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

* NMA_rosettafold_2round(rank4) *

CA strain for 2403040904371504613

--- normal mode 11 ---

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 ASP 2 -0.0000

ASP 2 PHE 3 0.0001

PHE 3 CYS 4 0.0001

CYS 4 LEU 5 0.0720

LEU 5 LEU 6 0.0001

LEU 6 ASN 7 0.0000

ASN 7 GLU 8 -0.0001

GLU 8 LYS 9 -0.0124

LYS 9 SER 10 0.0003

SER 10 GLN 11 -0.0001

GLN 11 ILE 12 0.0003

ILE 12 PHE 13 0.0108

PHE 13 VAL 14 0.0003

VAL 14 HIS 15 -0.0003

HIS 15 ALA 16 0.0001

ALA 16 GLU 17 0.0495

GLU 17 PRO 18 0.0000

PRO 18 TYR 19 0.0000

TYR 19 ALA 20 0.0001

ALA 20 VAL 21 0.0086

VAL 21 SER 22 -0.0000

SER 22 ASP 23 0.0001

ASP 23 TYR 24 0.0003

TYR 24 VAL 25 0.0231

VAL 25 ASN 26 0.0002

ASN 26 GLN 27 -0.0001

GLN 27 TYR 28 0.0002

TYR 28 VAL 29 0.0019

VAL 29 GLY 30 0.0002

GLY 30 THR 31 -0.0002

THR 31 HIS 32 0.0000

HIS 32 SER 33 -0.0419

SER 33 ILE 34 -0.0002

ILE 34 ARG 35 0.0002

ARG 35 LEU 36 -0.0003

LEU 36 PRO 37 -0.0240

PRO 37 LYS 38 -0.0001

LYS 38 GLY 39 -0.0001

GLY 39 GLY 40 -0.0003

GLY 40 ARG 41 0.0528

ARG 41 PRO 42 0.0002

PRO 42 ALA 43 0.0001

ALA 43 GLY 44 -0.0003

GLY 44 ARG 45 0.0634

ARG 45 LEU 46 0.0000

LEU 46 HIS 47 -0.0002

HIS 47 HIS 48 -0.0003

HIS 48 ARG 49 -0.0238

ARG 49 ILE 50 -0.0000

ILE 50 PHE 51 -0.0002

PHE 51 GLY 52 -0.0001

GLY 52 CYS 53 -0.1055

CYS 53 LEU 54 -0.0002

LEU 54 ASP 55 0.0002

ASP 55 LEU 56 -0.0002

LEU 56 CYS 57 -0.0205

CYS 57 ARG 58 0.0003

ARG 58 ILE 59 -0.0002

ILE 59 SER 60 0.0002

SER 60 TYR 61 0.0134

TYR 61 GLY 62 0.0005

GLY 62 GLY 63 -0.0002

GLY 63 SER 64 0.0001

SER 64 VAL 65 -0.0190

VAL 65 ARG 66 0.0000

ARG 66 VAL 67 -0.0000

VAL 67 ILE 68 0.0000

ILE 68 SER 69 -0.0504

SER 69 PRO 70 0.0001

PRO 70 GLY 71 0.0002

GLY 71 LEU 72 0.0001

LEU 72 GLU 73 -0.0047

GLU 73 THR 74 0.0003

THR 74 CYS 75 0.0004

CYS 75 TYR 76 -0.0002

TYR 76 HIS 77 0.0205

HIS 77 LEU 78 -0.0003

LEU 78 GLN 79 0.0002

GLN 79 ILE 80 -0.0005

ILE 80 ILE 81 -0.0126

ILE 81 LEU 82 0.0002

LEU 82 LYS 83 0.0003

LYS 83 GLY 84 0.0004

GLY 84 HIS 85 0.0075

HIS 85 CYS 86 -0.0002

CYS 86 LEU 87 0.0000

LEU 87 TRP 88 0.0001

TRP 88 ARG 89 0.0023

ARG 89 GLY 90 -0.0004

GLY 90 HIS 91 0.0003

HIS 91 GLY 92 -0.0000

GLY 92 GLN 93 0.0008

GLN 93 GLU 94 0.0005

GLU 94 HIS 95 -0.0002

HIS 95 TYR 96 0.0001

TYR 96 PHE 97 0.0008

PHE 97 ALA 98 0.0002

ALA 98 PRO 99 0.0000

PRO 99 GLY 100 -0.0002

GLY 100 GLU 101 0.0005

