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

* TRANSFERASE 31-MAR-06 2CJD *

CA strain for 220405004109145553

--- normal mode 13 ---

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
THR 15 THR 16 -0.0000

THR 16 PRO 17 0.0003

PRO 17 ASP 18 -0.0309

ASP 18 ARG 19 0.0002

ARG 19 VAL 20 0.0003

VAL 20 HIS 21 -0.0269

HIS 21 GLU 22 -0.0001

GLU 22 VAL 23 -0.0002

VAL 23 LEU 24 0.0490

LEU 24 GLY 25 0.0003

GLY 25 ARG 26 0.0000

ARG 26 SER 27 -0.0136

SER 27 MET 28 -0.0003

MET 28 LEU 29 -0.0003

LEU 29 VAL 30 -0.0592

VAL 30 ASP 31 -0.0003

ASP 31 GLY 32 0.0000

GLY 32 LEU 33 -0.0873

LEU 33 ASP 34 -0.0000

ASP 34 ILE 35 0.0000

ILE 35 VAL 36 -0.0185

VAL 36 LEU 37 0.0002

LEU 37 ASP 38 0.0003

ASP 38 LEU 39 -0.0094

LEU 39 THR 40 0.0000

THR 40 ARG 41 0.0001

ARG 41 SER 42 -0.0165

SER 42 GLY 43 -0.0000

GLY 43 GLY 44 0.0001

GLY 44 SER 45 0.0281

SER 45 TYR 46 0.0002

TYR 46 LEU 47 -0.0001

LEU 47 VAL 48 0.0181

VAL 48 ASP 49 -0.0001

ASP 49 ALA 50 0.0001

ALA 50 ILE 51 -0.0136

ILE 51 THR 52 -0.0001

THR 52 GLY 53 -0.0001

GLY 53 ARG 54 0.0326

ARG 54 ARG 55 -0.0004

ARG 55 TYR 56 0.0001

TYR 56 LEU 57 -0.0656

LEU 57 ASP 58 -0.0000

ASP 58 MET 59 -0.0000

MET 59 PHE 60 0.0002

PHE 60 THR 61 -0.0001

THR 61 PHE 62 0.0001

PHE 62 VAL 63 0.0520

VAL 63 ALA 64 -0.0002

ALA 64 SER 65 -0.0003

SER 65 SER 66 -0.0038

SER 66 ALA 67 0.0000

ALA 67 LEU 68 -0.0002

LEU 68 GLY 69 0.0445

GLY 69 MET 70 -0.0001

MET 70 ASN 71 0.0002

ASN 71 PRO 72 -0.0572

PRO 72 PRO 73 0.0001

PRO 73 ALA 74 0.0002

ALA 74 LEU 75 0.0271

LEU 75 VAL 76 -0.0002

VAL 76 ASP 77 0.0001

ASP 77 ASP 78 -0.0697

ASP 78 ARG 79 0.0001

ARG 79 GLU 80 0.0002

GLU 80 PHE 81 0.0115

PHE 81 HIS 82 -0.0004

HIS 82 ALA 83 0.0001

ALA 83 GLU 84 0.0123

GLU 84 LEU 85 -0.0001

LEU 85 MET 86 0.0002

MET 86 GLN 87 -0.0006

GLN 87 ALA 88 -0.0001

ALA 88 ALA 89 -0.0001

ALA 89 LEU 90 -0.0195

LEU 90 ASN 91 -0.0003

ASN 91 LYS 92 -0.0001

LYS 92 PRO 93 0.0446

PRO 93 SER 94 -0.0000

SER 94 ASN 95 -0.0000

ASN 95 SER 96 0.0697

SER 96 ASP 97 0.0001

ASP 97 VAL 98 -0.0000

VAL 98 TYR 99 0.0386

TYR 99 SER 100 0.0000

SER 100 VAL 101 0.0003

VAL 101 ALA 102 -0.0519

ALA 102 MET 103 -0.0000

MET 103 ALA 104 -0.0003

ALA 104 ARG 105 -0.0449

ARG 105 PHE 106 -0.0001

PHE 106 VAL 107 -0.0000

VAL 107 GLU 108 -0.0221

GLU 108 THR 109 -0.0005

THR 109 PHE 110 0.0003

PHE 110 ALA 111 -0.0528

ALA 111 ARG 112 -0.0001

ARG 112 VAL 113 0.0002

VAL 113 LEU 114 0.0108

LEU 114 GLY 115 -0.0001

GLY 115 ASP 116 -0.0004

ASP 116 PRO 117 0.1017

PRO 117 ALA 118 0.0001

ALA 118 LEU 119 -0.0001

LEU 119 PRO 120 -0.0072

PRO 120 HIS 121 0.0003

HIS 121 LEU 122 -0.0004

LEU 122 PHE 123 -0.0649

PHE 123 PHE 124 0.0004

PHE 124 VAL 125 -0.0004

VAL 125 GLU 126 0.0775

