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

* *

CA strain for 2404232236172138714

--- 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
SER 19 VAL 20 0.0000

VAL 20 ASP 21 -0.0017

ASP 21 GLN 22 0.0002

GLN 22 ALA 23 0.0363

ALA 23 THR 24 0.0002

THR 24 LEU 25 -0.0073

LEU 25 ASP 26 -0.0001

ASP 26 LYS 27 0.0422

LYS 27 LEU 28 0.0002

LEU 28 GLU 29 0.0333

GLU 29 ALA 30 -0.0002

ALA 30 GLY 31 0.0359

GLY 31 PHE 32 -0.0001

PHE 32 LYS 33 0.0109

LYS 33 LYS 34 -0.0000

LYS 34 LEU 35 -0.0225

LEU 35 GLN 36 0.0002

GLN 36 ASP 37 -0.0041

ASP 37 ALA 38 -0.0001

ALA 38 LYS 39 0.0529

LYS 39 ASP 40 0.0000

ASP 40 CYS 41 0.0502

CYS 41 LYS 42 0.0000

LYS 42 SER 43 0.0345

SER 43 LEU 44 0.0001

LEU 44 LEU 45 0.0348

LEU 45 LYS 46 0.0001

LYS 46 LYS 47 -0.0407

LYS 47 TYR 48 -0.0004

TYR 48 LEU 49 -0.0418

LEU 49 THR 50 -0.0001

THR 50 LYS 51 -0.0443

LYS 51 GLU 52 -0.0001

GLU 52 ILE 53 -0.0284

ILE 53 PHE 54 -0.0003

PHE 54 ASP 55 -0.0013

ASP 55 ARG 56 -0.0004

ARG 56 LEU 57 0.0131

LEU 57 LYS 58 -0.0003

LYS 58 THR 59 0.0094

THR 59 ARG 60 0.0000

ARG 60 LYS 61 0.0466

LYS 61 THR 62 -0.0001

THR 62 ALA 63 -0.0105

ALA 63 MET 64 0.0001

MET 64 GLY 65 0.0161

GLY 65 ALA 66 -0.0004

ALA 66 THR 67 0.0371

THR 67 LEU 68 -0.0002

LEU 68 LEU 69 0.0075

LEU 69 ASP 70 0.0002

ASP 70 VAL 71 0.0556

VAL 71 ILE 72 0.0002

ILE 72 GLN 73 0.0315

GLN 73 SER 74 -0.0002

SER 74 GLY 75 0.0310

GLY 75 VAL 76 -0.0001

VAL 76 GLU 77 0.0596

GLU 77 ASN 78 0.0002

ASN 78 LEU 79 0.0717

LEU 79 ASP 80 -0.0003

ASP 80 SER 81 0.0264

SER 81 GLY 82 0.0001

GLY 82 VAL 83 -0.0206

VAL 83 GLY 84 -0.0001

GLY 84 VAL 85 -0.0301

VAL 85 TYR 86 -0.0003

TYR 86 ALA 87 -0.0607

ALA 87 PRO 88 0.0004

PRO 88 ASP 89 -0.0064

ASP 89 ALA 90 -0.0001

ALA 90 GLU 91 -0.0614

GLU 91 SER 92 -0.0001

SER 92 TYR 93 0.0634

TYR 93 THR 94 0.0001

THR 94 VAL 95 -0.0754

VAL 95 PHE 96 -0.0002

PHE 96 ALA 97 0.0185

ALA 97 ASP 98 -0.0004

ASP 98 LEU 99 0.0165

LEU 99 PHE 100 -0.0002

PHE 100 ASN 101 0.0232

ASN 101 PRO 102 -0.0001

PRO 102 VAL 103 -0.0231

VAL 103 ILE 104 0.0000

ILE 104 GLU 105 0.0320

GLU 105 ASP 106 0.0002

ASP 106 TYR 107 -0.0844

TYR 107 HIS 108 0.0001

HIS 108 GLY 109 0.0034

