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* AtTPS1_Modelo_sin_Cterminal_sin_NHterminal *

CA strain for 261012135337721839

--- 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
GLN 1 ARG 2 0.0000

ARG 2 LEU 3 0.0003

LEU 3 LEU 4 0.0002

LEU 4 VAL 5 -0.0004

VAL 5 VAL 6 0.0001

VAL 6 ALA 7 0.0001

ALA 7 ASN 8 0.0001

ASN 8 ARG 9 -0.0016

ARG 9 LEU 10 -0.0001

LEU 10 PRO 11 0.0001

PRO 11 VAL 12 -0.0000

VAL 12 SER 13 0.0017

SER 13 ALA 14 0.0001

ALA 14 VAL 15 0.0002

VAL 15 ARG 16 -0.0004

ARG 16 ARG 17 -0.0003

ARG 17 GLY 18 0.0001

GLY 18 GLU 19 -0.0004

GLU 19 ASP 20 -0.0001

ASP 20 SER 21 0.0009

SER 21 TRP 22 -0.0002

TRP 22 SER 23 0.0002

SER 23 LEU 24 -0.0003

LEU 24 GLU 25 0.0016

GLU 25 ILE 26 -0.0001

ILE 26 SER 27 0.0002

SER 27 ALA 28 -0.0001

ALA 28 GLY 29 0.0006

GLY 29 GLY 30 0.0000

GLY 30 LEU 31 -0.0003

LEU 31 VAL 32 -0.0002

VAL 32 SER 33 -0.0027

SER 33 ALA 34 0.0005

ALA 34 LEU 35 -0.0003

LEU 35 LEU 36 0.0002

LEU 36 GLY 37 -0.0024

GLY 37 VAL 38 0.0002

VAL 38 LYS 39 0.0001

LYS 39 GLU 40 -0.0000

GLU 40 PHE 41 -0.0007

PHE 41 GLU 42 -0.0004

GLU 42 ALA 43 -0.0003

ALA 43 ARG 44 0.0001

ARG 44 TRP 45 0.0006

TRP 45 ILE 46 0.0001

ILE 46 GLY 47 -0.0002

GLY 47 TRP 48 0.0000

TRP 48 ALA 49 -0.0011

ALA 49 GLY 50 -0.0002

GLY 50 VAL 51 0.0002

VAL 51 ASN 52 -0.0001

ASN 52 VAL 53 -0.0008

VAL 53 PRO 54 0.0000

PRO 54 ASP 55 -0.0002

ASP 55 GLU 56 0.0001

GLU 56 VAL 57 0.0007

VAL 57 GLY 58 -0.0003

GLY 58 GLN 59 0.0004

GLN 59 LYS 60 -0.0000

LYS 60 ALA 61 0.0002

ALA 61 LEU 62 0.0001

LEU 62 SER 63 -0.0001

SER 63 LYS 64 0.0003

LYS 64 ALA 65 -0.0003

ALA 65 LEU 66 -0.0001

LEU 66 ALA 67 -0.0000

ALA 67 GLU 68 0.0003

GLU 68 LYS 69 0.0017

LYS 69 ARG 70 -0.0001

ARG 70 CYS 71 -0.0003

CYS 71 ILE 72 0.0001

ILE 72 PRO 73 0.0000

PRO 73 VAL 74 -0.0002

VAL 74 PHE 75 0.0001

PHE 75 LEU 76 0.0001

LEU 76 ASP 77 0.0016

ASP 77 GLU 78 -0.0000

GLU 78 GLU 79 -0.0002

GLU 79 ILE 80 -0.0002

ILE 80 VAL 81 0.0016

VAL 81 HIS 82 -0.0003

HIS 82 GLN 83 -0.0002

GLN 83 TYR 84 0.0001

TYR 84 TYR 85 0.0010

TYR 85 ASN 86 0.0004

ASN 86 GLY 87 -0.0001

GLY 87 TYR 88 -0.0000

TYR 88 CYS 89 -0.0004

CYS 89 ASN 90 0.0000

ASN 90 ASN 91 0.0001

ASN 91 ILE 92 -0.0001

