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

* Phrb Pseudomonas fluorescens model 5 *

CA strain for 221006205537110470

--- normal mode 14 ---

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 GLN 2 0.0000

GLN 2 LEU 3 0.0000

LEU 3 ILE 4 0.0370

ILE 4 TRP 5 -0.0001

TRP 5 LEU 6 -0.0004

LEU 6 ARG 7 -0.0095

ARG 7 SER 8 -0.0001

SER 8 ASP 9 -0.0003

ASP 9 LEU 10 -0.0867

LEU 10 ARG 11 0.0002

ARG 11 VAL 12 0.0000

VAL 12 HIS 13 0.0165

HIS 13 ASP 14 0.0002

ASP 14 ASN 15 0.0003

ASN 15 THR 16 0.0035

THR 16 ALA 17 -0.0001

ALA 17 LEU 18 0.0000

LEU 18 SER 19 -0.0095

SER 19 ALA 20 -0.0000

ALA 20 ALA 21 0.0003

ALA 21 ALA 22 -0.0482

ALA 22 VAL 23 0.0003

VAL 23 ARG 24 -0.0001

ARG 24 GLY 25 -0.0143

GLY 25 PRO 26 -0.0003

PRO 26 CYS 27 -0.0003

CYS 27 VAL 28 -0.0148

VAL 28 ALA 29 0.0003

ALA 29 VAL 30 0.0003

VAL 30 TYR 31 0.0703

TYR 31 LEU 32 0.0002

LEU 32 LEU 33 -0.0001

LEU 33 SER 34 -0.0768

SER 34 PRO 35 -0.0000

PRO 35 ALA 36 -0.0001

ALA 36 GLN 37 -0.0185

GLN 37 TRP 38 0.0001

TRP 38 LEU 39 -0.0003

LEU 39 ALA 40 -0.0372

ALA 40 HIS 41 -0.0000

HIS 41 ASP 42 -0.0001

ASP 42 ASP 43 -0.0104

ASP 43 ALA 44 -0.0003

ALA 44 PRO 45 -0.0000

PRO 45 CYS 46 -0.0273

CYS 46 LYS 47 -0.0001

LYS 47 VAL 48 0.0003

VAL 48 ASP 49 0.0149

ASP 49 PHE 50 -0.0002

PHE 50 TRP 51 -0.0003

TRP 51 LEU 52 -0.0198

LEU 52 ARG 53 -0.0001

ARG 53 ASN 54 -0.0002

ASN 54 LEU 55 0.1934

LEU 55 ARG 56 0.0001

ARG 56 ASP 57 0.0002

ASP 57 LEU 58 -0.0205

LEU 58 SER 59 0.0000

SER 59 GLN 60 -0.0000

GLN 60 THR 61 -0.0269

THR 61 LEU 62 0.0001

LEU 62 ALA 63 0.0002

ALA 63 ARG 64 -0.0619

ARG 64 LEU 65 -0.0001

LEU 65 ASN 66 -0.0002

ASN 66 ILE 67 -0.0754

ILE 67 PRO 68 -0.0002

PRO 68 LEU 69 0.0000

LEU 69 LEU 70 -0.0024

LEU 70 ILE 71 0.0003

ILE 71 ARG 72 -0.0002

ARG 72 GLU 73 -0.1772

GLU 73 ALA 74 0.0001

ALA 74 SER 75 0.0000

SER 75 HIS 76 -0.0933

HIS 76 TRP 77 -0.0001

TRP 77 ASP 78 -0.0003

ASP 78 ASP 79 -0.1026

ASP 79 ALA 80 0.0002

ALA 80 PRO 81 0.0002

PRO 81 ARG 82 -0.0876

ARG 82 VAL 83 -0.0000

VAL 83 LEU 84 -0.0001

LEU 84 ALA 85 0.0574

ALA 85 GLY 86 0.0001

GLY 86 LEU 87 -0.0003

LEU 87 CYS 88 0.0827

CYS 88 ASP 89 0.0002

ASP 89 GLU 90 0.0001

GLU 90 LEU 91 0.0006

LEU 91 GLY 92 0.0001

GLY 92 VAL 93 -0.0002

VAL 93 GLU 94 -0.0205

GLU 94 ALA 95 0.0000

ALA 95 VAL 96 0.0002

VAL 96 HIS 97 -0.0868

HIS 97 ALA 98 0.0001

ALA 98 ASN 99 0.0000