GLU 101 LEU 102 0.0001

LEU 102 LEU 103 0.0001

LEU 103 LEU 104 -0.0002

LEU 104 LEU 105 0.0030

LEU 105 ASN 106 0.0003

ASN 106 PRO 107 -0.0000

PRO 107 ASP 108 0.0000

ASP 108 ASP 109 -0.0130

ASP 109 GLN 110 -0.0005

GLN 110 ALA 111 0.0002

ALA 111 ASP 112 0.0003

ASP 112 LEU 113 -0.0076

LEU 113 THR 114 0.0000

THR 114 TYR 115 0.0000

TYR 115 SER 116 0.0000

SER 116 GLU 117 -0.0024

GLU 117 ASP 118 -0.0001

ASP 118 CYS 119 -0.0002

CYS 119 GLU 120 0.0002

GLU 120 LYS 121 -0.0225

LYS 121 PHE 122 -0.0004

PHE 122 ILE 123 0.0003

ILE 123 VAL 124 0.0001

VAL 124 LYS 125 0.0089

LYS 125 LEU 126 0.0004

LEU 126 PRO 127 -0.0002

PRO 127 SER 128 -0.0001

SER 128 VAL 129 -0.0099

VAL 129 VAL 130 0.0001

VAL 130 LEU 131 0.0000

LEU 131 ASP 132 0.0001

ASP 132 ARG 133 0.0076

ARG 133 ALA 134 -0.0002

ALA 134 CYS 135 0.0004

CYS 135 SER 136 -0.0001

SER 136 ASP 137 0.0069

ASP 137 ASN 138 0.0003

ASN 138 ASN 139 0.0004

ASN 139 TRP 140 -0.0000

TRP 140 HIS 141 0.0091

HIS 141 LYS 142 0.0004

LYS 142 PRO 143 -0.0001

PRO 143 ARG 144 0.0000

ARG 144 GLU 145 -0.0203

GLU 145 GLY 146 -0.0002

GLY 146 ILE 147 0.0004

ILE 147 ARG 148 -0.0002

ARG 148 PHE 149 -0.0079

PHE 149 ALA 150 -0.0001

ALA 150 ALA 151 0.0003

ALA 151 ARG 152 0.0003

ARG 152 HIS 153 -0.0018

HIS 153 ASN 154 -0.0000

ASN 154 LEU 155 0.0002

LEU 155 GLN 156 -0.0001

GLN 156 GLN 157 0.0028

GLN 157 LEU 158 0.0003

LEU 158 ASP 159 -0.0000

ASP 159 GLY 160 0.0002

GLY 160 PHE 161 -0.0064

PHE 161 ILE 162 -0.0002

ILE 162 ASN 163 -0.0004

ASN 163 LEU 164 -0.0002

LEU 164 LEU 165 0.0060

LEU 165 GLY 166 -0.0001

GLY 166 LEU 167 -0.0003

LEU 167 VAL 168 0.0001

VAL 168 CYS 169 0.0087

CYS 169 ASP 170 0.0003

ASP 170 GLU 171 0.0002

GLU 171 ALA 172 0.0001

ALA 172 GLU 173 0.0036

GLU 173 HIS 174 0.0002

HIS 174 THR 175 0.0002

THR 175 LYS 176 -0.0002

LYS 176 SER 177 0.0075

SER 177 MET 178 0.0002

MET 178 PRO 179 0.0000

PRO 179 ARG 180 -0.0000

ARG 180 VAL 181 0.0548

VAL 181 GLN 182 -0.0001

GLN 182 GLU 183 -0.0001

GLU 183 HIS 184 -0.0001

HIS 184 TYR 185 -0.0066

TYR 185 ALA 186 -0.0004

ALA 186 GLY 187 0.0002

GLY 187 ILE 188 0.0002

ILE 188 ILE 189 -0.0194

ILE 189 ALA 190 -0.0001

ALA 190 SER 191 -0.0003

SER 191 LYS 192 -0.0004

LYS 192 LEU 193 -0.0201

LEU 193 LEU 194 -0.0001

LEU 194 GLU 195 -0.0004

GLU 195 MET 196 0.0003

MET 196 LEU 197 -0.0037

LEU 197 GLY 198 -0.0001

GLY 198 SER 199 0.0000

SER 199 ASN 200 0.0002

