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

* Phrb Pseudomonas fluorescens model 5 *

CA strain for 221006205537110470

--- normal mode 10 ---

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 -0.0001

GLN 2 LEU 3 0.0000

LEU 3 ILE 4 -0.0244

ILE 4 TRP 5 -0.0002

TRP 5 LEU 6 0.0001

LEU 6 ARG 7 -0.0003

ARG 7 SER 8 0.0000

SER 8 ASP 9 -0.0002

ASP 9 LEU 10 0.0091

LEU 10 ARG 11 0.0001

ARG 11 VAL 12 0.0000

VAL 12 HIS 13 0.0238

HIS 13 ASP 14 0.0007

ASP 14 ASN 15 0.0001

ASN 15 THR 16 -0.0422

THR 16 ALA 17 -0.0003

ALA 17 LEU 18 -0.0002

LEU 18 SER 19 0.0032

SER 19 ALA 20 0.0002

ALA 20 ALA 21 0.0000

ALA 21 ALA 22 0.0407

ALA 22 VAL 23 -0.0005

VAL 23 ARG 24 -0.0000

ARG 24 GLY 25 0.0155

GLY 25 PRO 26 0.0004

PRO 26 CYS 27 -0.0002

CYS 27 VAL 28 -0.0005

VAL 28 ALA 29 -0.0000

ALA 29 VAL 30 0.0003

VAL 30 TYR 31 -0.0083

TYR 31 LEU 32 0.0002

LEU 32 LEU 33 0.0002

LEU 33 SER 34 0.0318

SER 34 PRO 35 0.0005

PRO 35 ALA 36 -0.0003

ALA 36 GLN 37 -0.0276

GLN 37 TRP 38 -0.0002

TRP 38 LEU 39 0.0001

LEU 39 ALA 40 -0.0365

ALA 40 HIS 41 0.0002

HIS 41 ASP 42 -0.0004

ASP 42 ASP 43 0.0231

ASP 43 ALA 44 0.0001

ALA 44 PRO 45 0.0000

PRO 45 CYS 46 0.0205

CYS 46 LYS 47 -0.0002

LYS 47 VAL 48 0.0000

VAL 48 ASP 49 0.0134

ASP 49 PHE 50 -0.0001

PHE 50 TRP 51 0.0001

TRP 51 LEU 52 -0.0025

LEU 52 ARG 53 -0.0002

ARG 53 ASN 54 0.0002

ASN 54 LEU 55 -0.0889

LEU 55 ARG 56 0.0004

ARG 56 ASP 57 -0.0001

ASP 57 LEU 58 -0.0312

LEU 58 SER 59 0.0001

SER 59 GLN 60 0.0001

GLN 60 THR 61 0.0331

THR 61 LEU 62 -0.0000

LEU 62 ALA 63 0.0001

ALA 63 ARG 64 0.0141

ARG 64 LEU 65 -0.0001

LEU 65 ASN 66 -0.0002

ASN 66 ILE 67 0.0276

ILE 67 PRO 68 -0.0004

PRO 68 LEU 69 0.0001

LEU 69 LEU 70 0.0171

LEU 70 ILE 71 -0.0001

ILE 71 ARG 72 -0.0003

ARG 72 GLU 73 0.0535

GLU 73 ALA 74 -0.0001

ALA 74 SER 75 0.0001

SER 75 HIS 76 -0.0049

HIS 76 TRP 77 0.0001

TRP 77 ASP 78 0.0000

ASP 78 ASP 79 0.0259

ASP 79 ALA 80 0.0004

ALA 80 PRO 81 -0.0004

PRO 81 ARG 82 0.0154

ARG 82 VAL 83 0.0004

VAL 83 LEU 84 -0.0003

LEU 84 ALA 85 -0.0176

ALA 85 GLY 86 0.0002

GLY 86 LEU 87 0.0002

LEU 87 CYS 88 -0.0206

CYS 88 ASP 89 -0.0001

ASP 89 GLU 90 -0.0000

GLU 90 LEU 91 -0.0014

LEU 91 GLY 92 0.0002

GLY 92 VAL 93 0.0000

VAL 93 GLU 94 -0.0036

GLU 94 ALA 95 -0.0000

ALA 95 VAL 96 0.0002

VAL 96 HIS 97 -0.0152

HIS 97 ALA 98 0.0001

ALA 98 ASN 99 -0.0000

