 -0.0002

GLY 161 ARG 162 0.0003

ARG 162 SER 163 -0.0003

SER 163 CYS 164 -0.0003

CYS 164 PRO 165 -0.0000

PRO 165 PRO 166 0.0002

PRO 166 CYS 167 -0.0000

CYS 167 HIS 168 0.0003

HIS 168 GLU 169 -0.0000

GLU 169 VAL 170 0.0001

VAL 170 CYS 171 -0.0002

CYS 171 LYS 172 0.0001

LYS 172 GLY 173 0.0001

GLY 173 ARG 174 -0.0003

ARG 174 CYS 175 0.0003

CYS 175 TRP 176 -0.0001

TRP 176 GLY 177 0.0003

GLY 177 PRO 178 0.0001

PRO 178 GLY 179 -0.0007

GLY 179 SER 180 0.0003

SER 180 GLU 181 0.0004

GLU 181 ASP 182 -0.0002

ASP 182 CYS 183 -0.0008

CYS 183 GLN 184 0.0001

GLN 184 THR 185 0.0000

THR 185 LEU 186 -0.0001

LEU 186 THR 187 -0.0008

THR 187 LYS 188 -0.0001

LYS 188 THR 189 0.0002

THR 189 ILE 190 -0.0001

ILE 190 CYS 191 -0.0011

CYS 191 ALA 192 0.0000

ALA 192 PRO 193 -0.0002

PRO 193 GLN 194 -0.0001

GLN 194 CYS 195 0.0002

CYS 195 ASN 196 0.0003

ASN 196 GLY 197 -0.0002

GLY 197 HIS 198 0.0001

HIS 198 CYS 199 -0.0023

CYS 199 PHE 200 0.0001

PHE 200 GLY 201 -0.0003

GLY 201 PRO 202 -0.0000

PRO 202 ASN 203 0.0006

ASN 203 PRO 204 0.0000

PRO 204 ASN 205 0.0003

ASN 205 GLN 206 -0.0003

GLN 206 CYS 207 -0.0008

CYS 207 CYS 208 -0.0003

CYS 208 HIS 209 -0.0000

HIS 209 ASP 210 0.0000

ASP 210 GLU 211 -0.0018

GLU 211 CYS 212 0.0002

CYS 212 ALA 213 0.0001

ALA 213 GLY 214 -0.0001

GLY 214 GLY 215 -0.0057

GLY 215 CYS 216 0.0001

CYS 216 SER 217 -0.0001

SER 217 GLY 218 0.0002

GLY 218 PRO 219 -0.0018

PRO 219 GLN 220 0.0003

GLN 220 ASP 221 -0.0004

ASP 221 THR 222 -0.0004

THR 222 ASP 223 0.0053

ASP 223 CYS 224 -0.0003

CYS 224 PHE 225 0.0004

PHE 225 ALA 226 0.0000

ALA 226 CYS 227 -0.0027

CYS 227 ARG 228 -0.0000

ARG 228 HIS 229 0.0004

HIS 229 PHE 230 -0.0000

PHE 230 ASN 231 0.0021

ASN 231 ASP 232 0.0002

ASP 232 SER 233 0.0003

SER 233 GLY 234 0.0002

GLY 234 ALA 235 -0.0061

ALA 235 CYS 236 0.0000

CYS 236 VAL 237 0.0001

VAL 237 PRO 238 -0.0002

PRO 238 ARG 239 -0.0148

ARG 239 CYS 240 -0.0002

CYS 240 PRO 241 -0.0001

PRO 241 GLN 242 -0.0003

GLN 242 PRO 243 0.0136

PRO 243 LEU 244 -0.0004

LEU 244 VAL 245 -0.0000

VAL 245 TYR 246 0.0002

TYR 246 ASN 247 0.0045

ASN 247 LYS 248 0.0001

LYS 248 LEU 249 -0.0003

LEU 249 THR 250 -0.0001

THR 250 PHE 251 -0.0065

PHE 251 GLN 252 0.0000