ASN 200 VAL 201 0.0025

VAL 201 SER 202 -0.0002

SER 202 ARG 203 0.0002

ARG 203 GLU 204 -0.0002

GLU 204 ILE 205 -0.0119

ILE 205 PHE 206 -0.0004

PHE 206 SER 207 -0.0000

SER 207 LYS 208 -0.0000

LYS 208 GLY 209 0.0579

GLY 209 ASN 210 0.0003

ASN 210 PRO 211 0.0001

PRO 211 SER 212 -0.0001

SER 212 PHE 213 -0.0001

PHE 213 GLU 214 0.0000

GLU 214 ARG 215 -0.0000

ARG 215 VAL 216 -0.0002

VAL 216 VAL 217 -0.0083

VAL 217 GLN 218 0.0002

GLN 218 PHE 219 0.0004

PHE 219 ILE 220 -0.0002

ILE 220 GLU 221 -0.0244

GLU 221 GLU 222 -0.0001

GLU 222 ASN 223 0.0000

ASN 223 LEU 224 -0.0001

LEU 224 LYS 225 0.0197

LYS 225 ARG 226 0.0001

ARG 226 ASN 227 -0.0001

ASN 227 ILE 228 0.0001

ILE 228 SER 229 -0.0083

SER 229 LEU 230 0.0002

LEU 230 GLU 231 0.0002

GLU 231 ARG 232 -0.0001

ARG 232 LEU 233 0.0117

LEU 233 ALA 234 0.0000

ALA 234 GLU 235 -0.0002

GLU 235 LEU 236 0.0001

LEU 236 ALA 237 -0.0073

ALA 237 MET 238 -0.0000

MET 238 MET 239 0.0002

MET 239 SER 240 -0.0003

SER 240 PRO 241 -0.0004

PRO 241 ARG 242 -0.0003

ARG 242 SER 243 0.0001

SER 243 LEU 244 0.0004

LEU 244 TYR 245 0.0027

TYR 245 ASN 246 -0.0000

ASN 246 LEU 247 0.0000

LEU 247 PHE 248 -0.0001

PHE 248 GLU 249 0.0028

GLU 249 LYS 250 0.0000

LYS 250 HIS 251 -0.0002

HIS 251 ALA 252 0.0001

ALA 252 GLY 253 -0.0016

GLY 253 THR 254 0.0000

THR 254 THR 255 0.0002

THR 255 PRO 256 -0.0002

PRO 256 LYS 257 0.0054

LYS 257 ASN 258 0.0001

ASN 258 TYR 259 -0.0003

TYR 259 ILE 260 0.0002

ILE 260 ARG 261 0.0360

ARG 261 ASN 262 -0.0001

ASN 262 ARG 263 -0.0002

ARG 263 LYS 264 -0.0000

LYS 264 LEU 265 0.0255

LEU 265 GLU 266 0.0001

GLU 266 SER 267 0.0002

SER 267 ILE 268 0.0001

ILE 268 ARG 269 0.0014

ARG 269 ALA 270 -0.0000

ALA 270 CYS 271 0.0001

CYS 271 LEU 272 -0.0002

LEU 272 ASN 273 -0.0187

ASN 273 ASP 274 0.0001

ASP 274 PRO 275 -0.0001

PRO 275 SER 276 0.0001

SER 276 ALA 277 0.0058

ALA 277 ASN 278 -0.0000

ASN 278 VAL 279 0.0004

VAL 279 ARG 280 -0.0002

ARG 280 SER 281 0.0123

SER 281 ILE 282 0.0001

ILE 282 THR 283 -0.0002

THR 283 GLU 284 -0.0003

GLU 284 ILE 285 -0.0055

ILE 285 ALA 286 0.0001

ALA 286 LEU 287 0.0001

LEU 287 ASP 288 -0.0001

ASP 288 TYR 289 -0.0638

TYR 289 GLY 290 0.0001

GLY 290 PHE 291 -0.0001

PHE 291 LEU 292 -0.0000

LEU 292 HIS 293 -0.0053

HIS 293 LEU 294 -0.0002

LEU 294 GLY 295 -0.0003

GLY 295 ARG 296 -0.0002

ARG 296 PHE 297 -0.0178

PHE 297 ALA 298 -0.0001

ALA 298 GLU 299 0.0001

