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

* *

CA strain for 2404232236172138714

--- normal mode 9 ---

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 -0.0003

VAL 20 ASP 21 -0.0552

ASP 21 GLN 22 0.0003

GLN 22 ALA 23 0.0546

ALA 23 THR 24 0.0002

THR 24 LEU 25 -0.0138

LEU 25 ASP 26 0.0001

ASP 26 LYS 27 0.0518

LYS 27 LEU 28 0.0001

LEU 28 GLU 29 0.0128

GLU 29 ALA 30 0.0001

ALA 30 GLY 31 0.0261

GLY 31 PHE 32 0.0000

PHE 32 LYS 33 -0.0087

LYS 33 LYS 34 -0.0000

LYS 34 LEU 35 -0.0314

LEU 35 GLN 36 -0.0001

GLN 36 ASP 37 0.0196

ASP 37 ALA 38 0.0000

ALA 38 LYS 39 -0.0495

LYS 39 ASP 40 0.0004

ASP 40 CYS 41 0.0515

CYS 41 LYS 42 -0.0001

LYS 42 SER 43 0.0774

SER 43 LEU 44 0.0001

LEU 44 LEU 45 -0.0286

LEU 45 LYS 46 0.0001

LYS 46 LYS 47 0.0138

LYS 47 TYR 48 0.0003

TYR 48 LEU 49 -0.1152

LEU 49 THR 50 0.0002

THR 50 LYS 51 -0.1008

LYS 51 GLU 52 0.0003

GLU 52 ILE 53 -0.0284

ILE 53 PHE 54 -0.0002

PHE 54 ASP 55 -0.0216

ASP 55 ARG 56 0.0001

ARG 56 LEU 57 0.0450

LEU 57 LYS 58 0.0002

LYS 58 THR 59 0.0036

THR 59 ARG 60 0.0000

ARG 60 LYS 61 0.1698

LYS 61 THR 62 -0.0002

THR 62 ALA 63 0.0896

ALA 63 MET 64 0.0003

MET 64 GLY 65 0.0081

GLY 65 ALA 66 -0.0001

ALA 66 THR 67 0.0370

THR 67 LEU 68 0.0001

LEU 68 LEU 69 0.0457

LEU 69 ASP 70 0.0004

ASP 70 VAL 71 0.0435

VAL 71 ILE 72 -0.0004

ILE 72 GLN 73 0.0237

GLN 73 SER 74 -0.0001

SER 74 GLY 75 -0.0201

GLY 75 VAL 76 -0.0001

VAL 76 GLU 77 0.0929

GLU 77 ASN 78 0.0001

ASN 78 LEU 79 -0.0651

LEU 79 ASP 80 0.0002

ASP 80 SER 81 0.0468

SER 81 GLY 82 -0.0001

GLY 82 VAL 83 0.0181

VAL 83 GLY 84 0.0002

GLY 84 VAL 85 -0.0313

VAL 85 TYR 86 -0.0001

TYR 86 ALA 87 -0.0186

ALA 87 PRO 88 -0.0000

PRO 88 ASP 89 -0.0456

ASP 89 ALA 90 0.0001

ALA 90 GLU 91 -0.0868

GLU 91 SER 92 -0.0000

SER 92 TYR 93 -0.0540

TYR 93 THR 94 -0.0001

THR 94 VAL 95 -0.2405

VAL 95 PHE 96 -0.0004

PHE 96 ALA 97 -0.1178

ALA 97 ASP 98 -0.0000

ASP 98 LEU 99 0.0375

LEU 99 PHE 100 -0.0000

PHE 100 ASN 101 -0.0026

ASN 101 PRO 102 -0.0001

PRO 102 VAL 103 -0.0197

VAL 103 ILE 104 -0.0000

ILE 104 GLU 105 0.0576

GLU 105 ASP 106 -0.0002

ASP 106 TYR 107 -0.0737

TYR 107 HIS 108 -0.0003

HIS 108 GLY 109 0.0689

GLY 109 GLY 110 -0.0002

GLY 110 PHE 111 0.0265

PHE 111 LYS 112 -0.0004

LYS 112 PRO 113 -0.0761

PRO 113 THR 114 0.0002

THR 114 ASP 115 -0.0644

