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

* *

CA strain for 2407051425092282339

--- 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
ALA 1 SER 2 0.0001

SER 2 LEU 3 0.0753

LEU 3 ARG 4 0.0001

ARG 4 ALA 5 -0.0029

ALA 5 ASN 6 -0.0002

ASN 6 ASP 7 -0.0195

ASP 7 ALA 8 -0.0004

ALA 8 PRO 9 -0.0443

PRO 9 ILE 10 0.0001

ILE 10 VAL 11 -0.0550

VAL 11 LEU 12 0.0003

LEU 12 LEU 13 -0.0431

LEU 13 HIS 14 0.0001

HIS 14 GLY 15 0.0352

GLY 15 PHE 16 0.0000

PHE 16 THR 17 0.0123

THR 17 GLY 18 -0.0001

GLY 18 TRP 19 0.0325

TRP 19 GLY 20 0.0001

GLY 20 ARG 21 0.0381

ARG 21 GLU 22 -0.0001

GLU 22 GLU 23 -0.0603

GLU 23 MET 24 0.0001

MET 24 PHE 25 0.0569

PHE 25 GLY 26 -0.0002

GLY 26 PHE 27 -0.1371

PHE 27 LYS 28 -0.0002

LYS 28 TYR 29 0.0182

TYR 29 TRP 30 0.0001

TRP 30 GLY 31 0.0093

GLY 31 GLY 32 0.0002

GLY 32 VAL 33 -0.0045

VAL 33 ARG 34 0.0000

ARG 34 GLY 35 0.0110

GLY 35 ASP 36 -0.0002

ASP 36 ILE 37 -0.0025

ILE 37 GLU 38 0.0000

GLU 38 GLN 39 -0.0027

GLN 39 TRP 40 0.0001

TRP 40 LEU 41 0.0352

LEU 41 ASN 42 0.0001

ASN 42 ASP 43 -0.0144

ASP 43 ASN 44 -0.0003

ASN 44 GLY 45 0.0179

GLY 45 TYR 46 0.0002

TYR 46 ARG 47 -0.0454

ARG 47 THR 48 0.0000

THR 48 TYR 49 -0.1004

TYR 49 THR 50 -0.0003

THR 50 LEU 51 -0.1169

LEU 51 ALA 52 -0.0001

ALA 52 VAL 53 -0.0191

VAL 53 GLY 54 -0.0000

GLY 54 PRO 55 0.0064

PRO 55 LEU 56 -0.0004

LEU 56 SER 57 -0.0386

SER 57 SER 58 0.0000

SER 58 ASN 59 -0.0323

ASN 59 TRP 60 -0.0001

TRP 60 ASP 61 0.0353

ASP 61 ARG 62 -0.0000

ARG 62 ALA 63 -0.0318

ALA 63 CYS 64 -0.0000

CYS 64 GLU 65 0.0416

GLU 65 ALA 66 0.0002

ALA 66 TYR 67 -0.0117

TYR 67 ALA 68 0.0001

ALA 68 GLN 69 -0.0389

GLN 69 LEU 70 0.0001

LEU 70 VAL 71 0.0213

VAL 71 GLY 72 0.0002

GLY 72 GLY 73 -0.1852

GLY 73 THR 74 0.0000

THR 74 VAL 75 0.0472

VAL 75 ASP 76 -0.0004

ASP 76 TYR 77 -0.0172

TYR 77 GLY 78 0.0000

GLY 78 ALA 79 -0.0216

ALA 79 ALA 80 -0.0001

ALA 80 HIS 81 0.0087

HIS 81 ALA 82 -0.0001

ALA 82 ALA 83 0.0007

ALA 83 LYS 84 -0.0001

LYS 84 HIS 85 -0.0284

HIS 85 GLY 86 -0.0004

GLY 86 HIS 87 -0.0239

HIS 87 ALA 88 -0.0001

ALA 88 ARG 89 -0.0815

ARG 89 PHE 90 -0.0003

PHE 90 GLY 91 0.0268

GLY 91 ARG 92 -0.0004

ARG 92 THR 93 -0.1214

THR 93 TYR 94 0.0002

TYR 94 PRO 95 -0.0437

PRO 95 GLY 96 0.0001

GLY 96 LEU 97 -0.1431

LEU 97 LEU 98 0.0003

LEU 98 PRO 99 0.0687

PRO 99 GLU 100 0.0000

GLU 100 LEU 101 0.0022