ASN 99 ASP 100 0.0984

ASP 100 GLU 101 0.0001

GLU 101 TYR 102 0.0001

TYR 102 GLY 103 0.0223

GLY 103 VAL 104 0.0001

VAL 104 HIS 105 -0.0000

HIS 105 GLU 106 0.0732

GLU 106 THR 107 -0.0004

THR 107 ARG 108 -0.0002

ARG 108 ARG 109 0.0745

ARG 109 ASP 110 0.0002

ASP 110 ALA 111 0.0002

ALA 111 ALA 112 -0.0037

ALA 112 VAL 113 -0.0001

VAL 113 ARG 114 -0.0002

ARG 114 GLN 115 -0.0306

GLN 115 ALA 116 -0.0004

ALA 116 LEU 117 -0.0001

LEU 117 GLU 118 -0.0117

GLU 118 THR 119 0.0001

THR 119 ALA 120 0.0002

ALA 120 GLY 121 -0.0051

GLY 121 ILE 122 -0.0002

ILE 122 ALA 123 0.0001

ALA 123 TRP 124 0.0178

TRP 124 HIS 125 -0.0005

HIS 125 ASN 126 0.0003

ASN 126 TYR 127 -0.0641

TYR 127 LEU 128 0.0000

LEU 128 ASP 129 -0.0001

ASP 129 GLN 130 -0.0084

GLN 130 LEU 131 -0.0003

LEU 131 LEU 132 0.0001

LEU 132 PHE 133 0.0209

PHE 133 GLN 134 -0.0001

GLN 134 PRO 135 -0.0001

PRO 135 GLY 136 -0.0011

GLY 136 SER 137 -0.0000

SER 137 VAL 138 0.0005

VAL 138 LEU 139 0.0109

LEU 139 THR 140 0.0001

THR 140 ARG 141 0.0001

ARG 141 THR 142 0.0077

THR 142 GLY 143 -0.0002

GLY 143 THR 144 -0.0002

THR 144 TYR 145 -0.0085

TYR 145 PHE 146 -0.0001

PHE 146 GLN 147 0.0002

GLN 147 VAL 148 -0.0363

VAL 148 PHE 149 -0.0001

PHE 149 SER 150 -0.0001

SER 150 GLN 151 0.0183

GLN 151 PHE 152 0.0001

PHE 152 ARG 153 -0.0001

ARG 153 LYS 154 0.0112

LYS 154 VAL 155 0.0002

VAL 155 CYS 156 -0.0003

CYS 156 TYR 157 -0.0088

TYR 157 SER 158 -0.0001

SER 158 ARG 159 -0.0001

ARG 159 LEU 160 0.0075

LEU 160 HIS 161 -0.0004

HIS 161 GLY 162 0.0001

GLY 162 SER 163 0.0123

SER 163 LEU 164 -0.0001

LEU 164 PRO 165 0.0003

PRO 165 GLN 166 0.0380

GLN 166 LEU 167 0.0001

LEU 167 VAL 168 0.0002

VAL 168 ALA 169 0.0472

ALA 169 PRO 170 0.0001

PRO 170 PRO 171 0.0000

PRO 171 LYS 172 0.0304

LYS 172 THR 173 -0.0001

THR 173 GLN 174 0.0000

GLN 174 ALA 175 0.0089

ALA 175 PRO 176 -0.0001

PRO 176 THR 177 0.0002

THR 177 GLY 178 -0.0089

GLY 178 ILE 179 -0.0001

ILE 179 ASP 180 -0.0000

ASP 180 SER 181 -0.0366

SER 181 ASP 182 0.0000

ASP 182 SER 183 0.0000

SER 183 ILE 184 -0.0386

ILE 184 PRO 185 -0.0002

PRO 185 GLU 186 0.0001

GLU 186 GLN 187 0.0038

GLN 187 LEU 188 -0.0000

LEU 188 ASP 189 0.0001

ASP 189 ASP 190 -0.0040

ASP 190 PHE 191 -0.0003

PHE 191 PRO 192 -0.0000

PRO 192 THR 193 -0.0038

THR 193 PRO 194 0.0000

PRO 194 SER 195 0.0000

SER 195 ALA 196 0.0578