GLN 252 LEU 253 -0.0001

LEU 253 GLU 254 0.0000

GLU 254 PRO 255 0.0345

PRO 255 ASN 256 -0.0002

ASN 256 PRO 257 -0.0002

PRO 257 HIS 258 -0.0001

HIS 258 THR 259 -0.0288

THR 259 LYS 260 0.0002

LYS 260 TYR 261 0.0001

TYR 261 GLN 262 0.0002

GLN 262 TYR 263 -0.0024

TYR 263 GLY 264 0.0002

GLY 264 GLY 265 -0.0003

GLY 265 VAL 266 0.0001

VAL 266 CYS 267 0.0038

CYS 267 VAL 268 -0.0001

VAL 268 ALA 269 0.0004

ALA 269 SER 270 0.0004

SER 270 CYS 271 -0.0036

CYS 271 PRO 272 0.0000

PRO 272 HIS 273 -0.0000

HIS 273 ASN 274 0.0001

ASN 274 PHE 275 0.0005

PHE 275 VAL 276 -0.0000

VAL 276 VAL 277 -0.0000

VAL 277 ASP 278 -0.0000

ASP 278 GLN 279 0.0029

GLN 279 THR 280 -0.0003

THR 280 SER 281 -0.0003

SER 281 CYS 282 0.0001

CYS 282 VAL 283 0.0025

VAL 283 ARG 284 -0.0001

ARG 284 ALA 285 0.0003

ALA 285 CYS 286 -0.0000

CYS 286 PRO 287 -0.0075

PRO 287 PRO 288 -0.0000

PRO 288 ASP 289 0.0001

ASP 289 LYS 290 -0.0002

LYS 290 MET 291 -0.0021

MET 291 GLU 292 0.0001

GLU 292 VAL 293 0.0001

VAL 293 ASP 294 -0.0005

ASP 294 LYS 295 -0.0009

LYS 295 ASN 296 0.0003

ASN 296 GLY 297 -0.0003

GLY 297 LEU 298 -0.0002

LEU 298 LYS 299 -0.0002

LYS 299 MET 300 0.0001

MET 300 CYS 301 0.0001

CYS 301 GLU 302 -0.0001

GLU 302 PRO 303 -0.0079

PRO 303 CYS 304 -0.0002

CYS 304 GLY 305 -0.0000

GLY 305 GLY 306 0.0002

GLY 306 LEU 307 0.0518

LEU 307 CYS 308 0.0001

CYS 308 PRO 309 0.0002

PRO 309 LYS 310 -0.0001

LYS 310 ALA 311 0.0239

ALA 311 CYS 312 -0.0003

CYS 312 GLU 313 -0.0001

GLU 313 GLY 314 0.0003

GLY 314 THR 315 0.0034

THR 315 GLY 316 -0.0001

GLY 316 SER 317 -0.0000

SER 317 GLY 318 -0.0003

GLY 318 SER 319 -0.0009

SER 319 ARG 320 -0.0000

ARG 320 PHE 321 0.0001

PHE 321 GLN 322 0.0000

GLN 322 THR 323 0.0002

THR 323 VAL 324 0.0002

VAL 324 ASP 325 0.0003

ASP 325 SER 326 -0.0001

SER 326 SER 327 -0.0008

SER 327 ASN 328 0.0001

ASN 328 ILE 329 -0.0001

ILE 329 ASP 330 -0.0001

ASP 330 GLY 331 -0.0050

GLY 331 PHE 332 -0.0002

PHE 332 VAL 333 0.0004

VAL 333 ASN 334 -0.0003

ASN 334 CYS 335 0.0050

CYS 335 THR 336 -0.0003

THR 336 LYS 337 0.0004

LYS 337 ILE 338 -0.0005

ILE 338 LEU 339 -0.0004

LEU 339 GLY 340 -0.0002

GLY 340 ASN 341 0.0000

ASN 341 LEU 342 -0.0000

LEU 342 ASP 343 0.0008

ASP 343 PHE 344 -0.0001