GLU 299 ASN 300 -0.0001

ASN 300 TYR 301 -0.0078

TYR 301 ARG 302 -0.0000

ARG 302 SER 303 -0.0001

SER 303 ALA 304 -0.0001

ALA 304 PHE 305 0.0146

PHE 305 GLY 306 -0.0001

GLY 306 GLU 307 -0.0001

GLU 307 LEU 308 -0.0001

LEU 308 PRO 309 0.0042

PRO 309 SER 310 -0.0002

SER 310 ASP 311 0.0002

ASP 311 THR 312 -0.0001

THR 312 LEU 313 0.0137

LEU 313 ARG 314 0.0001

ARG 314 GLN 315 0.0001

GLN 315 CYS 316 -0.0001

CYS 316 LYS 317 0.0142

LYS 317 LYS 318 0.0003

LYS 318 GLU 319 -0.0001

GLU 319 VAL 320 -0.0001

VAL 320 ALA 321 0.0870

ALA 321 ASN 322 -0.0002

ASN 322 GLY 323 -0.0004

GLY 323 GLY 324 0.0003

GLY 324 SER 325 0.0074

SER 325 GLY 326 -0.0001

GLY 326 GLY 327 0.0001

GLY 327 GLY 328 -0.0004

GLY 328 SER 329 -0.0168

SER 329 GLY 330 0.0003

GLY 330 GLY 331 -0.0001

GLY 331 GLY 332 -0.0002

GLY 332 SER 333 -0.0315

SER 333 GLY 334 -0.0002

GLY 334 GLY 335 -0.0002

GLY 335 GLY 336 0.0001

GLY 336 SER 337 0.0810

SER 337 GLY 338 -0.0002

GLY 338 GLY 339 0.0002

GLY 339 GLY 340 0.0001

GLY 340 SER 341 0.0143

SER 341 GLY 342 0.0000

GLY 342 GLY 343 0.0000

GLY 343 GLY 344 -0.0004

GLY 344 SER 345 0.0046

SER 345 GLY 346 -0.0000

GLY 346 GLY 347 -0.0004

GLY 347 GLY 348 -0.0004

GLY 348 SER 349 0.0432

SER 349 GLY 350 0.0000

GLY 350 GLY 351 0.0000

GLY 351 GLY 352 -0.0000

GLY 352 SER 353 0.0239

SER 353 GLY 354 -0.0000

GLY 354 GLY 355 -0.0000

GLY 355 GLY 356 0.0004

GLY 356 SER 357 0.0006

SER 357 GLY 358 -0.0003

GLY 358 GLY 359 -0.0003

GLY 359 GLY 360 -0.0001

GLY 360 SER 361 0.0095

SER 361 GLY 362 -0.0001

GLY 362 GLY 363 0.0002

GLY 363 LEU 364 -0.0000

LEU 364 MET 365 0.0783

MET 365 ASP 366 -0.0001

ASP 366 PHE 367 0.0001

PHE 367 CYS 368 -0.0000

CYS 368 LEU 369 0.0182

LEU 369 LEU 370 -0.0004

LEU 370 ASN 371 0.0001

ASN 371 GLU 372 -0.0003

GLU 372 LYS 373 0.0398

LYS 373 SER 374 -0.0003

SER 374 GLN 375 0.0002

GLN 375 ILE 376 -0.0003

ILE 376 PHE 377 -0.0012

PHE 377 VAL 378 -0.0001

VAL 378 HIS 379 0.0001

HIS 379 ALA 380 -0.0001

ALA 380 GLU 381 0.0168

GLU 381 PRO 382 -0.0003

PRO 382 TYR 383 -0.0000

TYR 383 ALA 384 -0.0003

ALA 384 VAL 385 -0.0061

VAL 385 SER 386 -0.0001

SER 386 ASP 387 -0.0001

ASP 387 TYR 388 -0.0001

TYR 388 VAL 389 0.0276

VAL 389 ASN 390 0.0000

ASN 390 GLN 391 0.0000

GLN 391 TYR 392 0.0001

TYR 392 VAL 393 -0.0230

VAL 393 GLY 394 -0.0001

GLY 394 THR 395 -0.0001

THR 395 HIS 396 -0.0005

HIS 396 SER 397 -0.0369

SER 397 ILE 398 0.0002