ALA 196 HIS 197 -0.0002

HIS 197 LEU 198 0.0005

LEU 198 ARG 199 -0.1434

ARG 199 ALA 200 -0.0000

ALA 200 LEU 201 -0.0001

LEU 201 TRP 202 -0.0673

TRP 202 PRO 203 -0.0004

PRO 203 ALA 204 0.0001

ALA 204 GLY 205 -0.1092

GLY 205 GLU 206 0.0002

GLU 206 ALA 207 -0.0001

ALA 207 GLU 208 -0.0711

GLU 208 ALA 209 0.0004

ALA 209 GLN 210 0.0003

GLN 210 ARG 211 -0.0151

ARG 211 ARG 212 -0.0000

ARG 212 LEU 213 0.0003

LEU 213 ASN 214 0.0236

ASN 214 GLU 215 -0.0000

GLU 215 PHE 216 -0.0002

PHE 216 THR 217 0.0114

THR 217 ASP 218 0.0002

ASP 218 ALA 219 -0.0002

ALA 219 GLN 220 -0.0237

GLN 220 ILE 221 -0.0001

ILE 221 ASP 222 -0.0001

ASP 222 TYR 223 -0.0176

TYR 223 TYR 224 -0.0002

TYR 224 LYS 225 -0.0002

LYS 225 ASP 226 0.0339

ASP 226 GLU 227 0.0000

GLU 227 ARG 228 0.0005

ARG 228 ASP 229 -0.0433

ASP 229 LEU 230 0.0001

LEU 230 PRO 231 -0.0002

PRO 231 ALA 232 0.0077

ALA 232 LYS 233 -0.0004

LYS 233 PRO 234 0.0003

PRO 234 GLY 235 0.0051

GLY 235 THR 236 -0.0001

THR 236 SER 237 -0.0000

SER 237 GLN 238 0.0440

GLN 238 LEU 239 0.0001

LEU 239 SER 240 0.0003

SER 240 THR 241 0.0194

THR 241 TYR 242 -0.0001

TYR 242 LEU 243 -0.0002

LEU 243 ALA 244 0.0118

ALA 244 ALA 245 0.0002

ALA 245 GLY 246 -0.0003

GLY 246 ILE 247 -0.0099

ILE 247 LEU 248 0.0004

LEU 248 SER 249 -0.0001

SER 249 PRO 250 0.0135

PRO 250 ARG 251 0.0000

ARG 251 GLN 252 -0.0001

GLN 252 CYS 253 -0.0577

CYS 253 LEU 254 0.0002

LEU 254 HIS 255 -0.0000

HIS 255 ALA 256 -0.0335

ALA 256 ALA 257 0.0002

ALA 257 LEU 258 -0.0001

LEU 258 GLN 259 -0.0063

GLN 259 SER 260 -0.0001

SER 260 ASN 261 -0.0000

ASN 261 GLN 262 -0.0052

GLN 262 GLY 263 -0.0000

GLY 263 GLU 264 -0.0002

GLU 264 PHE 265 -0.0093

PHE 265 GLU 266 -0.0002

GLU 266 SER 267 0.0003

SER 267 GLY 268 -0.0290

GLY 268 SER 269 -0.0003

SER 269 VAL 270 -0.0001

VAL 270 GLY 271 -0.0136

GLY 271 VAL 272 -0.0002

VAL 272 VAL 273 -0.0001

VAL 273 THR 274 0.0074

THR 274 TRP 275 -0.0002

TRP 275 ILE 276 -0.0004

ILE 276 ASN 277 -0.0173

ASN 277 GLU 278 -0.0003

GLU 278 LEU 279 0.0000

LEU 279 LEU 280 -0.0002

LEU 280 TRP 281 -0.0001

TRP 281 ARG 282 -0.0003

ARG 282 GLU 283 0.0046

GLU 283 PHE 284 0.0000

PHE 284 TYR 285 -0.0000

TYR 285 LYS 286 0.0300

LYS 286 HIS 287 0.0002

HIS 287 ILE 288 -0.0001

ILE 288 LEU 289 0.0207

LEU 289 VAL 290 0.0003

VAL 290 GLY 291 -0.0001

GLY 291 TYR 292 0.0405

TYR 292 PRO 293 0.0001