ASN 99 ASP 100 -0.1227

ASP 100 GLU 101 0.0001

GLU 101 TYR 102 -0.0002

TYR 102 GLY 103 0.1779

GLY 103 VAL 104 0.0004

VAL 104 HIS 105 -0.0001

HIS 105 GLU 106 0.0578

GLU 106 THR 107 0.0004

THR 107 ARG 108 -0.0001

ARG 108 ARG 109 -0.2469

ARG 109 ASP 110 0.0000

ASP 110 ALA 111 0.0003

ALA 111 ALA 112 -0.0721

ALA 112 VAL 113 -0.0005

VAL 113 ARG 114 -0.0003

ARG 114 GLN 115 0.0088

GLN 115 ALA 116 0.0002

ALA 116 LEU 117 -0.0003

LEU 117 GLU 118 0.0790

GLU 118 THR 119 0.0001

THR 119 ALA 120 0.0000

ALA 120 GLY 121 -0.0697

GLY 121 ILE 122 0.0000

ILE 122 ALA 123 -0.0000

ALA 123 TRP 124 -0.1385

TRP 124 HIS 125 -0.0002

HIS 125 ASN 126 -0.0001

ASN 126 TYR 127 -0.3813

TYR 127 LEU 128 0.0001

LEU 128 ASP 129 -0.0002

ASP 129 GLN 130 -0.0298

GLN 130 LEU 131 0.0002

LEU 131 LEU 132 0.0000

LEU 132 PHE 133 0.1115

PHE 133 GLN 134 0.0001

GLN 134 PRO 135 0.0000

PRO 135 GLY 136 -0.1389

GLY 136 SER 137 0.0003

SER 137 VAL 138 -0.0000

VAL 138 LEU 139 -0.0498

LEU 139 THR 140 0.0002

THR 140 ARG 141 0.0000

ARG 141 THR 142 0.0818

THR 142 GLY 143 -0.0001

GLY 143 THR 144 -0.0001

THR 144 TYR 145 -0.0630

TYR 145 PHE 146 0.0002

PHE 146 GLN 147 -0.0003

GLN 147 VAL 148 -0.1021

VAL 148 PHE 149 -0.0003

PHE 149 SER 150 0.0001

SER 150 GLN 151 0.0399

GLN 151 PHE 152 -0.0002

PHE 152 ARG 153 0.0002

ARG 153 LYS 154 0.0829

LYS 154 VAL 155 -0.0000

VAL 155 CYS 156 0.0002

CYS 156 TYR 157 -0.0231

TYR 157 SER 158 -0.0002

SER 158 ARG 159 0.0003

ARG 159 LEU 160 0.0380

LEU 160 HIS 161 -0.0003

HIS 161 GLY 162 -0.0001

GLY 162 SER 163 -0.0301

SER 163 LEU 164 0.0000

LEU 164 PRO 165 0.0001

PRO 165 GLN 166 0.0211

GLN 166 LEU 167 0.0001

LEU 167 VAL 168 -0.0001

VAL 168 ALA 169 0.0641

ALA 169 PRO 170 0.0002

PRO 170 PRO 171 -0.0002

PRO 171 LYS 172 0.0309

LYS 172 THR 173 0.0002

THR 173 GLN 174 0.0001

GLN 174 ALA 175 0.0270

ALA 175 PRO 176 -0.0001

PRO 176 THR 177 0.0000

THR 177 GLY 178 0.0214

GLY 178 ILE 179 -0.0002

ILE 179 ASP 180 0.0003

ASP 180 SER 181 0.0989

SER 181 ASP 182 0.0001

ASP 182 SER 183 -0.0004

SER 183 ILE 184 0.0830

ILE 184 PRO 185 -0.0000

PRO 185 GLU 186 0.0000

GLU 186 GLN 187 -0.0527

GLN 187 LEU 188 -0.0002

LEU 188 ASP 189 0.0000

ASP 189 ASP 190 -0.0220

ASP 190 PHE 191 -0.0002

PHE 191 PRO 192 0.0004

PRO 192 THR 193 0.0353

THR 193 PRO 194 0.0000

PRO 194 SER 195 0.0000

SER 195 ALA 196 -0.0703

ALA 196 HIS 197 0.0003

HIS 197 LEU 198 -0.0001