ILE 398 ARG 399 0.0003

ARG 399 LEU 400 -0.0003

LEU 400 PRO 401 -0.0421

PRO 401 LYS 402 -0.0001

LYS 402 GLY 403 -0.0002

GLY 403 GLY 404 0.0003

GLY 404 ARG 405 -0.1111

ARG 405 PRO 406 0.0001

PRO 406 ALA 407 -0.0001

ALA 407 GLY 408 0.0001

GLY 408 ARG 409 0.0118

ARG 409 LEU 410 -0.0001

LEU 410 HIS 411 -0.0002

HIS 411 HIS 412 -0.0000

HIS 412 ARG 413 -0.0252

ARG 413 ILE 414 0.0000

ILE 414 PHE 415 -0.0001

PHE 415 GLY 416 0.0001

GLY 416 CYS 417 0.0183

CYS 417 LEU 418 -0.0003

LEU 418 ASP 419 0.0005

ASP 419 LEU 420 0.0003

LEU 420 CYS 421 -0.0056

CYS 421 ARG 422 0.0000

ARG 422 ILE 423 -0.0004

ILE 423 SER 424 -0.0001

SER 424 TYR 425 0.0622

TYR 425 GLY 426 0.0002

GLY 426 GLY 427 0.0002

GLY 427 SER 428 -0.0003

SER 428 VAL 429 -0.0168

VAL 429 ARG 430 0.0003

ARG 430 VAL 431 -0.0003

VAL 431 ILE 432 0.0001

ILE 432 SER 433 -0.0097

SER 433 PRO 434 -0.0002

PRO 434 GLY 435 0.0001

GLY 435 LEU 436 -0.0001

LEU 436 GLU 437 0.0125

GLU 437 THR 438 0.0000

THR 438 CYS 439 0.0003

CYS 439 TYR 440 -0.0003

TYR 440 HIS 441 -0.0134

HIS 441 LEU 442 -0.0001

LEU 442 GLN 443 0.0001

GLN 443 ILE 444 -0.0004

ILE 444 ILE 445 0.0178

ILE 445 LEU 446 -0.0001

LEU 446 LYS 447 -0.0002

LYS 447 GLY 448 0.0005

GLY 448 HIS 449 -0.0460

HIS 449 CYS 450 -0.0001

CYS 450 LEU 451 -0.0001

LEU 451 TRP 452 0.0003

TRP 452 ARG 453 -0.0100

ARG 453 GLY 454 -0.0002

GLY 454 HIS 455 -0.0000

HIS 455 GLY 456 0.0000

GLY 456 GLN 457 -0.0042

GLN 457 GLU 458 0.0002

GLU 458 HIS 459 0.0002

HIS 459 TYR 460 0.0000

TYR 460 PHE 461 -0.0188

PHE 461 ALA 462 0.0004

ALA 462 PRO 463 -0.0000

PRO 463 GLY 464 -0.0001

GLY 464 GLU 465 -0.0082

GLU 465 LEU 466 0.0001

LEU 466 LEU 467 -0.0000

LEU 467 LEU 468 -0.0001

LEU 468 LEU 469 0.0031

LEU 469 ASN 470 -0.0003

ASN 470 PRO 471 0.0002

PRO 471 ASP 472 0.0001

ASP 472 ASP 473 0.0239

ASP 473 GLN 474 0.0003

GLN 474 ALA 475 -0.0002

ALA 475 ASP 476 -0.0000

ASP 476 LEU 477 -0.0042

LEU 477 THR 478 0.0002

THR 478 TYR 479 0.0001

TYR 479 SER 480 0.0001

SER 480 GLU 481 0.0088

GLU 481 ASP 482 0.0003

ASP 482 CYS 483 -0.0003

CYS 483 GLU 484 0.0001

GLU 484 LYS 485 0.0170

LYS 485 PHE 486 -0.0004

PHE 486 ILE 487 0.0001

ILE 487 VAL 488 0.0002

VAL 488 LYS 489 -0.0270

LYS 489 LEU 490 -0.0000

LEU 490 PRO 491 0.0000

PRO 491 SER 492 0.0003

SER 492 VAL 493 0.0157

VAL 493 VAL 494 -0.0003

VAL 494 LEU 495 -0.0000

LEU 495 ASP 496 -0.0003

ASP 496 ARG 497 0.0019