ILE 92 LEU 93 -0.0006

LEU 93 TRP 94 0.0002

TRP 94 PRO 95 -0.0004

PRO 95 LEU 96 0.0003

LEU 96 PHE 97 -0.0004

PHE 97 HIS 98 -0.0002

HIS 98 TYR 99 0.0003

TYR 99 LEU 100 -0.0002

LEU 100 GLY 101 -0.0015

GLY 101 LEU 102 -0.0001

LEU 102 PRO 103 -0.0003

PRO 103 GLN 104 0.0000

GLN 104 GLU 105 -0.0029

GLU 105 ASP 106 -0.0001

ASP 106 ARG 107 -0.0001

ARG 107 LEU 108 0.0002

LEU 108 ALA 109 0.0012

ALA 109 THR 110 0.0003

THR 110 THR 111 -0.0003

THR 111 ARG 112 0.0003

ARG 112 SER 113 0.0006

SER 113 PHE 114 0.0000

PHE 114 GLN 115 0.0004

GLN 115 SER 116 -0.0000

SER 116 GLN 117 0.0019

GLN 117 PHE 118 0.0003

PHE 118 ALA 119 0.0001

ALA 119 ALA 120 0.0002

ALA 120 TYR 121 0.0027

TYR 121 LYS 122 0.0002

LYS 122 LYS 123 -0.0003

LYS 123 ALA 124 0.0003

ALA 124 ASN 125 0.0039

ASN 125 GLN 126 -0.0004

GLN 126 MET 127 -0.0001

MET 127 PHE 128 0.0002

PHE 128 ALA 129 0.0028

ALA 129 ASP 130 -0.0002

ASP 130 VAL 131 0.0003

VAL 131 VAL 132 -0.0001

VAL 132 ASN 133 0.0013

ASN 133 GLU 134 0.0004

GLU 134 HIS 135 0.0003

HIS 135 TYR 136 -0.0001

TYR 136 GLU 137 0.0008

GLU 137 GLU 138 -0.0002

GLU 138 GLY 139 0.0005

GLY 139 ASP 140 -0.0000

ASP 140 VAL 141 0.0005

VAL 141 VAL 142 -0.0000

VAL 142 TRP 143 -0.0003

TRP 143 CYS 144 0.0005

CYS 144 HIS 145 0.0004

HIS 145 ASP 146 -0.0001

ASP 146 TYR 147 -0.0003

TYR 147 HIS 148 -0.0001

HIS 148 LEU 149 0.0017

LEU 149 MET 150 0.0001

MET 150 PHE 151 -0.0000

PHE 151 LEU 152 -0.0001

LEU 152 PRO 153 0.0048

PRO 153 LYS 154 -0.0002

LYS 154 CYS 155 -0.0001

CYS 155 LEU 156 -0.0000

LEU 156 LYS 157 0.0045

LYS 157 GLU 158 0.0001

GLU 158 TYR 159 -0.0004

TYR 159 ASN 160 0.0002

ASN 160 SER 161 0.0013

SER 161 LYS 162 0.0001

LYS 162 MET 163 0.0001

MET 163 LYS 164 -0.0003

LYS 164 VAL 165 0.0005

VAL 165 GLY 166 -0.0002

GLY 166 TRP 167 -0.0001

TRP 167 PHE 168 -0.0001

PHE 168 LEU 169 -0.0002

LEU 169 HIS 170 0.0000

HIS 170 THR 171 -0.0005

THR 171 PRO 172 0.0007

PRO 172 PHE 173 0.0059

PHE 173 PRO 174 -0.0001

PRO 174 SER 175 -0.0002

SER 175 SER 176 0.0003

SER 176 GLU 177 0.0003

GLU 177 ILE 178 0.0004

ILE 178 HIS 179 -0.0004

HIS 179 ARG 180 -0.0000

ARG 180 THR 181 -0.0061

THR 181 LEU 182 -0.0005

LEU 182 PRO 183 -0.0002

