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

* *

CA strain for 2404232236172138714

--- 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
SER 19 VAL 20 -0.0002

VAL 20 ASP 21 -0.0220

ASP 21 GLN 22 -0.0001

GLN 22 ALA 23 -0.0396

ALA 23 THR 24 -0.0000

THR 24 LEU 25 0.0094

LEU 25 ASP 26 -0.0002

ASP 26 LYS 27 -0.0231

LYS 27 LEU 28 0.0000

LEU 28 GLU 29 -0.0901

GLU 29 ALA 30 0.0002

ALA 30 GLY 31 -0.0043

GLY 31 PHE 32 0.0002

PHE 32 LYS 33 -0.0342

LYS 33 LYS 34 -0.0005

LYS 34 LEU 35 0.0475

LEU 35 GLN 36 0.0000

GLN 36 ASP 37 -0.0576

ASP 37 ALA 38 -0.0001

ALA 38 LYS 39 -0.0185

LYS 39 ASP 40 -0.0002

ASP 40 CYS 41 0.0744

CYS 41 LYS 42 -0.0003

LYS 42 SER 43 0.1334

SER 43 LEU 44 0.0004

LEU 44 LEU 45 0.0271

LEU 45 LYS 46 0.0002

LYS 46 LYS 47 0.0775

LYS 47 TYR 48 -0.0004

TYR 48 LEU 49 0.1787

LEU 49 THR 50 0.0000

THR 50 LYS 51 0.1445

LYS 51 GLU 52 0.0002

GLU 52 ILE 53 0.0225

ILE 53 PHE 54 0.0003

PHE 54 ASP 55 0.0318

ASP 55 ARG 56 0.0000

ARG 56 LEU 57 -0.0275

LEU 57 LYS 58 0.0004

LYS 58 THR 59 -0.0097

THR 59 ARG 60 -0.0003

ARG 60 LYS 61 -0.1524

LYS 61 THR 62 0.0002

THR 62 ALA 63 -0.0203

ALA 63 MET 64 0.0002

MET 64 GLY 65 -0.2182

GLY 65 ALA 66 -0.0000

ALA 66 THR 67 -0.2041

THR 67 LEU 68 -0.0000

LEU 68 LEU 69 0.0256

LEU 69 ASP 70 0.0001

ASP 70 VAL 71 -0.0425

VAL 71 ILE 72 0.0003

ILE 72 GLN 73 -0.0297

GLN 73 SER 74 -0.0002

SER 74 GLY 75 -0.0029

GLY 75 VAL 76 0.0000

VAL 76 GLU 77 -0.0005

GLU 77 ASN 78 -0.0001

ASN 78 LEU 79 0.0313

LEU 79 ASP 80 -0.0004

ASP 80 SER 81 0.0148

SER 81 GLY 82 -0.0004

GLY 82 VAL 83 0.0860

VAL 83 GLY 84 -0.0003

GLY 84 VAL 85 0.0298

VAL 85 TYR 86 0.0001

TYR 86 ALA 87 0.0420

ALA 87 PRO 88 -0.0000

PRO 88 ASP 89 0.0094

ASP 89 ALA 90 -0.0003

ALA 90 GLU 91 -0.1334

GLU 91 SER 92 -0.0002

SER 92 TYR 93 -0.0593

TYR 93 THR 94 -0.0001

THR 94 VAL 95 -0.0172

VAL 95 PHE 96 0.0002

PHE 96 ALA 97 0.0429

ALA 97 ASP 98 -0.0000

ASP 98 LEU 99 -0.0224

LEU 99 PHE 100 0.0001

PHE 100 ASN 101 0.0397

ASN 101 PRO 102 0.0001

PRO 102 VAL 103 0.0077

VAL 103 ILE 104 0.0002

ILE 104 GLU 105 -0.0331

GLU 105 ASP 106 0.0002

ASP 106 TYR 107 0.1103

TYR 107 HIS 108 -0.0002

HIS 108 GLY 109 -0.0680

GLY 109 GLY 110 0.0001