PRO 293 ARG 294 0.0000

ARG 294 VAL 295 -0.0698

VAL 295 SER 296 -0.0000

SER 296 ARG 297 -0.0003

ARG 297 HIS 298 0.0925

HIS 298 ARG 299 -0.0003

ARG 299 ALA 300 0.0002

ALA 300 PHE 301 -0.0424

PHE 301 ARG 302 0.0001

ARG 302 PRO 303 0.0000

PRO 303 GLU 304 0.0914

GLU 304 THR 305 0.0001

THR 305 GLU 306 -0.0000

GLU 306 ALA 307 0.0676

ALA 307 LEU 308 0.0001

LEU 308 ALA 309 0.0001

ALA 309 TRP 310 -0.0050

TRP 310 ARG 311 -0.0001

ARG 311 HIS 312 0.0002

HIS 312 ALA 313 0.0021

ALA 313 PRO 314 0.0000

PRO 314 GLU 315 0.0000

GLU 315 ASP 316 -0.0129

ASP 316 LEU 317 -0.0001

LEU 317 ALA 318 -0.0000

ALA 318 ALA 319 -0.0145

ALA 319 TRP 320 -0.0000

TRP 320 LYS 321 -0.0000

LYS 321 GLU 322 -0.0298

GLU 322 ALA 323 0.0002

ALA 323 ARG 324 -0.0002

ARG 324 THR 325 -0.0198

THR 325 GLY 326 -0.0001

GLY 326 LEU 327 -0.0002

LEU 327 PRO 328 0.0009

PRO 328 ILE 329 0.0001

ILE 329 ILE 330 0.0000

ILE 330 ASP 331 0.0053

ASP 331 ALA 332 -0.0000

ALA 332 ALA 333 0.0002

ALA 333 MET 334 0.0134

MET 334 ARG 335 -0.0004

ARG 335 GLN 336 -0.0003

GLN 336 LEU 337 -0.0712

LEU 337 LEU 338 0.0001

LEU 338 GLU 339 -0.0000

GLU 339 THR 340 0.0392

THR 340 GLY 341 -0.0002

GLY 341 TRP 342 0.0002

TRP 342 MET 343 -0.0672

MET 343 HIS 344 -0.0001

HIS 344 ASN 345 0.0003

ASN 345 ARG 346 0.0126

ARG 346 LEU 347 0.0003

LEU 347 ARG 348 0.0001

ARG 348 MET 349 -0.0360

MET 349 VAL 350 0.0001

VAL 350 VAL 351 -0.0003

VAL 351 ALA 352 0.0338

ALA 352 MET 353 0.0003

MET 353 PHE 354 0.0000

PHE 354 LEU 355 0.0213

LEU 355 THR 356 0.0002

THR 356 LYS 357 -0.0004

LYS 357 ASN 358 0.0638

ASN 358 LEU 359 0.0002

LEU 359 LEU 360 -0.0000

LEU 360 ILE 361 0.0371

ILE 361 ASP 362 0.0004

ASP 362 TRP 363 0.0002

TRP 363 ARG 364 0.0368

ARG 364 GLU 365 -0.0003

GLU 365 GLY 366 0.0001

GLY 366 GLU 367 0.0462

GLU 367 ARG 368 -0.0004

ARG 368 PHE 369 -0.0004

PHE 369 PHE 370 0.0213

PHE 370 MET 371 0.0003

MET 371 ARG 372 -0.0002

ARG 372 HIS 373 0.0196

HIS 373 LEU 374 -0.0002

LEU 374 ILE 375 0.0002

ILE 375 ASP 376 -0.0024

ASP 376 GLY 377 0.0004

GLY 377 ASP 378 -0.0005

ASP 378 LEU 379 -0.0177

LEU 379 ALA 380 -0.0001

ALA 380 ALA 381 -0.0002

ALA 381 ASN 382 0.0092

ASN 382 ASN 383 -0.0002

ASN 383 GLY 384 0.0003

GLY 384 GLY 385 0.0506

GLY 385 TRP 386 -0.0001

TRP 386 GLN 387 -0.0000

GLN 387 TRP 388 0.0279

TRP 388 SER 389 0.0004

SER 389 SER 390 -0.0002