LEU 101 LYS 102 -0.0002

LYS 102 ARG 103 -0.1463

ARG 103 GLY 104 -0.0002

GLY 104 GLY 105 0.0144

GLY 105 ARG 106 0.0001

ARG 106 ILE 107 0.0159

ILE 107 HIS 108 0.0001

HIS 108 ILE 109 0.0068

ILE 109 ILE 110 0.0000

ILE 110 ALA 111 0.0104

ALA 111 HIS 112 0.0001

HIS 112 SER 113 0.0268

SER 113 GLN 114 0.0002

GLN 114 GLY 115 -0.0156

GLY 115 GLY 116 0.0001

GLY 116 GLN 117 0.0094

GLN 117 THR 118 -0.0000

THR 118 ALA 119 -0.0493

ALA 119 ARG 120 -0.0002

ARG 120 MET 121 0.0954

MET 121 LEU 122 -0.0001

LEU 122 VAL 123 -0.0175

VAL 123 SER 124 -0.0001

SER 124 LEU 125 0.0518

LEU 125 LEU 126 0.0000

LEU 126 GLU 127 0.0055

GLU 127 ASN 128 0.0002

ASN 128 GLY 129 0.1086

GLY 129 SER 130 0.0003

SER 130 GLN 131 -0.0261

GLN 131 GLU 132 -0.0000

GLU 132 GLU 133 -0.0039

GLU 133 ARG 134 0.0002

ARG 134 GLU 135 -0.0015

GLU 135 TYR 136 -0.0000

TYR 136 ALA 137 -0.0355

ALA 137 LYS 138 0.0001

LYS 138 ALA 139 -0.0467

ALA 139 HIS 140 -0.0002

HIS 140 ASN 141 -0.0169

ASN 141 VAL 142 0.0002

VAL 142 SER 143 -0.0126

SER 143 LEU 144 -0.0003

LEU 144 SER 145 -0.1280

SER 145 PRO 146 0.0002

PRO 146 LEU 147 0.0032

LEU 147 PHE 148 -0.0002

PHE 148 GLU 149 -0.0085

GLU 149 GLY 150 -0.0003

GLY 150 GLY 151 0.0193

GLY 151 HIS 152 0.0003

HIS 152 HIS 153 0.0063

HIS 153 PHE 154 0.0000

PHE 154 VAL 155 -0.0208

VAL 155 LEU 156 -0.0001

LEU 156 SER 157 0.0038

SER 157 VAL 158 -0.0003

VAL 158 THR 159 0.0339

THR 159 THR 160 0.0002

THR 160 ILE 161 0.0261

ILE 161 ALA 162 -0.0000

ALA 162 THR 163 0.0161

THR 163 PRO 164 0.0003

PRO 164 HIS 165 -0.0252

HIS 165 ASP 166 0.0000

ASP 166 GLY 167 -0.0468

GLY 167 THR 168 -0.0001

THR 168 THR 169 -0.0200

THR 169 LEU 170 -0.0001

LEU 170 VAL 171 0.0497

VAL 171 ASN 172 -0.0001

ASN 172 MET 173 -0.0770

MET 173 VAL 174 0.0000

VAL 174 ASP 175 0.1027

ASP 175 PHE 176 -0.0001

PHE 176 THR 177 0.1863

THR 177 ASP 178 -0.0000

ASP 178 ARG 179 0.0200

ARG 179 PHE 180 -0.0003

PHE 180 PHE 181 0.1083

PHE 181 ASP 182 0.0000

ASP 182 LEU 183 0.0225

LEU 183 GLN 184 -0.0001

GLN 184 LYS 185 -0.0191

LYS 185 ALA 186 -0.0004

ALA 186 VAL 187 0.0012

VAL 187 LEU 188 -0.0003

LEU 188 GLU 189 0.0075

GLU 189 ALA 190 -0.0002

ALA 190 ALA 191 -0.0355

ALA 191 ALA 192 -0.0000

ALA 192 VAL 193 0.0509

VAL 193 ALA 194 0.0000

ALA 194 SER 195 -0.1009

SER 195 ASN 196 -0.0002

ASN 196 VAL 197 0.0020

VAL 197 PRO 198 0.0003

PRO 198 TYR 199 -0.0151