PHE 344 LEU 345 -0.0003

LEU 345 ILE 346 0.0002

ILE 346 THR 347 -0.0008

THR 347 GLY 348 0.0003

GLY 348 LEU 349 0.0003

LEU 349 ASN 350 0.0003

ASN 350 GLY 351 0.0008

GLY 351 ASP 352 0.0000

ASP 352 PRO 353 -0.0000

PRO 353 TRP 354 -0.0001

TRP 354 HIS 355 0.0000

HIS 355 LYS 356 -0.0002

LYS 356 ILE 357 -0.0001

ILE 357 PRO 358 -0.0002

PRO 358 ALA 359 0.0021

ALA 359 LEU 360 0.0000

LEU 360 ASP 361 -0.0000

ASP 361 PRO 362 -0.0002

PRO 362 GLU 363 0.0002

GLU 363 LYS 364 0.0002

LYS 364 LEU 365 -0.0000

LEU 365 ASN 366 -0.0002

ASN 366 VAL 367 -0.0019

VAL 367 PHE 368 0.0001

PHE 368 ARG 369 0.0003

ARG 369 THR 370 0.0002

THR 370 VAL 371 -0.0006

VAL 371 ARG 372 0.0000

ARG 372 GLU 373 0.0001

GLU 373 ILE 374 0.0001

ILE 374 THR 375 -0.0015

THR 375 GLY 376 -0.0001

GLY 376 TYR 377 0.0003

TYR 377 LEU 378 0.0001

LEU 378 ASN 379 0.0003

ASN 379 ILE 380 0.0002

ILE 380 GLN 381 -0.0001

GLN 381 SER 382 -0.0002

SER 382 TRP 383 -0.0000

TRP 383 PRO 384 -0.0001

PRO 384 PRO 385 -0.0002

PRO 385 HIS 386 0.0001

HIS 386 MET 387 0.0007

MET 387 HIS 388 -0.0003

HIS 388 ASN 389 -0.0001

ASN 389 PHE 390 -0.0001

PHE 390 SER 391 -0.0002

SER 391 VAL 392 -0.0000

VAL 392 PHE 393 0.0002

PHE 393 SER 394 -0.0002

SER 394 ASN 395 0.0004

ASN 395 LEU 396 -0.0000

LEU 396 THR 397 -0.0003

THR 397 THR 398 0.0002

THR 398 ILE 399 -0.0002

ILE 399 GLY 400 -0.0000

GLY 400 GLY 401 0.0000

GLY 401 ARG 402 0.0000

ARG 402 SER 403 -0.0008

SER 403 LEU 404 0.0000

LEU 404 TYR 405 0.0000

TYR 405 ASN 406 -0.0000

ASN 406 ARG 407 -0.0004

ARG 407 GLY 408 -0.0001

GLY 408 PHE 409 0.0002

PHE 409 SER 410 -0.0002

SER 410 LEU 411 0.0004

LEU 411 LEU 412 -0.0003

LEU 412 ILE 413 -0.0001

ILE 413 MET 414 -0.0002

MET 414 LYS 415 0.0003

LYS 415 ASN 416 -0.0000

ASN 416 LEU 417 -0.0001

LEU 417 ASN 418 -0.0002

ASN 418 VAL 419 0.0013

VAL 419 THR 420 0.0001

THR 420 SER 421 -0.0003

SER 421 LEU 422 0.0003

LEU 422 GLY 423 0.0008

GLY 423 PHE 424 0.0001

PHE 424 ARG 425 -0.0001

ARG 425 SER 426 -0.0001

SER 426 LEU 427 0.0028

LEU 427 LYS 428 -0.0000

LYS 428 GLU 429 0.0001

GLU 429 ILE 430 0.0003

ILE 430 SER 431 -0.0002

SER 431 ALA 432 0.0001

ALA 432 GLY 433 0.0002

GLY 433 ARG 434 0.0001

ARG 434 ILE 435 0.0001