PRO 183 SER 184 -0.0000

SER 184 ARG 185 -0.0143

ARG 185 SER 186 -0.0001

SER 186 GLU 187 0.0002

GLU 187 LEU 188 -0.0000

LEU 188 LEU 189 0.0007

LEU 189 ARG 190 0.0002

ARG 190 SER 191 -0.0001

SER 191 VAL 192 -0.0001

VAL 192 LEU 193 0.0147

LEU 193 ALA 194 0.0001

ALA 194 ALA 195 -0.0001

ALA 195 ASP 196 -0.0002

ASP 196 LEU 197 -0.0005

LEU 197 VAL 198 0.0001

VAL 198 GLY 199 -0.0000

GLY 199 PHE 200 0.0001

PHE 200 HIS 201 -0.0010

HIS 201 THR 202 -0.0002

THR 202 TYR 203 -0.0001

TYR 203 ASP 204 -0.0001

ASP 204 TYR 205 -0.0025

TYR 205 ALA 206 0.0003

ALA 206 ARG 207 -0.0000

ARG 207 HIS 208 -0.0001

HIS 208 PHE 209 -0.0049

PHE 209 VAL 210 -0.0002

VAL 210 SER 211 -0.0000

SER 211 ALA 212 0.0003

ALA 212 CYS 213 0.0115

CYS 213 THR 214 -0.0000

THR 214 ARG 215 -0.0001

ARG 215 ILE 216 0.0000

ILE 216 LEU 217 0.0127

LEU 217 GLY 218 0.0000

GLY 218 LEU 219 -0.0001

LEU 219 GLU 220 0.0002

GLU 220 GLY 221 -0.0143

GLY 221 THR 222 0.0002

THR 222 PRO 223 -0.0001

PRO 223 GLU 224 0.0003

GLU 224 GLY 225 -0.0318

GLY 225 VAL 226 0.0003

VAL 226 GLU 227 -0.0002

GLU 227 ASP 228 0.0005

ASP 228 GLN 229 0.0062

GLN 229 GLY 230 -0.0002

GLY 230 ARG 231 0.0001

ARG 231 LEU 232 0.0001

LEU 232 THR 233 0.0011

THR 233 ARG 234 -0.0001

ARG 234 VAL 235 0.0000

VAL 235 ALA 236 0.0002

ALA 236 ALA 237 0.0060

ALA 237 PHE 238 0.0001

PHE 238 PRO 239 0.0002

PRO 239 ILE 240 -0.0000

ILE 240 GLY 241 0.0066

GLY 241 ILE 242 -0.0002

ILE 242 ASP 243 0.0001

ASP 243 SER 244 0.0003

SER 244 ASP 245 0.0030

ASP 245 ARG 246 -0.0001

ARG 246 PHE 247 -0.0001

PHE 247 ILE 248 -0.0003

ILE 248 ARG 249 0.0019

ARG 249 ALA 250 0.0000

ALA 250 LEU 251 0.0000

LEU 251 GLU 252 -0.0001

GLU 252 VAL 253 0.0003

VAL 253 PRO 254 -0.0001

PRO 254 GLU 255 -0.0001

GLU 255 VAL 256 -0.0002

VAL 256 ILE 257 -0.0006

ILE 257 GLN 258 -0.0002

GLN 258 HIS 259 0.0001

HIS 259 MET 260 0.0003

MET 260 LYS 261 -0.0002

LYS 261 GLU 262 0.0003

GLU 262 LEU 263 0.0001

LEU 263 LYS 264 -0.0001

LYS 264 GLU 265 -0.0002

GLU 265 ARG 266 0.0001

ARG 266 PHE 267 0.0001

PHE 267 ALA 268 0.0000

ALA 268 GLY 269 0.0011

GLY 269 ARG 270 -0.0000

ARG 270 LYS 271 -0.0003

LYS 271 VAL 272 0.0001

VAL 272 MET 273 0.0009

MET 273 LEU 274 -0.0003