GLY 110 PHE 111 -0.0153

PHE 111 LYS 112 -0.0001

LYS 112 PRO 113 0.0171

PRO 113 THR 114 -0.0003

THR 114 ASP 115 -0.0008

ASP 115 LYS 116 -0.0002

LYS 116 HIS 117 -0.0093

HIS 117 PRO 118 0.0002

PRO 118 PRO 119 0.0355

PRO 119 THR 120 0.0001

THR 120 ASP 121 0.0229

ASP 121 PHE 122 -0.0002

PHE 122 GLY 123 -0.0060

GLY 123 ASP 124 0.0001

ASP 124 MET 125 -0.0315

MET 125 ASN 126 -0.0002

ASN 126 THR 127 0.0459

THR 127 ILE 128 0.0001

ILE 128 VAL 129 -0.0128

VAL 129 ASN 130 0.0000

ASN 130 VAL 131 0.0726

VAL 131 ASP 132 -0.0002

ASP 132 PRO 133 -0.0323

PRO 133 GLU 134 0.0005

GLU 134 ASN 135 -0.0016

ASN 135 LYS 136 0.0004

LYS 136 TYR 137 -0.0335

TYR 137 VAL 138 0.0004

VAL 138 VAL 139 0.0829

VAL 139 SER 140 -0.0001

SER 140 THR 141 -0.0124

THR 141 ARG 142 -0.0002

ARG 142 VAL 143 0.0413

VAL 143 ARG 144 -0.0001

ARG 144 CYS 145 -0.0056

CYS 145 GLY 146 -0.0004

GLY 146 ARG 147 -0.0513

ARG 147 SER 148 -0.0001

SER 148 LEU 149 -0.0425

LEU 149 GLN 150 0.0002

GLN 150 GLY 151 0.0051

GLY 151 TYR 152 -0.0001

TYR 152 PRO 153 -0.1966

PRO 153 PHE 154 0.0003

PHE 154 ASN 155 0.0456

ASN 155 PRO 156 0.0001

PRO 156 CYS 157 0.0173

CYS 157 LEU 158 -0.0001

LEU 158 THR 159 -0.0554

THR 159 GLU 160 0.0002

GLU 160 ALA 161 -0.0219

ALA 161 GLN 162 -0.0002

GLN 162 TYR 163 -0.0175

TYR 163 LYS 164 0.0003

LYS 164 GLU 165 0.0364

GLU 165 MET 166 0.0001

MET 166 GLU 167 -0.0631

GLU 167 ASP 168 0.0000

ASP 168 LYS 169 0.0256

LYS 169 VAL 170 -0.0003

VAL 170 SER 171 -0.0352

SER 171 SER 172 0.0001

SER 172 GLN 173 0.0128

GLN 173 LEU 174 0.0002

LEU 174 LYS 175 -0.0169

LYS 175 GLY 176 -0.0001

GLY 176 MET 177 0.0443

MET 177 THR 178 0.0001

THR 178 GLY 179 0.0697

GLY 179 ASP 180 -0.0001

ASP 180 LEU 181 -0.0244

LEU 181 LYS 182 0.0000

LYS 182 GLY 183 -0.0472

GLY 183 THR 184 -0.0004

THR 184 TYR 185 -0.0204

TYR 185 TYR 186 -0.0003

TYR 186 PRO 187 0.0238

PRO 187 LEU 188 -0.0002

LEU 188 THR 189 -0.0002

THR 189 GLY 190 0.0005

GLY 190 MET 191 0.0312

MET 191 ASP 192 0.0000

ASP 192 LYS 193 0.0184

LYS 193 LYS 194 -0.0002

LYS 194 THR 195 -0.0890

THR 195 GLN 196 0.0002

GLN 196 GLN 197 -0.0072

GLN 197 GLN 198 -0.0001

GLN 198 LEU 199 -0.0173

LEU 199 ILE 200 -0.0001