GLU 126 GLY 127 -0.0001

GLY 127 GLY 128 0.0005

GLY 128 ALA 129 -0.0789

ALA 129 LEU 130 0.0001

LEU 130 ALA 131 0.0005

ALA 131 VAL 132 0.0255

VAL 132 GLU 133 0.0000

GLU 133 ASN 134 0.0002

ASN 134 ALA 135 0.0260

ALA 135 LEU 136 -0.0002

LEU 136 LYS 137 -0.0001

LYS 137 ALA 138 -0.0927

ALA 138 ALA 139 -0.0004

ALA 139 PHE 140 -0.0001

PHE 140 ASP 141 -0.0939

ASP 141 TRP 142 0.0001

TRP 142 LYS 143 0.0001

LYS 143 SER 144 0.0096

SER 144 ARG 145 0.0000

ARG 145 HIS 146 -0.0002

HIS 146 ASN 147 0.0620

ASN 147 GLN 148 -0.0002

GLN 148 ALA 149 -0.0003

ALA 149 HIS 150 0.0173

HIS 150 GLY 151 0.0001

GLY 151 ILE 152 -0.0003

ILE 152 ASP 153 -0.0185

ASP 153 PRO 154 -0.0001

PRO 154 ALA 155 0.0002

ALA 155 LEU 156 -0.0262

LEU 156 GLY 157 0.0001

GLY 157 THR 158 -0.0000

THR 158 GLN 159 -0.0755

GLN 159 VAL 160 0.0001

VAL 160 LEU 161 -0.0000

LEU 161 HIS 162 -0.1312

HIS 162 LEU 163 0.0001

LEU 163 ARG 164 0.0002

ARG 164 GLY 165 -0.1084

GLY 165 ALA 166 0.0003

ALA 166 PHE 167 -0.0002

PHE 167 HIS 168 -0.0348

HIS 168 GLY 169 0.0002

GLY 169 ARG 170 -0.0000

ARG 170 SER 171 -0.0660

SER 171 GLY 172 0.0001

GLY 172 TYR 173 -0.0001

TYR 173 THR 174 -0.0107

THR 174 LEU 175 -0.0001

LEU 175 SER 176 -0.0002

SER 176 LEU 177 -0.0104

LEU 177 THR 178 -0.0001

THR 178 ASN 179 -0.0003

ASN 179 THR 180 -0.3096

THR 180 LYS 181 0.0002

LYS 181 PRO 182 -0.0001

PRO 182 THR 183 0.0953

THR 183 ILE 184 0.0003

ILE 184 THR 185 -0.0004

THR 185 ALA 186 0.1140

ALA 186 ARG 187 -0.0000

ARG 187 PHE 188 0.0002

PHE 188 PRO 189 0.0562

PRO 189 LYS 190 -0.0000

LYS 190 PHE 191 -0.0002

PHE 191 ASP 192 0.1044

ASP 192 TRP 193 -0.0003

TRP 193 PRO 194 -0.0003

PRO 194 ARG 195 -0.1248

ARG 195 ILE 196 0.0002

ILE 196 ASP 197 0.0001

ASP 197 ALA 198 -0.1369

ALA 198 PRO 199 0.0000

PRO 199 TYR 200 -0.0003

TYR 200 MET 201 -0.0629

MET 201 ARG 202 0.0002

ARG 202 PRO 203 -0.0001

PRO 203 GLY 204 -0.1928

GLY 204 LEU 205 -0.0001

LEU 205 ASP 206 0.0000

ASP 206 GLU 207 -0.0274

GLU 207 PRO 208 -0.0002

PRO 208 ALA 209 -0.0002

ALA 209 MET 210 -0.0033

MET 210 ALA 211 -0.0002

ALA 211 ALA 212 -0.0001

ALA 212 LEU 213 0.0871

LEU 213 GLU 214 -0.0001

GLU 214 ALA 215 0.0001

ALA 215 GLU 216 0.1364

GLU 216 ALA 217 -0.0002

ALA 217 LEU 218 0.0002

LEU 218 ARG 219 -0.0385

ARG 219 GLN 220 0.0003

GLN 220 ALA 221 -0.0002

ALA 221 ARG 222 -0.0414

ARG 222 ALA 223 0.0001

ALA 223 ALA 224 0.0001

ALA 224 PHE 225 -0.0169

PHE 225 GLU 226 0.0001

GLU 226 THR 227 0.0000

THR 227 ARG 228 0.0137

ARG 228 PRO 229 0.0002

PRO 229 HIS 230 0.0001

HIS 230 ASP 231 -0.0055

ASP 231 ILE 232 0.0001

ILE 232 ALA 233 0.0000

ALA 233 CYS 234 -0.0391

CYS 234 PHE 235 -0.0005

PHE 235 VAL 236 0.0001

VAL 236 ALA 237 -0.1385

ALA 237 GLU 238 -0.0000