ILE 435 TYR 436 -0.0000

TYR 436 ILE 437 0.0001

ILE 437 SER 438 -0.0004

SER 438 ALA 439 0.0003

ALA 439 ASN 440 -0.0001

ASN 440 ARG 441 -0.0001

ARG 441 GLN 442 -0.0000

GLN 442 LEU 443 -0.0002

LEU 443 CYS 444 0.0001

CYS 444 TYR 445 -0.0000

TYR 445 HIS 446 0.0003

HIS 446 HIS 447 -0.0001

HIS 447 SER 448 0.0000

SER 448 LEU 449 0.0004

LEU 449 ASN 450 -0.0001

ASN 450 TRP 451 -0.0013

TRP 451 THR 452 0.0003

THR 452 LYS 453 0.0001

LYS 453 VAL 454 0.0003

VAL 454 LEU 455 -0.0025

LEU 455 ARG 456 -0.0003

ARG 456 GLY 457 -0.0000

GLY 457 PRO 458 -0.0001

PRO 458 THR 459 -0.0000

THR 459 GLU 460 0.0002

GLU 460 GLU 461 0.0004

GLU 461 ARG 462 0.0005

ARG 462 LEU 463 0.0005

LEU 463 ASP 464 0.0001

ASP 464 ILE 465 0.0001

ILE 465 LYS 466 -0.0004

LYS 466 HIS 467 0.0007

HIS 467 ASN 468 0.0002

ASN 468 ARG 469 -0.0001

ARG 469 PRO 470 -0.0001

PRO 470 ARG 471 -0.0013

ARG 471 ARG 472 -0.0000

ARG 472 ASP 473 -0.0001

ASP 473 CYS 474 -0.0002

CYS 474 VAL 475 0.0004

VAL 475 ALA 476 0.0003

ALA 476 GLU 477 0.0003

GLU 477 GLY 478 0.0001

GLY 478 LYS 479 0.0001

LYS 479 VAL 480 -0.0001

VAL 480 CYS 481 -0.0004

CYS 481 ASP 482 -0.0000

ASP 482 PRO 483 0.0032

PRO 483 LEU 484 -0.0000

LEU 484 CYS 485 -0.0003

CYS 485 SER 486 0.0002

SER 486 SER 487 -0.0035

SER 487 GLY 488 0.0001

GLY 488 GLY 489 -0.0001

GLY 489 CYS 490 0.0002

CYS 490 TRP 491 -0.0001

TRP 491 GLY 492 0.0001

GLY 492 PRO 493 0.0004

PRO 493 GLY 494 0.0001

GLY 494 PRO 495 0.0029

PRO 495 GLY 496 0.0002

GLY 496 GLN 497 0.0002

GLN 497 CYS 498 0.0001

CYS 498 LEU 499 0.0020

LEU 499 SER 500 0.0000

SER 500 CYS 501 0.0000

CYS 501 ARG 502 -0.0002

ARG 502 ASN 503 -0.0242

ASN 503 TYR 504 0.0001

TYR 504 SER 505 0.0001

SER 505 ARG 506 -0.0003

ARG 506 GLY 507 0.0097

GLY 507 GLY 508 -0.0002

GLY 508 VAL 509 -0.0002

VAL 509 CYS 510 0.0001

CYS 510 VAL 511 0.0061

VAL 511 THR 512 0.0004

THR 512 HIS 513 0.0001

HIS 513 CYS 514 -0.0003

CYS 514 ASN 515 -0.0019

ASN 515 PHE 516 -0.0003

PHE 516 LEU 517 0.0003

LEU 517 ASN 518 0.0002

ASN 518 GLY 519 -0.0052

GLY 519 GLU 520 -0.0000

GLU 520 PRO 521 -0.0001

PRO 521 ARG 522 0.0003

ARG 522 GLU 523 -0.0018

GLU 523 PHE 524 0.0001

PHE 524 ALA 525 -0.0001

ALA 525 HIS 526 0.0001

HIS 526 GLU 527 -0.0066