ARG 497 ALA 498 -0.0001

ALA 498 CYS 499 0.0001

CYS 499 SER 500 0.0000

SER 500 ASP 501 -0.0141

ASP 501 ASN 502 -0.0002

ASN 502 ASN 503 -0.0000

ASN 503 TRP 504 -0.0002

TRP 504 HIS 505 0.0001

HIS 505 LYS 506 -0.0001

LYS 506 PRO 507 -0.0003

PRO 507 ARG 508 0.0002

ARG 508 GLU 509 -0.0203

GLU 509 GLY 510 -0.0000

GLY 510 ILE 511 -0.0001

ILE 511 ARG 512 -0.0000

ARG 512 PHE 513 -0.0112

PHE 513 ALA 514 0.0003

ALA 514 ALA 515 -0.0003

ALA 515 ARG 516 0.0002

ARG 516 HIS 517 -0.0117

HIS 517 ASN 518 -0.0001

ASN 518 LEU 519 -0.0002

LEU 519 GLN 520 0.0001

GLN 520 GLN 521 0.0382

GLN 521 LEU 522 -0.0000

LEU 522 ASP 523 0.0001

ASP 523 GLY 524 0.0002

GLY 524 PHE 525 0.0043

PHE 525 ILE 526 -0.0001

ILE 526 ASN 527 0.0002

ASN 527 LEU 528 -0.0002

LEU 528 LEU 529 0.0123

LEU 529 GLY 530 -0.0001

GLY 530 LEU 531 0.0002

LEU 531 VAL 532 -0.0001

VAL 532 CYS 533 0.0243

CYS 533 ASP 534 -0.0001

ASP 534 GLU 535 0.0001

GLU 535 ALA 536 -0.0001

ALA 536 GLU 537 0.0326

GLU 537 HIS 538 0.0001

HIS 538 THR 539 -0.0001

THR 539 LYS 540 -0.0002

LYS 540 SER 541 -0.0209

SER 541 MET 542 -0.0002

MET 542 PRO 543 0.0001

PRO 543 ARG 544 -0.0005

ARG 544 VAL 545 0.0036

VAL 545 GLN 546 -0.0001

GLN 546 GLU 547 0.0006

GLU 547 HIS 548 0.0001

HIS 548 TYR 549 -0.0091

TYR 549 ALA 550 0.0002

ALA 550 GLY 551 0.0003

GLY 551 ILE 552 0.0000

ILE 552 ILE 553 0.0037

ILE 553 ALA 554 0.0002

ALA 554 SER 555 -0.0001

SER 555 LYS 556 0.0000

LYS 556 LEU 557 0.0278

LEU 557 LEU 558 -0.0001

LEU 558 GLU 559 -0.0002

GLU 559 MET 560 -0.0001

MET 560 LEU 561 0.0105

LEU 561 GLY 562 -0.0000

GLY 562 SER 563 -0.0001

SER 563 ASN 564 -0.0004

ASN 564 VAL 565 -0.0065

VAL 565 SER 566 -0.0003

SER 566 ARG 567 -0.0002

ARG 567 GLU 568 -0.0001

GLU 568 ILE 569 -0.0041

ILE 569 PHE 570 0.0001

PHE 570 SER 571 -0.0002

SER 571 LYS 572 0.0003

LYS 572 GLY 573 0.0320

GLY 573 ASN 574 0.0001

ASN 574 PRO 575 -0.0002

PRO 575 SER 576 -0.0003

SER 576 PHE 577 0.0052

PHE 577 GLU 578 -0.0001

GLU 578 ARG 579 -0.0004

ARG 579 VAL 580 -0.0000

VAL 580 VAL 581 0.0222

VAL 581 GLN 582 -0.0001

GLN 582 PHE 583 0.0002

PHE 583 ILE 584 -0.0001

ILE 584 GLU 585 0.0343

GLU 585 GLU 586 0.0000

GLU 586 ASN 587 0.0002

ASN 587 LEU 588 0.0001

LEU 588 LYS 589 -0.0130

LYS 589 ARG 590 -0.0000

ARG 590 ASN 591 -0.0003

ASN 591 ILE 592 0.0001

ILE 592 SER 593 0.0465

SER 593 LEU 594 -0.0001

LEU 594 GLU 595 0.0005

GLU 595 ARG 596 0.0001