GLY 109 GLY 110 -0.0000

GLY 110 PHE 111 -0.0186

PHE 111 LYS 112 -0.0001

LYS 112 PRO 113 -0.0033

PRO 113 THR 114 -0.0002

THR 114 ASP 115 0.0067

ASP 115 LYS 116 -0.0003

LYS 116 HIS 117 0.0229

HIS 117 PRO 118 0.0001

PRO 118 PRO 119 -0.0496

PRO 119 THR 120 -0.0000

THR 120 ASP 121 0.1349

ASP 121 PHE 122 -0.0002

PHE 122 GLY 123 0.0655

GLY 123 ASP 124 -0.0001

ASP 124 MET 125 -0.0493

MET 125 ASN 126 -0.0001

ASN 126 THR 127 -0.0390

THR 127 ILE 128 -0.0000

ILE 128 VAL 129 0.2629

VAL 129 ASN 130 0.0002

ASN 130 VAL 131 -0.0244

VAL 131 ASP 132 -0.0002

ASP 132 PRO 133 0.0030

PRO 133 GLU 134 -0.0003

GLU 134 ASN 135 -0.1341

ASN 135 LYS 136 0.0001

LYS 136 TYR 137 -0.0436

TYR 137 VAL 138 -0.0001

VAL 138 VAL 139 -0.0894

VAL 139 SER 140 -0.0001

SER 140 THR 141 0.0504

THR 141 ARG 142 0.0002

ARG 142 VAL 143 0.0243

VAL 143 ARG 144 -0.0002

ARG 144 CYS 145 0.0125

CYS 145 GLY 146 -0.0001

GLY 146 ARG 147 -0.0015

ARG 147 SER 148 -0.0001

SER 148 LEU 149 -0.0023

LEU 149 GLN 150 0.0004

GLN 150 GLY 151 0.0171

GLY 151 TYR 152 0.0003

TYR 152 PRO 153 -0.0515

PRO 153 PHE 154 0.0004

PHE 154 ASN 155 -0.0000

ASN 155 PRO 156 -0.0001

PRO 156 CYS 157 -0.0552

CYS 157 LEU 158 -0.0005

LEU 158 THR 159 0.0494

THR 159 GLU 160 -0.0002

GLU 160 ALA 161 -0.0025

ALA 161 GLN 162 -0.0005

GLN 162 TYR 163 -0.0211

TYR 163 LYS 164 0.0003

LYS 164 GLU 165 0.0198

GLU 165 MET 166 0.0002

MET 166 GLU 167 -0.0192

GLU 167 ASP 168 0.0001

ASP 168 LYS 169 0.0001

LYS 169 VAL 170 0.0000

VAL 170 SER 171 -0.0139

SER 171 SER 172 -0.0000

SER 172 GLN 173 -0.0193

GLN 173 LEU 174 -0.0001

LEU 174 LYS 175 -0.0109

LYS 175 GLY 176 0.0000

GLY 176 MET 177 -0.0261

MET 177 THR 178 -0.0001

THR 178 GLY 179 0.0025

GLY 179 ASP 180 0.0001

ASP 180 LEU 181 -0.0044

LEU 181 LYS 182 0.0002

LYS 182 GLY 183 -0.0599

GLY 183 THR 184 0.0000

THR 184 TYR 185 -0.0100

TYR 185 TYR 186 -0.0003

TYR 186 PRO 187 -0.0090

PRO 187 LEU 188 0.0001

LEU 188 THR 189 -0.0480

THR 189 GLY 190 -0.0000

GLY 190 MET 191 0.0582

MET 191 ASP 192 -0.0001

ASP 192 LYS 193 0.0439

LYS 193 LYS 194 -0.0000

LYS 194 THR 195 -0.1951

THR 195 GLN 196 -0.0000

GLN 196 GLN 197 0.0213

GLN 197 GLN 198 -0.0001

GLN 198 LEU 199 0.0099