ILE 200 ASP 201 -0.0004

ASP 201 ASP 202 -0.0000

ASP 202 HIS 203 0.0586

HIS 203 PHE 204 0.0000

PHE 204 LEU 205 -0.0110

LEU 205 PHE 206 0.0000

PHE 206 LYS 207 0.0340

LYS 207 GLU 208 -0.0004

GLU 208 GLY 209 0.2320

GLY 209 ASP 210 -0.0000

ASP 210 ARG 211 0.0971

ARG 211 PHE 212 0.0003

PHE 212 LEU 213 0.0326

LEU 213 GLN 214 0.0001

GLN 214 ALA 215 -0.0596

ALA 215 ALA 216 0.0001

ALA 216 ASN 217 -0.0525

ASN 217 ALA 218 0.0003

ALA 218 CYS 219 -0.0063

CYS 219 ARG 220 -0.0003

ARG 220 TYR 221 -0.0371

TYR 221 TRP 222 0.0002

TRP 222 PRO 223 0.0224

PRO 223 THR 224 -0.0001

THR 224 GLY 225 0.0259

GLY 225 ARG 226 0.0001

ARG 226 GLY 227 -0.0269

GLY 227 ILE 228 -0.0002

ILE 228 TYR 229 -0.0126

TYR 229 HIS 230 -0.0001

HIS 230 ASN 231 -0.0294

ASN 231 ASP 232 0.0001

ASP 232 ALA 233 0.0796

ALA 233 LYS 234 -0.0001

LYS 234 THR 235 -0.0559

THR 235 PHE 236 -0.0000

PHE 236 LEU 237 -0.0146

LEU 237 VAL 238 0.0000

VAL 238 TRP 239 0.0124

TRP 239 VAL 240 -0.0003

VAL 240 ASN 241 -0.0413

ASN 241 GLU 242 0.0002

GLU 242 GLU 243 0.0375

GLU 243 ASP 244 0.0004

ASP 244 HIS 245 0.0008

HIS 245 LEU 246 0.0002

LEU 246 ARG 247 -0.0410

ARG 247 ILE 248 0.0002

ILE 248 ILE 249 0.0399

ILE 249 SER 250 -0.0000

SER 250 MET 251 0.0714

MET 251 GLN 252 -0.0002

GLN 252 GLN 253 0.1944

GLN 253 GLY 254 0.0003

GLY 254 GLY 255 -0.0333

GLY 255 ASP 256 0.0003

ASP 256 LEU 257 -0.0103

LEU 257 LYS 258 -0.0002

LYS 258 GLN 259 -0.0067

GLN 259 VAL 260 -0.0001

VAL 260 TYR 261 0.0083

TYR 261 SER 262 0.0000

SER 262 ARG 263 -0.0546

ARG 263 MET 264 -0.0001

MET 264 VAL 265 -0.0137

VAL 265 SER 266 -0.0001

SER 266 GLY 267 -0.0175

GLY 267 VAL 268 -0.0001

VAL 268 LYS 269 -0.0153

LYS 269 GLU 270 -0.0001

GLU 270 ILE 271 -0.0090

ILE 271 GLU 272 -0.0001

GLU 272 LYS 273 -0.0527

LYS 273 LYS 274 -0.0002

LYS 274 LEU 275 -0.0607

LEU 275 PRO 276 -0.0003

PRO 276 PHE 277 -0.0566

PHE 277 SER 278 -0.0000

SER 278 ARG 279 0.0507

ARG 279 ASP 280 -0.0001

ASP 280 ASP 281 0.0718

ASP 281 ARG 282 0.0003

ARG 282 LEU 283 0.0106

LEU 283 GLY 284 0.0003

GLY 284 PHE 285 0.0605

PHE 285 LEU 286 -0.0004

LEU 286 THR 287 0.0581

THR 287 PHE 288 0.0000

PHE 288 CYS 289 -0.0157

CYS 289 PRO 290 -0.0002