ARG 596 LEU 597 -0.0091

LEU 597 ALA 598 0.0002

ALA 598 GLU 599 -0.0000

GLU 599 LEU 600 0.0000

LEU 600 ALA 601 -0.0001

ALA 601 MET 602 0.0000

MET 602 MET 603 -0.0000

MET 603 SER 604 -0.0004

SER 604 PRO 605 -0.0041

PRO 605 ARG 606 0.0002

ARG 606 SER 607 -0.0000

SER 607 LEU 608 0.0001

LEU 608 TYR 609 -0.0052

TYR 609 ASN 610 -0.0001

ASN 610 LEU 611 -0.0002

LEU 611 PHE 612 0.0003

PHE 612 GLU 613 -0.0199

GLU 613 LYS 614 0.0000

LYS 614 HIS 615 -0.0000

HIS 615 ALA 616 0.0005

ALA 616 GLY 617 0.0121

GLY 617 THR 618 0.0001

THR 618 THR 619 -0.0002

THR 619 PRO 620 -0.0001

PRO 620 LYS 621 -0.0090

LYS 621 ASN 622 0.0002

ASN 622 TYR 623 0.0000

TYR 623 ILE 624 -0.0002

ILE 624 ARG 625 0.0039

ARG 625 ASN 626 -0.0002

ASN 626 ARG 627 0.0003

ARG 627 LYS 628 -0.0003

LYS 628 LEU 629 -0.0054

LEU 629 GLU 630 -0.0004

GLU 630 SER 631 0.0004

SER 631 ILE 632 -0.0001

ILE 632 ARG 633 0.0076

ARG 633 ALA 634 0.0003

ALA 634 CYS 635 -0.0002

CYS 635 LEU 636 0.0001

LEU 636 ASN 637 0.0049

ASN 637 ASP 638 0.0001

ASP 638 PRO 639 -0.0002

PRO 639 SER 640 -0.0004

SER 640 ALA 641 -0.0254

ALA 641 ASN 642 0.0002

ASN 642 VAL 643 0.0001

VAL 643 ARG 644 0.0001

ARG 644 SER 645 -0.0465

SER 645 ILE 646 0.0006

ILE 646 THR 647 0.0002

THR 647 GLU 648 0.0000

GLU 648 ILE 649 -0.0064

ILE 649 ALA 650 -0.0001

ALA 650 LEU 651 -0.0001

LEU 651 ASP 652 0.0001

ASP 652 TYR 653 -0.0103

TYR 653 GLY 654 -0.0000

GLY 654 PHE 655 -0.0000

PHE 655 LEU 656 0.0001

LEU 656 HIS 657 -0.0339

HIS 657 LEU 658 -0.0002

LEU 658 GLY 659 -0.0001

GLY 659 ARG 660 -0.0003

ARG 660 PHE 661 0.0056

PHE 661 ALA 662 0.0001

ALA 662 GLU 663 0.0002

GLU 663 ASN 664 0.0000

ASN 664 TYR 665 -0.0050

TYR 665 ARG 666 0.0003

ARG 666 SER 667 0.0000

SER 667 ALA 668 0.0002

ALA 668 PHE 669 -0.0144

PHE 669 GLY 670 -0.0000

GLY 670 GLU 671 0.0005

GLU 671 LEU 672 0.0001

LEU 672 PRO 673 -0.0002

PRO 673 SER 674 -0.0003

SER 674 ASP 675 -0.0000

ASP 675 THR 676 0.0001

THR 676 LEU 677 -0.0077

LEU 677 ARG 678 0.0002

ARG 678 GLN 679 -0.0003

GLN 679 CYS 680 0.0002

CYS 680 LYS 681 0.0009

LYS 681 LYS 682 0.0000

LYS 682 GLU 683 0.0002

GLU 683 VAL 684 0.0001

VAL 684 ALA 685 -0.0019

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.

*** NMA_rosettafold_2round(rank4) ***

CA strain for 2403040904371504613

--- normal mode 11 ---

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

* NMA_rosettafold_2round(rank4) *