LEU 199 ILE 200 -0.0003

ILE 200 ASP 201 -0.0379

ASP 201 ASP 202 -0.0003

ASP 202 HIS 203 0.0008

HIS 203 PHE 204 0.0000

PHE 204 LEU 205 -0.1399

LEU 205 PHE 206 0.0000

PHE 206 LYS 207 -0.0293

LYS 207 GLU 208 0.0004

GLU 208 GLY 209 0.2620

GLY 209 ASP 210 -0.0000

ASP 210 ARG 211 0.1890

ARG 211 PHE 212 0.0001

PHE 212 LEU 213 0.0090

LEU 213 GLN 214 -0.0001

GLN 214 ALA 215 0.1696

ALA 215 ALA 216 -0.0000

ALA 216 ASN 217 0.0336

ASN 217 ALA 218 0.0003

ALA 218 CYS 219 0.0901

CYS 219 ARG 220 -0.0000

ARG 220 TYR 221 0.1203

TYR 221 TRP 222 -0.0000

TRP 222 PRO 223 0.0974

PRO 223 THR 224 0.0003

THR 224 GLY 225 -0.0064

GLY 225 ARG 226 -0.0001

ARG 226 GLY 227 -0.0328

GLY 227 ILE 228 -0.0001

ILE 228 TYR 229 0.0221

TYR 229 HIS 230 -0.0000

HIS 230 ASN 231 -0.0043

ASN 231 ASP 232 0.0001

ASP 232 ALA 233 0.0365

ALA 233 LYS 234 0.0003

LYS 234 THR 235 -0.1948

THR 235 PHE 236 -0.0001

PHE 236 LEU 237 -0.0577

LEU 237 VAL 238 -0.0002

VAL 238 TRP 239 0.0273

TRP 239 VAL 240 -0.0004

VAL 240 ASN 241 0.0244

ASN 241 GLU 242 -0.0002

GLU 242 GLU 243 0.0402

GLU 243 ASP 244 -0.0002

ASP 244 HIS 245 0.0255

HIS 245 LEU 246 0.0000

LEU 246 ARG 247 -0.0125

ARG 247 ILE 248 -0.0001

ILE 248 ILE 249 -0.0019

ILE 249 SER 250 0.0004

SER 250 MET 251 0.0362

MET 251 GLN 252 -0.0003

GLN 252 GLN 253 0.0335

GLN 253 GLY 254 0.0001

GLY 254 GLY 255 -0.1469

GLY 255 ASP 256 -0.0002

ASP 256 LEU 257 0.0545

LEU 257 LYS 258 0.0001

LYS 258 GLN 259 -0.1690

GLN 259 VAL 260 -0.0001

VAL 260 TYR 261 0.0428

TYR 261 SER 262 -0.0001

SER 262 ARG 263 -0.2027

ARG 263 MET 264 0.0001

MET 264 VAL 265 0.0091

VAL 265 SER 266 -0.0001

SER 266 GLY 267 -0.0421

GLY 267 VAL 268 -0.0001

VAL 268 LYS 269 0.0175

LYS 269 GLU 270 0.0002

GLU 270 ILE 271 0.0005

ILE 271 GLU 272 -0.0000

GLU 272 LYS 273 -0.0492

LYS 273 LYS 274 0.0001

LYS 274 LEU 275 -0.0151

LEU 275 PRO 276 0.0001

PRO 276 PHE 277 -0.0755

PHE 277 SER 278 -0.0004

SER 278 ARG 279 -0.0196

ARG 279 ASP 280 0.0002

ASP 280 ASP 281 -0.0018

ASP 281 ARG 282 -0.0003

ARG 282 LEU 283 0.0066

LEU 283 GLY 284 -0.0003

GLY 284 PHE 285 -0.0322

PHE 285 LEU 286 -0.0002

LEU 286 THR 287 0.0394

THR 287 PHE 288 -0.0002

PHE 288 CYS 289 0.0049