LEU 274 GLY 275 -0.0001

GLY 275 VAL 276 0.0001

VAL 276 ASP 277 -0.0028

ASP 277 ARG 278 -0.0003

ARG 278 LEU 279 0.0002

LEU 279 ASP 280 -0.0002

ASP 280 MET 281 0.0001

MET 281 ILE 282 0.0002

ILE 282 LYS 283 0.0003

LYS 283 GLY 284 -0.0002

GLY 284 ILE 285 0.0007

ILE 285 PRO 286 0.0003

PRO 286 GLN 287 -0.0005

GLN 287 LYS 288 0.0002

LYS 288 ILE 289 0.0010

ILE 289 LEU 290 0.0002

LEU 290 ALA 291 0.0002

ALA 291 PHE 292 0.0000

PHE 292 GLU 293 -0.0001

GLU 293 LYS 294 -0.0002

LYS 294 PHE 295 0.0003

PHE 295 LEU 296 0.0003

LEU 296 GLU 297 -0.0002

GLU 297 GLU 298 0.0000

GLU 298 ASN 299 0.0001

ASN 299 ALA 300 -0.0001

ALA 300 ASN 301 0.0001

ASN 301 TRP 302 0.0002

TRP 302 ARG 303 -0.0006

ARG 303 ASP 304 -0.0001

ASP 304 LYS 305 0.0002

LYS 305 VAL 306 0.0000

VAL 306 VAL 307 0.0001

VAL 307 LEU 308 -0.0001

LEU 308 LEU 309 -0.0009

LEU 309 GLN 310 -0.0003

GLN 310 ILE 311 0.0002

ILE 311 ALA 312 -0.0001

ALA 312 VAL 313 -0.0025

VAL 313 PRO 314 -0.0001

PRO 314 THR 315 -0.0000

THR 315 ARG 316 -0.0001

ARG 316 THR 317 0.0023

THR 317 ASP 318 0.0001

ASP 318 VAL 319 -0.0000

VAL 319 PRO 320 -0.0000

PRO 320 GLU 321 0.0003

GLU 321 TYR 322 -0.0001

TYR 322 GLN 323 0.0002

GLN 323 LYS 324 0.0002

LYS 324 LEU 325 -0.0001

LEU 325 THR 326 -0.0003

THR 326 SER 327 0.0004

SER 327 GLN 328 0.0000

GLN 328 VAL 329 0.0000

VAL 329 HIS 330 -0.0001

HIS 330 GLU 331 0.0001

GLU 331 ILE 332 0.0000

ILE 332 VAL 333 0.0001

VAL 333 GLY 334 -0.0002

GLY 334 ARG 335 -0.0000

ARG 335 ILE 336 -0.0002

ILE 336 ASN 337 0.0000

ASN 337 GLY 338 0.0001

GLY 338 ARG 339 -0.0001

ARG 339 PHE 340 -0.0001

PHE 340 GLY 341 -0.0001

GLY 341 THR 342 -0.0003

THR 342 LEU 343 -0.0001

LEU 343 THR 344 0.0002

THR 344 ALA 345 0.0005

ALA 345 VAL 346 0.0001

VAL 346 PRO 347 -0.0001

PRO 347 ILE 348 0.0000

ILE 348 HIS 349 -0.0009

HIS 349 HIS 350 -0.0002

HIS 350 LEU 351 -0.0001

LEU 351 ASP 352 0.0002

ASP 352 ARG 353 -0.0003

ARG 353 SER 354 -0.0002

SER 354 LEU 355 0.0001

LEU 355 ASP 356 -0.0002

ASP 356 PHE 357 0.0029

PHE 357 HIS 358 0.0003

HIS 358 ALA 359 -0.0002

ALA 359 LEU 360 -0.0001

LEU 360 CYS 361 -0.0003

CYS 361 ALA 362 0.0001

ALA 362 LEU 363 0.0001

LEU 363 TYR 364 0.0003

TYR 364 ALA 365 -0.0000