SER 390 SER 391 0.0362

SER 391 THR 392 0.0000

THR 392 GLY 393 -0.0003

GLY 393 THR 394 -0.0307

THR 394 ASP 395 -0.0004

ASP 395 SER 396 0.0000

SER 396 ALA 397 0.0878

ALA 397 PRO 398 -0.0004

PRO 398 TYR 399 0.0001

TYR 399 PHE 400 0.0344

PHE 400 ARG 401 -0.0002

ARG 401 ILE 402 0.0002

ILE 402 PHE 403 0.0470

PHE 403 ASN 404 0.0001

ASN 404 PRO 405 -0.0001

PRO 405 LEU 406 0.1430

LEU 406 SER 407 0.0003

SER 407 GLN 408 -0.0000

GLN 408 SER 409 0.0173

SER 409 GLU 410 -0.0001

GLU 410 LYS 411 0.0001

LYS 411 PHE 412 -0.0014

PHE 412 ASP 413 -0.0004

ASP 413 SER 414 0.0004

SER 414 GLU 415 0.0178

GLU 415 GLY 416 -0.0004

GLY 416 LEU 417 0.0003

LEU 417 PHE 418 0.0118

PHE 418 ILE 419 -0.0003

ILE 419 LYS 420 0.0003

LYS 420 HIS 421 -0.1375

HIS 421 TRP 422 -0.0001

TRP 422 LEU 423 0.0000

LEU 423 PRO 424 -0.0154

PRO 424 GLU 425 0.0001

GLU 425 LEU 426 -0.0002

LEU 426 ALA 427 0.1212

ALA 427 GLY 428 0.0002

GLY 428 LEU 429 -0.0000

LEU 429 ASN 430 -0.0003

ASN 430 LYS 431 -0.0001

LYS 431 LYS 432 -0.0002

LYS 432 ASP 433 -0.0374

ASP 433 ILE 434 -0.0000

ILE 434 HIS 435 0.0001

HIS 435 ASN 436 0.0992

ASN 436 PRO 437 -0.0005

PRO 437 ALA 438 -0.0002

ALA 438 ASN 439 -0.1109

ASN 439 MET 440 0.0002

MET 440 GLY 441 -0.0002

GLY 441 GLY 442 0.3249

GLY 442 LEU 443 -0.0011

LEU 443 PHE 444 0.0005

PHE 444 GLY 445 0.1064

GLY 445 VAL 446 0.0001

VAL 446 ALA 447 0.0004

ALA 447 ASP 448 0.0430

ASP 448 TYR 449 -0.0001

TYR 449 PRO 450 0.0002

PRO 450 LEU 451 0.0500

LEU 451 PRO 452 -0.0001

PRO 452 ILE 453 -0.0001

ILE 453 VAL 454 0.0696

VAL 454 ASN 455 0.0001

ASN 455 LEU 456 0.0001

LEU 456 GLY 457 0.0118

GLY 457 GLN 458 0.0002

GLN 458 SER 459 -0.0005

SER 459 ARG 460 0.0233

ARG 460 GLU 461 0.0004

GLU 461 ARG 462 0.0000

ARG 462 ALA 463 0.0122

ALA 463 LEU 464 0.0002

LEU 464 ALA 465 -0.0000

ALA 465 ALA 466 0.0097

ALA 466 PHE 467 0.0001

PHE 467 LYS 468 0.0001

LYS 468 ASN 469 -0.0358

ASN 469 LEU 470 0.0001

LEU 470 PRO 471 -0.0002

PRO 471 THR 472 0.0315

THR 472 ARG 473 -0.0003

ARG 473 MET 474 0.0002

MET 474 ASP 475 -0.0784

ASP 475 ALA 476 0.0000

ALA 476 ALA 477 0.0000

ALA 477 GLY 478 0.0113

GLY 478 VAL 479 -0.0001

VAL 479 TYR 480 0.0001

TYR 480 ASP 481 0.0200

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 10 ---

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

* Phrb Pseudomonas fluorescens model 5 *