TYR 199 THR 200 -0.0003

THR 200 SER 201 0.0106

SER 201 GLN 202 -0.0000

GLN 202 VAL 203 -0.2266

VAL 203 TYR 204 0.0002

TYR 204 ASP 205 0.1180

ASP 205 PHE 206 0.0004

PHE 206 LYS 207 0.0307

LYS 207 LEU 208 0.0002

LEU 208 ASP 209 -0.0030

ASP 209 GLN 210 0.0002

GLN 210 TRP 211 -0.1022

TRP 211 GLY 212 -0.0000

GLY 212 LEU 213 -0.0389

LEU 213 ARG 214 -0.0001

ARG 214 ARG 215 -0.0229

ARG 215 GLN 216 -0.0001

GLN 216 PRO 217 0.0852

PRO 217 GLY 218 -0.0000

GLY 218 GLU 219 0.1175

GLU 219 SER 220 0.0001

SER 220 PHE 221 -0.1086

PHE 221 ASP 222 0.0001

ASP 222 HIS 223 -0.0642

HIS 223 TYR 224 -0.0002

TYR 224 PHE 225 0.0839

PHE 225 GLU 226 0.0000

GLU 226 ARG 227 -0.0453

ARG 227 LEU 228 -0.0000

LEU 228 LYS 229 0.0911

LYS 229 ARG 230 -0.0002

ARG 230 SER 231 -0.1267

SER 231 PRO 232 0.0002

PRO 232 VAL 233 -0.0261

VAL 233 TRP 234 0.0002

TRP 234 THR 235 -0.0265

THR 235 SER 236 0.0003

SER 236 THR 237 0.1070

THR 237 ASP 238 -0.0002

ASP 238 THR 239 -0.0409

THR 239 ALA 240 -0.0001

ALA 240 ARG 241 -0.0476

ARG 241 TYR 242 -0.0001

TYR 242 ASP 243 -0.0550

ASP 243 LEU 244 0.0001

LEU 244 SER 245 0.0470

SER 245 VAL 246 0.0001

VAL 246 SER 247 0.0205

SER 247 GLY 248 -0.0001

GLY 248 ALA 249 0.0384

ALA 249 GLU 250 -0.0001

GLU 250 LYS 251 0.0335

LYS 251 LEU 252 -0.0002

LEU 252 ASN 253 0.0680

ASN 253 GLN 254 -0.0000

GLN 254 TRP 255 0.0235

TRP 255 VAL 256 -0.0001

VAL 256 GLN 257 0.0071

GLN 257 ALA 258 -0.0002

ALA 258 SER 259 -0.0570

SER 259 PRO 260 -0.0003

PRO 260 ASN 261 -0.0084

ASN 261 THR 262 0.0002

THR 262 TYR 263 0.0061

TYR 263 TYR 264 -0.0001

TYR 264 LEU 265 0.0483

LEU 265 SER 266 -0.0000

SER 266 PHE 267 0.0307

PHE 267 SER 268 -0.0001

SER 268 THR 269 0.0828

THR 269 GLU 270 -0.0004

GLU 270 ARG 271 0.0545

ARG 271 THR 272 0.0001

THR 272 TYR 273 0.0099

TYR 273 ARG 274 0.0002

ARG 274 GLY 275 0.0369

GLY 275 ALA 276 -0.0000

ALA 276 LEU 277 0.0814

LEU 277 THR 278 -0.0002

THR 278 GLY 279 0.1567

GLY 279 ASN 280 -0.0004

ASN 280 HIS 281 0.0258

HIS 281 TYR 282 -0.0001

TYR 282 PRO 283 -0.1404

PRO 283 GLU 284 -0.0004

GLU 284 LEU 285 0.0158

LEU 285 GLY 286 0.0002

GLY 286 MET 287 -0.0461

MET 287 ASN 288 -0.0003

ASN 288 ALA 289 0.1026

ALA 289 PHE 290 0.0002

PHE 290 SER 291 -0.0393

SER 291 ALA 292 0.0002

ALA 292 VAL 293 0.0665

VAL 293 VAL 294 0.0000

VAL 294 CYS 295 0.0127

CYS 295 ALA 296 0.0001

ALA 296 PRO 297 0.0184