ALA 365 VAL 366 -0.0002

VAL 366 THR 367 0.0000

THR 367 ASP 368 -0.0001

ASP 368 VAL 369 0.0021

VAL 369 ALA 370 -0.0002

ALA 370 LEU 371 0.0001

LEU 371 VAL 372 0.0001

VAL 372 THR 373 0.0020

THR 373 SER 374 -0.0002

SER 374 LEU 375 0.0001

LEU 375 ARG 376 0.0004

ARG 376 ASP 377 -0.0005

ASP 377 GLY 378 -0.0000

GLY 378 MET 379 -0.0002

MET 379 ASN 380 0.0002

ASN 380 LEU 381 0.0019

LEU 381 VAL 382 -0.0001

VAL 382 SER 383 0.0004

SER 383 TYR 384 0.0000

TYR 384 GLU 385 0.0021

GLU 385 PHE 386 0.0003

PHE 386 VAL 387 -0.0001

VAL 387 ALA 388 -0.0001

ALA 388 CYS 389 0.0004

CYS 389 GLN 390 0.0001

GLN 390 GLU 391 0.0001

GLU 391 ALA 392 -0.0001

ALA 392 LYS 393 -0.0004

LYS 393 LYS 394 -0.0000

LYS 394 GLY 395 -0.0002

GLY 395 VAL 396 0.0003

VAL 396 LEU 397 0.0026

LEU 397 ILE 398 0.0000

ILE 398 LEU 399 0.0001

LEU 399 SER 400 -0.0002

SER 400 GLU 401 0.0010

GLU 401 PHE 402 0.0004

PHE 402 ALA 403 -0.0000

ALA 403 GLY 404 -0.0000

GLY 404 ALA 405 0.0042

ALA 405 ALA 406 0.0002

ALA 406 GLN 407 -0.0001

GLN 407 SER 408 0.0000

SER 408 LEU 409 0.0041

LEU 409 GLY 410 0.0002

GLY 410 ALA 411 0.0004

ALA 411 GLY 412 -0.0001

GLY 412 ALA 413 -0.0006

ALA 413 ILE 414 -0.0004

ILE 414 LEU 415 -0.0000

LEU 415 VAL 416 0.0002

VAL 416 ASN 417 0.0008

ASN 417 PRO 418 -0.0001

PRO 418 TRP 419 -0.0002

TRP 419 ASN 420 0.0001

ASN 420 ILE 421 -0.0007

ILE 421 THR 422 0.0002

THR 422 GLU 423 0.0000

GLU 423 VAL 424 0.0001

VAL 424 ALA 425 0.0010

ALA 425 ALA 426 0.0004

ALA 426 SER 427 -0.0003

SER 427 ILE 428 -0.0000

ILE 428 GLY 429 0.0003

GLY 429 GLN 430 -0.0000

GLN 430 ALA 431 0.0000

ALA 431 LEU 432 -0.0001

LEU 432 ASN 433 0.0001

ASN 433 MET 434 0.0001

MET 434 THR 435 -0.0001

THR 435 ALA 436 0.0002

ALA 436 GLU 437 0.0003

GLU 437 GLU 438 -0.0003

GLU 438 ARG 439 0.0003

ARG 439 GLU 440 -0.0001

GLU 440 LYS 441 0.0005

LYS 441 ARG 442 -0.0001

ARG 442 HIS 443 0.0002

HIS 443 ARG 444 0.0001

ARG 444 HIS 445 0.0012

HIS 445 ASN 446 0.0000

ASN 446 PHE 447 0.0001

PHE 447 HIS 448 -0.0001

HIS 448 HIS 449 0.0011

HIS 449 VAL 450 -0.0002

VAL 450 LYS 451 0.0002

LYS 451 THR 452 -0.0001

THR 452 HIS 453 0.0006

HIS 453 THR 454 -0.0001

THR 454 ALA 455 0.0004

ALA 455 GLN 456 0.0002