LEU 198 ARG 199 0.1091

ARG 199 ALA 200 0.0003

ALA 200 LEU 201 -0.0003

LEU 201 TRP 202 -0.0077

TRP 202 PRO 203 0.0005

PRO 203 ALA 204 -0.0001

ALA 204 GLY 205 -0.0544

GLY 205 GLU 206 0.0001

GLU 206 ALA 207 -0.0000

ALA 207 GLU 208 0.0019

GLU 208 ALA 209 0.0001

ALA 209 GLN 210 -0.0001

GLN 210 ARG 211 0.0038

ARG 211 ARG 212 0.0003

ARG 212 LEU 213 -0.0002

LEU 213 ASN 214 -0.0292

ASN 214 GLU 215 -0.0004

GLU 215 PHE 216 0.0001

PHE 216 THR 217 0.0035

THR 217 ASP 218 0.0004

ASP 218 ALA 219 0.0002

ALA 219 GLN 220 -0.0677

GLN 220 ILE 221 0.0000

ILE 221 ASP 222 0.0007

ASP 222 TYR 223 -0.0448

TYR 223 TYR 224 0.0000

TYR 224 LYS 225 -0.0001

LYS 225 ASP 226 0.0507

ASP 226 GLU 227 0.0002

GLU 227 ARG 228 0.0002

ARG 228 ASP 229 0.0121

ASP 229 LEU 230 -0.0003

LEU 230 PRO 231 -0.0000

PRO 231 ALA 232 0.0269

ALA 232 LYS 233 -0.0002

LYS 233 PRO 234 -0.0005

PRO 234 GLY 235 0.0117

GLY 235 THR 236 -0.0001

THR 236 SER 237 0.0003

SER 237 GLN 238 0.0565

GLN 238 LEU 239 -0.0001

LEU 239 SER 240 -0.0000

SER 240 THR 241 0.0039

THR 241 TYR 242 0.0002

TYR 242 LEU 243 0.0002

LEU 243 ALA 244 -0.0324

ALA 244 ALA 245 0.0002

ALA 245 GLY 246 0.0000

GLY 246 ILE 247 -0.0081

ILE 247 LEU 248 0.0002

LEU 248 SER 249 -0.0002

SER 249 PRO 250 0.0124

PRO 250 ARG 251 -0.0003

ARG 251 GLN 252 0.0000

GLN 252 CYS 253 0.0855

CYS 253 LEU 254 -0.0003

LEU 254 HIS 255 -0.0003

HIS 255 ALA 256 -0.0777

ALA 256 ALA 257 -0.0002

ALA 257 LEU 258 0.0001

LEU 258 GLN 259 -0.0096

GLN 259 SER 260 -0.0002

SER 260 ASN 261 -0.0004

ASN 261 GLN 262 -0.0345

GLN 262 GLY 263 -0.0000

GLY 263 GLU 264 0.0001

GLU 264 PHE 265 -0.0207

PHE 265 GLU 266 0.0000

GLU 266 SER 267 0.0003

SER 267 GLY 268 -0.0200

GLY 268 SER 269 -0.0002

SER 269 VAL 270 -0.0002

VAL 270 GLY 271 -0.0123

GLY 271 VAL 272 0.0004

VAL 272 VAL 273 -0.0002

VAL 273 THR 274 -0.0003

THR 274 TRP 275 -0.0002

TRP 275 ILE 276 -0.0001

ILE 276 ASN 277 0.0106

ASN 277 GLU 278 -0.0002

GLU 278 LEU 279 0.0002

LEU 279 LEU 280 0.0430

LEU 280 TRP 281 -0.0004

TRP 281 ARG 282 -0.0002

ARG 282 GLU 283 -0.0058

GLU 283 PHE 284 0.0000

PHE 284 TYR 285 0.0000

TYR 285 LYS 286 -0.1031

LYS 286 HIS 287 -0.0001

HIS 287 ILE 288 0.0002

ILE 288 LEU 289 -0.1084

LEU 289 VAL 290 -0.0005

VAL 290 GLY 291 -0.0001

GLY 291 TYR 292 -0.0139

TYR 292 PRO 293 0.0000

PRO 293 ARG 294 -0.0003

ARG 294 VAL 295 0.0450

VAL 295 SER 296 -0.0001