GLU 238 PRO 239 0.0004

PRO 239 ILE 240 -0.0394

ILE 240 GLN 241 -0.0005

GLN 241 GLY 242 -0.0001

GLY 242 GLU 243 -0.0029

GLU 243 GLY 244 0.0000

GLY 244 GLY 245 0.0004

GLY 245 ASP 246 -0.0136

ASP 246 ARG 247 -0.0001

ARG 247 HIS 248 0.0000

HIS 248 PHE 249 -0.1112

PHE 249 ARG 250 -0.0003

ARG 250 PRO 251 0.0003

PRO 251 GLU 252 0.0144

GLU 252 PHE 253 0.0001

PHE 253 PHE 254 -0.0005

PHE 254 ALA 255 0.0009

ALA 255 ALA 256 -0.0000

ALA 256 MET 257 -0.0001

MET 257 ARG 258 -0.0106

ARG 258 GLU 259 0.0004

GLU 259 LEU 260 -0.0001

LEU 260 CYS 261 -0.0122

CYS 261 ASP 262 -0.0001

ASP 262 GLU 263 0.0000

GLU 263 PHE 264 0.0019

PHE 264 ASP 265 0.0002

ASP 265 ALA 266 -0.0000

ALA 266 LEU 267 0.0485

LEU 267 LEU 268 0.0002

LEU 268 ILE 269 0.0001

ILE 269 PHE 270 0.0007

PHE 270 ASP 271 0.0001

ASP 271 GLU 272 0.0001

GLU 272 VAL 273 -0.0148

VAL 273 GLN 274 -0.0002

GLN 274 THR 275 -0.0002

THR 275 GLY 276 -0.0347

GLY 276 CYS 277 0.0003

CYS 277 GLY 278 -0.0000

GLY 278 LEU 279 0.0144

LEU 279 THR 280 0.0001

THR 280 GLY 281 0.0001

GLY 281 THR 282 0.1289

THR 282 ALA 283 0.0001

ALA 283 TRP 284 -0.0001

TRP 284 ALA 285 -0.0567

ALA 285 TYR 286 0.0002

TYR 286 GLN 287 0.0002

GLN 287 GLN 288 0.0307

GLN 288 LEU 289 0.0000

LEU 289 ASP 290 -0.0002

ASP 290 VAL 291 0.0599

VAL 291 ALA 292 0.0001

ALA 292 PRO 293 0.0001

PRO 293 ASP 294 -0.0160

ASP 294 ILE 295 0.0000

ILE 295 VAL 296 -0.0002

VAL 296 ALA 297 -0.0233

ALA 297 PHE 298 -0.0001

PHE 298 GLY 299 -0.0002

GLY 299 LYS 300 0.1331

LYS 300 LYS 301 0.0001

LYS 301 THR 302 0.0002

THR 302 GLN 303 0.0009

GLN 303 VAL 304 0.0001

VAL 304 CYS 305 -0.0002

CYS 305 GLY 306 0.0520

GLY 306 VAL 307 0.0002

VAL 307 MET 308 0.0001

MET 308 ALA 309 0.1178

ALA 309 GLY 310 -0.0001

GLY 310 ARG 311 0.0001

ARG 311 ARG 312 0.0835

ARG 312 VAL 313 -0.0001

VAL 313 ASP 314 -0.0002

ASP 314 GLU 315 0.0978

GLU 315 VAL 316 0.0003

VAL 316 ALA 317 0.0002

ALA 317 ASP 318 -0.0243

ASP 318 ASN 319 0.0003

ASN 319 VAL 320 -0.0000

VAL 320 PHE 321 0.0695

PHE 321 ALA 322 0.0001

ALA 322 VAL 323 0.0001

VAL 323 PRO 324 0.0356

PRO 324 SER 325 0.0000

SER 325 ARG 326 0.0003

ARG 326 LEU 327 0.0863

LEU 327 ASN 328 0.0002

ASN 328 SER 329 -0.0003

SER 329 THR 330 -0.0270

THR 330 TRP 331 -0.0005

TRP 331 GLY 332 -0.0002

GLY 332 GLY 333 0.0397

GLY 333 ASN 334 -0.0001

ASN 334 LEU 335 -0.0000

LEU 335 THR 336 -0.0067

THR 336 ASP 337 -0.0002

ASP 337 MET 338 0.0004

MET 338 VAL 339 0.0353

VAL 339 ARG 340 -0.0002

ARG 340 ALA 341 0.0003

ALA 341 ARG 342 -0.0793

ARG 342 ARG 343 0.0003

ARG 343 ILE 344 0.0005

ILE 344 LEU 345 0.0371

LEU 345 GLU 346 -0.0002

GLU 346 VAL 347 -0.0001

VAL 347 ILE 348 0.0060

ILE 348 GLU 349 0.0001

GLU 349 ALA 350 -0.0000