PRO 290 THR 291 -0.1033

THR 291 ASN 292 0.0000

ASN 292 LEU 293 0.0004

LEU 293 GLY 294 -0.0002

GLY 294 THR 295 0.0295

THR 295 THR 296 -0.0002

THR 296 ILE 297 -0.0565

ILE 297 ARG 298 0.0001

ARG 298 ALA 299 -0.0089

ALA 299 SER 300 0.0001

SER 300 VAL 301 -0.0178

VAL 301 HIS 302 0.0001

HIS 302 ILE 303 0.0864

ILE 303 LYS 304 -0.0001

LYS 304 LEU 305 0.0995

LEU 305 PRO 306 -0.0002

PRO 306 LYS 307 0.0529

LYS 307 LEU 308 0.0001

LEU 308 ALA 309 -0.0209

ALA 309 ALA 310 0.0000

ALA 310 ASP 311 -0.0038

ASP 311 LYS 312 -0.0001

LYS 312 ALA 313 0.0392

ALA 313 LYS 314 0.0001

LYS 314 LEU 315 0.0037

LEU 315 ASP 316 0.0001

ASP 316 SER 317 0.0528

SER 317 ILE 318 0.0003

ILE 318 ALA 319 -0.0946

ALA 319 ALA 320 -0.0002

ALA 320 LYS 321 -0.0245

LYS 321 TYR 322 0.0003

TYR 322 ASN 323 -0.2872

ASN 323 LEU 324 0.0003

LEU 324 GLN 325 0.1022

GLN 325 VAL 326 0.0000

VAL 326 ARG 327 -0.0120

ARG 327 GLY 328 0.0002

GLY 328 THR 329 0.0189

THR 329 ARG 330 0.0001

ARG 330 GLY 331 0.0827

GLY 331 GLU 332 -0.0002

GLU 332 HIS 333 0.0649

HIS 333 THR 334 0.0001

THR 334 GLU 335 -0.1758

GLU 335 SER 336 0.0001

SER 336 GLU 337 0.0401

GLU 337 GLY 338 -0.0002

GLY 338 GLY 339 0.0635

GLY 339 VAL 340 -0.0003

VAL 340 TYR 341 -0.0020

TYR 341 ASP 342 -0.0002

ASP 342 ILE 343 0.0284

ILE 343 SER 344 0.0002

SER 344 ASN 345 -0.0496

ASN 345 LYS 346 0.0000

LYS 346 ARG 347 -0.0597

ARG 347 ARG 348 -0.0002

ARG 348 MET 349 -0.0745

MET 349 GLY 350 0.0002

GLY 350 LEU 351 0.0742

LEU 351 THR 352 -0.0000

THR 352 GLU 353 0.0124

GLU 353 TYR 354 -0.0002

TYR 354 GLN 355 0.0205

GLN 355 ALA 356 0.0002

ALA 356 VAL 357 -0.0052

VAL 357 ARG 358 0.0001

ARG 358 GLU 359 0.0790

GLU 359 MET 360 -0.0001

MET 360 GLN 361 -0.0513

GLN 361 ASP 362 0.0001

ASP 362 GLY 363 0.1015

GLY 363 ILE 364 0.0004

ILE 364 GLN 365 -0.0347

GLN 365 GLU 366 -0.0000

GLU 366 LEU 367 0.0229

LEU 367 ILE 368 -0.0003

ILE 368 LYS 369 0.0392

LYS 369 LEU 370 -0.0003

LEU 370 GLU 371 -0.0066

GLU 371 GLN 372 -0.0004

GLN 372 ALA 373 0.0960

ALA 373 ALA 374 0.0003

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 2404232236172138714

--- normal mode 10 ---

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

* *