SER 296 ARG 297 -0.0001

ARG 297 HIS 298 -0.1232

HIS 298 ARG 299 -0.0005

ARG 299 ALA 300 0.0003

ALA 300 PHE 301 0.0178

PHE 301 ARG 302 0.0000

ARG 302 PRO 303 0.0002

PRO 303 GLU 304 -0.0772

GLU 304 THR 305 -0.0007

THR 305 GLU 306 0.0003

GLU 306 ALA 307 -0.0174

ALA 307 LEU 308 0.0002

LEU 308 ALA 309 0.0000

ALA 309 TRP 310 -0.0061

TRP 310 ARG 311 -0.0003

ARG 311 HIS 312 0.0001

HIS 312 ALA 313 0.0002

ALA 313 PRO 314 -0.0003

PRO 314 GLU 315 -0.0001

GLU 315 ASP 316 -0.0372

ASP 316 LEU 317 -0.0001

LEU 317 ALA 318 -0.0002

ALA 318 ALA 319 -0.0547

ALA 319 TRP 320 -0.0002

TRP 320 LYS 321 -0.0002

LYS 321 GLU 322 -0.0626

GLU 322 ALA 323 -0.0002

ALA 323 ARG 324 0.0004

ARG 324 THR 325 0.0334

THR 325 GLY 326 0.0001

GLY 326 LEU 327 -0.0003

LEU 327 PRO 328 0.0066

PRO 328 ILE 329 0.0001

ILE 329 ILE 330 -0.0000

ILE 330 ASP 331 -0.0014

ASP 331 ALA 332 0.0001

ALA 332 ALA 333 -0.0003

ALA 333 MET 334 -0.0053

MET 334 ARG 335 -0.0000

ARG 335 GLN 336 0.0002

GLN 336 LEU 337 -0.0338

LEU 337 LEU 338 -0.0001

LEU 338 GLU 339 0.0000

GLU 339 THR 340 0.0028

THR 340 GLY 341 0.0002

GLY 341 TRP 342 -0.0000

TRP 342 MET 343 0.0938

MET 343 HIS 344 -0.0001

HIS 344 ASN 345 0.0001

ASN 345 ARG 346 0.0633

ARG 346 LEU 347 0.0001

LEU 347 ARG 348 -0.0001

ARG 348 MET 349 0.0428

MET 349 VAL 350 -0.0003

VAL 350 VAL 351 0.0001

VAL 351 ALA 352 0.0346

ALA 352 MET 353 0.0001

MET 353 PHE 354 0.0002

PHE 354 LEU 355 -0.0230

LEU 355 THR 356 0.0002

THR 356 LYS 357 0.0000

LYS 357 ASN 358 0.0359

ASN 358 LEU 359 -0.0000

LEU 359 LEU 360 -0.0000

LEU 360 ILE 361 0.0280

ILE 361 ASP 362 -0.0000

ASP 362 TRP 363 0.0001

TRP 363 ARG 364 0.0136

ARG 364 GLU 365 0.0002

GLU 365 GLY 366 0.0004

GLY 366 GLU 367 -0.0067

GLU 367 ARG 368 -0.0001

ARG 368 PHE 369 -0.0000

PHE 369 PHE 370 0.0051

PHE 370 MET 371 0.0001

MET 371 ARG 372 0.0002

ARG 372 HIS 373 -0.0560

HIS 373 LEU 374 -0.0004

LEU 374 ILE 375 0.0001

ILE 375 ASP 376 -0.0124

ASP 376 GLY 377 -0.0005

GLY 377 ASP 378 0.0002

ASP 378 LEU 379 -0.0268

LEU 379 ALA 380 0.0001

ALA 380 ALA 381 0.0003

ALA 381 ASN 382 0.0212

ASN 382 ASN 383 -0.0004

ASN 383 GLY 384 0.0003

GLY 384 GLY 385 -0.0021

GLY 385 TRP 386 -0.0000

TRP 386 GLN 387 -0.0003

GLN 387 TRP 388 0.0199

TRP 388 SER 389 0.0003

SER 389 SER 390 -0.0004

SER 390 SER 391 0.0397

SER 391 THR 392 -0.0003

THR 392 GLY 393 -0.0001

GLY 393 THR 394 -0.0548