GLN 456 GLU 457 0.0041

GLU 457 TRP 458 0.0000

TRP 458 ALA 459 -0.0003

ALA 459 GLU 460 0.0002

GLU 460 THR 461 0.0042

THR 461 PHE 462 0.0002

PHE 462 VAL 463 -0.0003

VAL 463 SER 464 0.0001

SER 464 GLU 465 0.0055

GLU 465 LEU 466 -0.0001

LEU 466 ASN 467 -0.0002

ASN 467 ASP 468 -0.0000

ASP 468 THR 469 0.0040

THR 469 VAL 470 0.0000

VAL 470 ILE 471 0.0001

ILE 471 GLU 472 -0.0002

GLU 472 ALA 473 0.0030

ALA 473 GLN 474 -0.0001

GLN 474 LEU 475 0.0003

LEU 475 ARG 476 -0.0001

ARG 476 ILE 477 -0.0233

ILE 477 SER 478 -0.0003

SER 478 LYS 479 0.0005

LYS 479 VAL 480 0.0002

VAL 480 PRO 481 0.0066

PRO 481 PRO 482 0.0002

PRO 482 GLU 483 -0.0003

GLU 483 LEU 484 0.0000

LEU 484 PRO 485 -0.0371

PRO 485 GLN 486 -0.0001

GLN 486 HIS 487 -0.0001

HIS 487 ASP 488 0.0002

ASP 488 ALA 489 0.0043

ALA 489 ILE 490 -0.0001

ILE 490 GLN 491 0.0001

GLN 491 ARG 492 -0.0001

ARG 492 TYR 493 -0.0004

TYR 493 SER 494 0.0001

SER 494 LYS 495 -0.0002

LYS 495 SER 496 0.0001

SER 496 ASN 497 -0.0010

ASN 497 ASN 498 -0.0001

ASN 498 ARG 499 -0.0002

ARG 499 LEU 500 0.0003

LEU 500 LEU 501 0.0020

LEU 501 ILE 502 0.0004

ILE 502 LEU 503 -0.0005

LEU 503 GLY 504 -0.0000

GLY 504 PHE 505 -0.0001

PHE 505 ASN 506 -0.0001

ASN 506 ALA 507 -0.0001

ALA 507 THR 508 -0.0001

THR 508 LEU 509 -0.0049

LEU 509 THR 510 0.0005

THR 510 GLU 511 -0.0000

GLU 511 PRO 512 -0.0002

PRO 512 VAL 513 0.0556

VAL 513 ASP 514 0.0001

ASP 514 ASN 515 -0.0001

ASN 515 GLN 516 -0.0005

GLN 516 GLY 517 -0.0283

GLY 517 ARG 518 0.0000

ARG 518 ARG 519 -0.0002

ARG 519 GLY 520 0.0000

GLY 520 ASP 521 -0.0644

ASP 521 GLN 522 0.0003

GLN 522 ILE 523 0.0000

ILE 523 LYS 524 0.0000

LYS 524 GLU 525 0.0095

GLU 525 MET 526 -0.0001

MET 526 ASP 527 -0.0000

ASP 527 LEU 528 0.0004

LEU 528 ASN 529 0.0091

ASN 529 LEU 530 -0.0000

LEU 530 HIS 531 -0.0001

HIS 531 PRO 532 -0.0000

PRO 532 GLU 533 0.0089

GLU 533 LEU 534 0.0002

LEU 534 LYS 535 -0.0003

LYS 535 GLY 536 0.0002

GLY 536 PRO 537 0.0018

PRO 537 LEU 538 0.0003

LEU 538 LYS 539 0.0001

LYS 539 ALA 540 0.0002

ALA 540 LEU 541 -0.0019

LEU 541 CYS 542 -0.0003

CYS 542 SER 543 0.0000

SER 543 ASP 544 0.0003

ASP 544 PRO 545 0.0045

PRO 545 SER 546 0.0000

SER 546 THR 547 0.0001