PRO 297 PHE 298 0.0001

PHE 298 LEU 299 0.0006

LEU 299 GLY 300 -0.0001

GLY 300 SER 301 -0.0038

SER 301 TYR 302 0.0002

TYR 302 ARG 303 0.0339

ARG 303 ASN 304 0.0002

ASN 304 PRO 305 0.0698

PRO 305 THR 306 -0.0000

THR 306 LEU 307 0.0404

LEU 307 GLY 308 0.0001

GLY 308 ILE 309 -0.0306

ILE 309 ASP 310 0.0000

ASP 310 ASP 311 0.0042

ASP 311 ARG 312 0.0002

ARG 312 TRP 313 0.0520

TRP 313 LEU 314 -0.0000

LEU 314 GLU 315 -0.0423

GLU 315 ASN 316 0.0001

ASN 316 ASP 317 -0.0702

ASP 317 GLY 318 -0.0002

GLY 318 ILE 319 -0.0240

ILE 319 VAL 320 0.0003

VAL 320 ASN 321 -0.0170

ASN 321 THR 322 0.0004

THR 322 VAL 323 -0.0820

VAL 323 SER 324 0.0001

SER 324 MET 325 -0.0200

MET 325 ASN 326 -0.0002

ASN 326 GLY 327 0.0408

GLY 327 PRO 328 -0.0000

PRO 328 LYS 329 -0.0290

LYS 329 ARG 330 0.0004

ARG 330 GLY 331 -0.0012

GLY 331 SER 332 -0.0002

SER 332 SER 333 -0.0364

SER 333 ASP 334 -0.0000

ASP 334 ARG 335 0.0801

ARG 335 ILE 336 0.0004

ILE 336 VAL 337 0.0498

VAL 337 PRO 338 0.0001

PRO 338 TYR 339 -0.0118

TYR 339 ASP 340 -0.0002

ASP 340 GLY 341 0.0285

GLY 341 THR 342 -0.0000

THR 342 LEU 343 -0.0071

LEU 343 LYS 344 -0.0004

LYS 344 LYS 345 0.0545

LYS 345 GLY 346 -0.0004

GLY 346 VAL 347 -0.0143

VAL 347 TRP 348 -0.0002

TRP 348 ASN 349 0.0233

ASN 349 ASP 350 -0.0001

ASP 350 MET 351 -0.0375

MET 351 GLY 352 -0.0002

GLY 352 THR 353 0.1151

THR 353 TYR 354 -0.0003

TYR 354 ASN 355 0.1421

ASN 355 VAL 356 -0.0003

VAL 356 ASP 357 0.0110

ASP 357 HIS 358 0.0001

HIS 358 LEU 359 -0.0779

LEU 359 GLU 360 0.0004

GLU 360 ILE 361 -0.0063

ILE 361 ILE 362 0.0002

ILE 362 GLY 363 -0.0219

GLY 363 VAL 364 0.0003

VAL 364 ASP 365 -0.0212

ASP 365 PRO 366 0.0002

PRO 366 ASN 367 -0.0623

ASN 367 PRO 368 -0.0001

PRO 368 SER 369 0.0069

SER 369 PHE 370 0.0003

PHE 370 ASP 371 0.0208

ASP 371 ILE 372 0.0002

ILE 372 ARG 373 0.0447

ARG 373 ALA 374 0.0001

ALA 374 PHE 375 -0.0258

PHE 375 TYR 376 -0.0001

TYR 376 LEU 377 0.0273

LEU 377 ARG 378 0.0000

ARG 378 LEU 379 -0.0220

LEU 379 ALA 380 -0.0000

ALA 380 GLU 381 -0.0097

GLU 381 GLN 382 0.0003

GLN 382 LEU 383 -0.0187

LEU 383 ALA 384 0.0005

ALA 384 SER 385 -0.0105

SER 385 LEU 386 -0.0003

LEU 386 ARG 387 0.0150

ARG 387 PRO 388 0.0001

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.

*** ***

CA strain for 2407051425092282339

--- normal mode 11 ---

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

* *