THR 394 ASP 395 -0.0004

ASP 395 SER 396 0.0001

SER 396 ALA 397 0.0618

ALA 397 PRO 398 -0.0003

PRO 398 TYR 399 -0.0003

TYR 399 PHE 400 -0.0002

PHE 400 ARG 401 0.0000

ARG 401 ILE 402 -0.0000

ILE 402 PHE 403 0.0662

PHE 403 ASN 404 0.0004

ASN 404 PRO 405 0.0000

PRO 405 LEU 406 0.1547

LEU 406 SER 407 -0.0002

SER 407 GLN 408 0.0001

GLN 408 SER 409 0.0209

SER 409 GLU 410 0.0002

GLU 410 LYS 411 -0.0003

LYS 411 PHE 412 0.0003

PHE 412 ASP 413 -0.0002

ASP 413 SER 414 0.0003

SER 414 GLU 415 0.0289

GLU 415 GLY 416 0.0000

GLY 416 LEU 417 -0.0000

LEU 417 PHE 418 0.0160

PHE 418 ILE 419 -0.0002

ILE 419 LYS 420 0.0001

LYS 420 HIS 421 -0.0277

HIS 421 TRP 422 0.0002

TRP 422 LEU 423 -0.0003

LEU 423 PRO 424 -0.0015

PRO 424 GLU 425 -0.0002

GLU 425 LEU 426 -0.0000

LEU 426 ALA 427 0.0735

ALA 427 GLY 428 -0.0002

GLY 428 LEU 429 -0.0003

LEU 429 ASN 430 0.0281

ASN 430 LYS 431 0.0000

LYS 431 LYS 432 0.0002

LYS 432 ASP 433 -0.0324

ASP 433 ILE 434 -0.0001

ILE 434 HIS 435 0.0001

HIS 435 ASN 436 0.1037

ASN 436 PRO 437 -0.0001

PRO 437 ALA 438 -0.0000

ALA 438 ASN 439 -0.1685

ASN 439 MET 440 -0.0001

MET 440 GLY 441 -0.0002

GLY 441 GLY 442 0.4163

GLY 442 LEU 443 -0.0003

LEU 443 PHE 444 0.0000

PHE 444 GLY 445 -0.0456

GLY 445 VAL 446 -0.0002

VAL 446 ALA 447 -0.0001

ALA 447 ASP 448 -0.1937

ASP 448 TYR 449 -0.0002

TYR 449 PRO 450 -0.0000

PRO 450 LEU 451 0.0865

LEU 451 PRO 452 -0.0001

PRO 452 ILE 453 -0.0001

ILE 453 VAL 454 0.1434

VAL 454 ASN 455 0.0002

ASN 455 LEU 456 -0.0001

LEU 456 GLY 457 0.0357

GLY 457 GLN 458 -0.0003

GLN 458 SER 459 0.0002

SER 459 ARG 460 0.0226

ARG 460 GLU 461 0.0000

GLU 461 ARG 462 0.0002

ARG 462 ALA 463 -0.0168

ALA 463 LEU 464 0.0002

LEU 464 ALA 465 -0.0003

ALA 465 ALA 466 -0.0226

ALA 466 PHE 467 -0.0001

PHE 467 LYS 468 -0.0001

LYS 468 ASN 469 -0.0098

ASN 469 LEU 470 -0.0001

LEU 470 PRO 471 -0.0003

PRO 471 THR 472 -0.0793

THR 472 ARG 473 0.0002

ARG 473 MET 474 -0.0003

MET 474 ASP 475 0.0639

ASP 475 ALA 476 -0.0001

ALA 476 ALA 477 0.0000

ALA 477 GLY 478 -0.1308

GLY 478 VAL 479 -0.0000

VAL 479 TYR 480 -0.0002

TYR 480 ASP 481 -0.0119

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.

*** Phrb Pseudomonas fluorescens model 5 ***

CA strain for 221006205537110470

--- normal mode 14 ---

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

* Phrb Pseudomonas fluorescens model 5 *