CYS 289 PRO 290 -0.0002

PRO 290 THR 291 -0.0031

THR 291 ASN 292 -0.0002

ASN 292 LEU 293 -0.0428

LEU 293 GLY 294 -0.0000

GLY 294 THR 295 0.0691

THR 295 THR 296 0.0002

THR 296 ILE 297 0.0109

ILE 297 ARG 298 0.0003

ARG 298 ALA 299 0.0365

ALA 299 SER 300 -0.0002

SER 300 VAL 301 -0.0322

VAL 301 HIS 302 0.0001

HIS 302 ILE 303 -0.0121

ILE 303 LYS 304 0.0000

LYS 304 LEU 305 0.0665

LEU 305 PRO 306 -0.0001

PRO 306 LYS 307 0.0440

LYS 307 LEU 308 0.0001

LEU 308 ALA 309 0.0176

ALA 309 ALA 310 0.0003

ALA 310 ASP 311 0.0127

ASP 311 LYS 312 -0.0001

LYS 312 ALA 313 0.1627

ALA 313 LYS 314 -0.0000

LYS 314 LEU 315 -0.0158

LEU 315 ASP 316 -0.0001

ASP 316 SER 317 0.1694

SER 317 ILE 318 0.0004

ILE 318 ALA 319 0.0133

ALA 319 ALA 320 -0.0001

ALA 320 LYS 321 0.1319

LYS 321 TYR 322 -0.0000

TYR 322 ASN 323 0.2706

ASN 323 LEU 324 -0.0001

LEU 324 GLN 325 0.1127

GLN 325 VAL 326 0.0000

VAL 326 ARG 327 0.2293

ARG 327 GLY 328 -0.0004

GLY 328 THR 329 0.1129

THR 329 ARG 330 0.0004

ARG 330 GLY 331 -0.0044

GLY 331 GLU 332 0.0003

GLU 332 HIS 333 -0.0262

HIS 333 THR 334 0.0002

THR 334 GLU 335 -0.0913

GLU 335 SER 336 -0.0002

SER 336 GLU 337 0.0425

GLU 337 GLY 338 0.0000

GLY 338 GLY 339 -0.0521

GLY 339 VAL 340 -0.0000

VAL 340 TYR 341 -0.0472

TYR 341 ASP 342 -0.0000

ASP 342 ILE 343 0.0231

ILE 343 SER 344 0.0004

SER 344 ASN 345 -0.0226

ASN 345 LYS 346 -0.0002

LYS 346 ARG 347 -0.0672

ARG 347 ARG 348 0.0000

ARG 348 MET 349 -0.0868

MET 349 GLY 350 -0.0003

GLY 350 LEU 351 0.1384

LEU 351 THR 352 -0.0001

THR 352 GLU 353 -0.0065

GLU 353 TYR 354 0.0002

TYR 354 GLN 355 -0.0417

GLN 355 ALA 356 -0.0000

ALA 356 VAL 357 0.0881

VAL 357 ARG 358 0.0002

ARG 358 GLU 359 -0.1438

GLU 359 MET 360 0.0002

MET 360 GLN 361 0.1220

GLN 361 ASP 362 -0.0002

ASP 362 GLY 363 -0.1635

GLY 363 ILE 364 0.0002

ILE 364 GLN 365 0.0484

GLN 365 GLU 366 0.0000

GLU 366 LEU 367 0.0079

LEU 367 ILE 368 -0.0001

ILE 368 LYS 369 -0.0879

LYS 369 LEU 370 0.0003

LEU 370 GLU 371 0.0136

GLU 371 GLN 372 0.0002

GLN 372 ALA 373 -0.0516

ALA 373 ALA 374 0.0004

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 11 ---

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

* *