THR 547 THR 548 0.0002

THR 548 ILE 549 0.0006

ILE 549 VAL 550 -0.0001

VAL 550 VAL 551 0.0000

VAL 551 LEU 552 -0.0000

LEU 552 SER 553 0.0030

SER 553 GLY 554 -0.0002

GLY 554 SER 555 0.0001

SER 555 SER 556 -0.0003

SER 556 ARG 557 0.0045

ARG 557 SER 558 -0.0001

SER 558 VAL 559 -0.0001

VAL 559 LEU 560 0.0001

LEU 560 ASP 561 0.0019

ASP 561 LYS 562 0.0003

LYS 562 ASN 563 0.0004

ASN 563 PHE 564 -0.0000

PHE 564 GLY 565 -0.0008

GLY 565 GLU 566 -0.0001

GLU 566 TYR 567 -0.0001

TYR 567 ASP 568 -0.0000

ASP 568 MET 569 -0.0004

MET 569 TRP 570 0.0001

TRP 570 LEU 571 -0.0003

LEU 571 ALA 572 -0.0000

ALA 572 ALA 573 0.0015

ALA 573 GLU 574 -0.0000

GLU 574 ASN 575 -0.0000

ASN 575 GLY 576 -0.0002

GLY 576 MET 577 0.0007

MET 577 PHE 578 0.0002

PHE 578 LEU 579 -0.0001

LEU 579 ARG 580 -0.0003

ARG 580 LEU 581 -0.0007

LEU 581 THR 582 -0.0001

THR 582 ASN 583 -0.0003

ASN 583 GLY 584 0.0002

GLY 584 GLU 585 0.0011

GLU 585 TRP 586 0.0001

TRP 586 MET 587 0.0000

MET 587 THR 588 0.0002

THR 588 THR 589 -0.0001

THR 589 MET 590 -0.0001

MET 590 PRO 591 0.0003

PRO 591 GLU 592 -0.0002

GLU 592 HIS 593 0.0005

HIS 593 LEU 594 0.0002

LEU 594 ASN 595 -0.0000

ASN 595 MET 596 -0.0004

MET 596 GLU 597 -0.0031

GLU 597 TRP 598 0.0001

TRP 598 VAL 599 -0.0001

VAL 599 ASP 600 0.0000

ASP 600 SER 601 0.0013

SER 601 VAL 602 -0.0000

VAL 602 LYS 603 0.0002

LYS 603 HIS 604 -0.0001

HIS 604 VAL 605 0.0013

VAL 605 PHE 606 -0.0002

PHE 606 LYS 607 -0.0001

LYS 607 TYR 608 -0.0001

TYR 608 PHE 609 0.0003

PHE 609 THR 610 0.0004

THR 610 GLU 611 -0.0004

GLU 611 ARG 612 -0.0000

ARG 612 THR 613 -0.0018

THR 613 PRO 614 -0.0003

PRO 614 ARG 615 0.0002

ARG 615 SER 616 -0.0003

SER 616 HIS 617 -0.0084

HIS 617 PHE 618 -0.0002

PHE 618 GLU 619 0.0001

GLU 619 THR 620 -0.0003

THR 620 ARG 621 -0.0015

ARG 621 ASP 622 -0.0001

ASP 622 THR 623 -0.0001

THR 623 SER 624 0.0002

SER 624 LEU 625 -0.0002

LEU 625 ILE 626 -0.0001

ILE 626 TRP 627 -0.0002

TRP 627 ASN 628 -0.0001

ASN 628 TYR 629 0.0029

TYR 629 LYS 630 -0.0002

LYS 630 TYR 631 0.0002

TYR 631 ALA 632 0.0000

ALA 632 ASP 633 -0.0063

ASP 633 ILE 634 0.0001

ILE 634 GLU 635 -0.0003

GLU 635 PHE 636 0.0001

PHE 636 GLY 637 0.0023

GLY 637 ARG 638 0.0002