GLU 527 ALA 528 -0.0000

ALA 528 GLU 529 0.0000

GLU 529 CYS 530 0.0002

CYS 530 PHE 531 0.0031

PHE 531 SER 532 -0.0001

SER 532 CYS 533 -0.0001

CYS 533 HIS 534 0.0001

HIS 534 PRO 535 0.0088

PRO 535 GLU 536 -0.0003

GLU 536 CYS 537 -0.0002

CYS 537 GLN 538 0.0001

GLN 538 PRO 539 -0.0063

PRO 539 MET 540 -0.0002

MET 540 GLU 541 0.0005

GLU 541 GLY 542 -0.0002

GLY 542 THR 543 0.0040

THR 543 ALA 544 0.0004

ALA 544 THR 545 -0.0005

THR 545 CYS 546 -0.0000

CYS 546 ASN 547 -0.0025

ASN 547 GLY 548 -0.0000

GLY 548 SER 549 0.0001

SER 549 GLY 550 -0.0002

GLY 550 SER 551 0.0056

SER 551 ASP 552 0.0001

ASP 552 THR 553 -0.0001

THR 553 CYS 554 0.0000

CYS 554 ALA 555 0.0103

ALA 555 GLN 556 0.0003

GLN 556 CYS 557 -0.0005

CYS 557 ALA 558 0.0002

ALA 558 HIS 559 -0.0272

HIS 559 PHE 560 0.0001

PHE 560 ARG 561 -0.0001

ARG 561 ASP 562 0.0003

ASP 562 GLY 563 -0.0043

GLY 563 PRO 564 0.0000

PRO 564 PHE 565 -0.0001

PHE 565 CYS 566 0.0001

CYS 566 VAL 567 0.0010

VAL 567 SER 568 0.0002

SER 568 SER 569 0.0002

SER 569 CYS 570 0.0001

CYS 570 PRO 571 -0.0167

PRO 571 HIS 572 -0.0001

HIS 572 GLY 573 0.0000

GLY 573 VAL 574 -0.0002

VAL 574 LEU 575 -0.0188

LEU 575 GLY 576 0.0003

GLY 576 ALA 577 -0.0001

ALA 577 LYS 578 -0.0001

LYS 578 GLY 579 -0.0168

GLY 579 PRO 580 0.0002

PRO 580 ILE 581 -0.0002

ILE 581 TYR 582 -0.0002

TYR 582 LYS 583 -0.0100

LYS 583 TYR 584 0.0001

TYR 584 PRO 585 -0.0000

PRO 585 ASP 586 0.0001

ASP 586 VAL 587 -0.0020

VAL 587 GLN 588 0.0001

GLN 588 ASN 589 -0.0001

ASN 589 GLU 590 -0.0001

GLU 590 CYS 591 -0.0033

CYS 591 ARG 592 0.0000

ARG 592 PRO 593 -0.0001

PRO 593 CYS 594 -0.0000

CYS 594 HIS 595 -0.0002

HIS 595 GLU 596 -0.0004

GLU 596 ASN 597 0.0003

ASN 597 CYS 598 0.0000

CYS 598 THR 599 0.0015

THR 599 GLN 600 -0.0001

GLN 600 GLY 601 0.0002

GLY 601 CYS 602 -0.0000

CYS 602 LYS 603 -0.0016

LYS 603 GLY 604 0.0005

GLY 604 PRO 605 -0.0003

PRO 605 GLU 606 0.0000

GLU 606 LEU 607 0.0011

LEU 607 GLN 608 0.0001

GLN 608 ASP 609 0.0002

ASP 609 CYS 610 0.0002

CYS 610 LEU 611 -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.

*** erb3MUT ***

CA strain for 22042816174173283

--- normal mode 7 ---

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

* erb3MUT *