ALA 350 GLU 351 0.0700

GLU 351 GLY 352 -0.0002

GLY 352 LEU 353 -0.0002

LEU 353 PHE 354 -0.0250

PHE 354 GLU 355 0.0001

GLU 355 ARG 356 -0.0002

ARG 356 ALA 357 -0.0579

ALA 357 VAL 358 0.0002

VAL 358 GLN 359 0.0003

GLN 359 HIS 360 0.0153

HIS 360 GLY 361 -0.0001

GLY 361 LYS 362 0.0003

LYS 362 TYR 363 0.0281

TYR 363 LEU 364 0.0001

LEU 364 ARG 365 -0.0001

ARG 365 ALA 366 -0.0174

ALA 366 ARG 367 0.0001

ARG 367 LEU 368 0.0001

LEU 368 ASP 369 0.0176

ASP 369 GLU 370 -0.0002

GLU 370 LEU 371 -0.0001

LEU 371 ALA 372 0.0012

ALA 372 ALA 373 -0.0001

ALA 373 ASP 374 0.0001

ASP 374 PHE 375 0.0121

PHE 375 PRO 376 -0.0001

PRO 376 ALA 377 0.0000

ALA 377 VAL 378 0.0083

VAL 378 VAL 379 -0.0002

VAL 379 LEU 380 0.0003

LEU 380 ASP 381 -0.1150

ASP 381 PRO 382 0.0001

PRO 382 ARG 383 0.0000

ARG 383 GLY 384 0.1258

GLY 384 ARG 385 0.0003

ARG 385 GLY 386 0.0003

GLY 386 LEU 387 -0.1153

LEU 387 MET 388 -0.0002

MET 388 CYS 389 -0.0001

CYS 389 ALA 390 0.0949

ALA 390 PHE 391 0.0001

PHE 391 SER 392 -0.0000

SER 392 LEU 393 0.0627

LEU 393 PRO 394 0.0002

PRO 394 THR 395 -0.0004

THR 395 THR 396 0.0251

THR 396 ALA 397 -0.0001

ALA 397 ASP 398 0.0004

ASP 398 ARG 399 -0.0391

ARG 399 ASP 400 -0.0001

ASP 400 GLU 401 -0.0002

GLU 401 LEU 402 0.0246

LEU 402 ILE 403 -0.0005

ILE 403 ARG 404 -0.0001

ARG 404 GLN 405 0.0449

GLN 405 LEU 406 0.0002

LEU 406 TRP 407 -0.0002

TRP 407 GLN 408 -0.0389

GLN 408 ARG 409 0.0001

ARG 409 ALA 410 -0.0002

ALA 410 VAL 411 -0.0297

VAL 411 ILE 412 -0.0001

ILE 412 VAL 413 0.0001

VAL 413 LEU 414 -0.0269

LEU 414 PRO 415 0.0001

PRO 415 ALA 416 -0.0002

ALA 416 GLY 417 -0.0827

GLY 417 ALA 418 0.0001

ALA 418 ASP 419 -0.0002

ASP 419 THR 420 0.0300

THR 420 VAL 421 0.0002

VAL 421 ARG 422 -0.0001

ARG 422 PHE 423 -0.0077

PHE 423 ARG 424 0.0001

ARG 424 PRO 425 -0.0001

PRO 425 PRO 426 0.0169

PRO 426 LEU 427 0.0004

LEU 427 THR 428 0.0001

THR 428 VAL 429 0.1386

VAL 429 SER 430 -0.0000

SER 430 THR 431 -0.0002

THR 431 ALA 432 0.0377

ALA 432 GLU 433 -0.0001

GLU 433 ILE 434 0.0003

ILE 434 ASP 435 0.0237

ASP 435 ALA 436 0.0003

ALA 436 ALA 437 -0.0001

ALA 437 ILE 438 -0.0156

ILE 438 ALA 439 0.0001

ALA 439 ALA 440 -0.0001

ALA 440 VAL 441 -0.0353

VAL 441 ARG 442 0.0003

ARG 442 SER 443 -0.0001

SER 443 ALA 444 -0.0060

ALA 444 LEU 445 -0.0003

LEU 445 PRO 446 0.0001

PRO 446 VAL 447 -0.0003

VAL 447 VAL 448 -0.0001

VAL 448 THR 449 -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).
Last modification: October 18th, 2018.

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

*** TRANSFERASE 31-MAR-06 2CJD ***

CA strain for 220405004109145553

--- normal mode 13 ---

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

* TRANSFERASE 31-MAR-06 2CJD *