ARG 638 LEU 639 0.0000

LEU 639 GLN 640 -0.0000

GLN 640 ALA 641 -0.0263

ALA 641 ARG 642 0.0003

ARG 642 ASP 643 -0.0003

ASP 643 LEU 644 -0.0001

LEU 644 LEU 645 -0.0032

LEU 645 GLN 646 -0.0001

GLN 646 HIS 647 0.0002

HIS 647 LEU 648 -0.0001

LEU 648 TRP 649 -0.0023

TRP 649 THR 650 0.0001

THR 650 GLY 651 0.0000

GLY 651 PRO 652 0.0002

PRO 652 ILE 653 -0.0023

ILE 653 SER 654 0.0000

SER 654 ASN 655 -0.0001

ASN 655 ALA 656 0.0000

ALA 656 SER 657 -0.0021

SER 657 VAL 658 0.0000

VAL 658 ASP 659 0.0001

ASP 659 VAL 660 0.0000

VAL 660 VAL 661 0.0153

VAL 661 GLN 662 -0.0004

GLN 662 GLY 663 0.0001

GLY 663 SER 664 -0.0001

SER 664 ARG 665 0.0303

ARG 665 SER 666 -0.0000

SER 666 VAL 667 -0.0002

VAL 667 GLU 668 0.0003

GLU 668 VAL 669 0.0019

VAL 669 ARG 670 -0.0000

ARG 670 ALA 671 -0.0000

ALA 671 VAL 672 0.0000

VAL 672 GLY 673 -0.0088

GLY 673 VAL 674 -0.0002

VAL 674 THR 675 -0.0000

THR 675 LYS 676 0.0001

LYS 676 GLY 677 0.0001

GLY 677 ALA 678 0.0002

ALA 678 ALA 679 -0.0001

ALA 679 ILE 680 0.0001

ILE 680 ASP 681 0.0014

ASP 681 ARG 682 0.0002

ARG 682 ILE 683 -0.0001

ILE 683 LEU 684 0.0002

LEU 684 GLY 685 0.0042

GLY 685 GLU 686 -0.0001

GLU 686 ILE 687 -0.0000

ILE 687 VAL 688 -0.0002

VAL 688 HIS 689 0.0015

HIS 689 SER 690 -0.0002

SER 690 LYS 691 -0.0000

LYS 691 SER 692 -0.0000

SER 692 MET 693 -0.0010

MET 693 THR 694 0.0001

THR 694 THR 695 -0.0002

THR 695 PRO 696 -0.0001

PRO 696 ILE 697 0.0041

ILE 697 ASP 698 -0.0001

ASP 698 TYR 699 0.0001

TYR 699 VAL 700 0.0001

VAL 700 LEU 701 0.0003

LEU 701 CYS 702 0.0001

CYS 702 ILE 703 -0.0000

ILE 703 GLY 704 -0.0002

GLY 704 HIS 705 0.0057

HIS 705 PHE 706 0.0001

PHE 706 LEU 707 -0.0003

LEU 707 GLY 708 0.0001

GLY 708 LYS 709 0.0005

LYS 709 ASP 710 -0.0000

ASP 710 GLU 711 -0.0001

GLU 711 ASP 712 -0.0000

ASP 712 VAL 713 0.0006

VAL 713 TYR 714 0.0002

TYR 714 THR 715 0.0000

THR 715 PHE 716 -0.0000

PHE 716 PHE 717 -0.0013

PHE 717 GLU 718 -0.0002

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** AtTPS1_Modelo_sin_Cterminal_sin_NHterminal ***

CA strain for 261012135337721839

--- normal mode 8 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* AtTPS1_Modelo_sin_Cterminal_sin_NHterminal *