ASP 115 LYS 116 -0.0001

LYS 116 HIS 117 -0.0766

HIS 117 PRO 118 -0.0001

PRO 118 PRO 119 0.0002

PRO 119 THR 120 0.0000

THR 120 ASP 121 -0.0469

ASP 121 PHE 122 -0.0002

PHE 122 GLY 123 -0.0032

GLY 123 ASP 124 0.0001

ASP 124 MET 125 0.0117

MET 125 ASN 126 -0.0000

ASN 126 THR 127 0.0313

THR 127 ILE 128 0.0001

ILE 128 VAL 129 -0.0736

VAL 129 ASN 130 0.0000

ASN 130 VAL 131 0.0307

VAL 131 ASP 132 -0.0000

ASP 132 PRO 133 -0.0203

PRO 133 GLU 134 -0.0004

GLU 134 ASN 135 0.0467

ASN 135 LYS 136 0.0001

LYS 136 TYR 137 -0.0009

TYR 137 VAL 138 0.0000

VAL 138 VAL 139 0.0423

VAL 139 SER 140 0.0001

SER 140 THR 141 -0.0182

THR 141 ARG 142 -0.0002

ARG 142 VAL 143 -0.0069

VAL 143 ARG 144 0.0001

ARG 144 CYS 145 0.0063

CYS 145 GLY 146 0.0004

GLY 146 ARG 147 -0.0024

ARG 147 SER 148 -0.0000

SER 148 LEU 149 -0.0101

LEU 149 GLN 150 -0.0004

GLN 150 GLY 151 -0.0087

GLY 151 TYR 152 0.0001

TYR 152 PRO 153 -0.0014

PRO 153 PHE 154 -0.0000

PHE 154 ASN 155 -0.0201

ASN 155 PRO 156 -0.0004

PRO 156 CYS 157 -0.0393

CYS 157 LEU 158 0.0004

LEU 158 THR 159 0.0462

THR 159 GLU 160 -0.0004

GLU 160 ALA 161 -0.0280

ALA 161 GLN 162 -0.0001

GLN 162 TYR 163 0.0017

TYR 163 LYS 164 0.0003

LYS 164 GLU 165 -0.0169

GLU 165 MET 166 0.0005

MET 166 GLU 167 0.0155

GLU 167 ASP 168 0.0003

ASP 168 LYS 169 -0.0069

LYS 169 VAL 170 -0.0004

VAL 170 SER 171 -0.0078

SER 171 SER 172 0.0003

SER 172 GLN 173 -0.0006

GLN 173 LEU 174 -0.0001

LEU 174 LYS 175 -0.0047

LYS 175 GLY 176 0.0004

GLY 176 MET 177 0.0138

MET 177 THR 178 0.0003

THR 178 GLY 179 0.0220

GLY 179 ASP 180 0.0004

ASP 180 LEU 181 0.0034

LEU 181 LYS 182 -0.0000

LYS 182 GLY 183 0.0021

GLY 183 THR 184 0.0002

THR 184 TYR 185 0.0395

TYR 185 TYR 186 0.0001

TYR 186 PRO 187 0.0516

PRO 187 LEU 188 -0.0000

LEU 188 THR 189 -0.0242

THR 189 GLY 190 -0.0002

GLY 190 MET 191 0.0271

MET 191 ASP 192 0.0001

ASP 192 LYS 193 0.0019

LYS 193 LYS 194 -0.0001

LYS 194 THR 195 -0.0602

THR 195 GLN 196 0.0001

GLN 196 GLN 197 -0.0214

GLN 197 GLN 198 0.0002

GLN 198 LEU 199 -0.0077

LEU 199 ILE 200 0.0001

ILE 200 ASP 201 0.0206

ASP 201 ASP 202 -0.0001

ASP 202 HIS 203 -0.0155

HIS 203 PHE 204 0.0001

PHE 204 LEU 205 0.0783

LEU 205 PHE 206 0.0000

PHE 206 LYS 207 0.0540

LYS 207 GLU 208 -0.0000

GLU 208 GLY 209 0.2003

GLY 209 ASP 210 -0.0001

ASP 210 ARG 211 0.1731

ARG 211 PHE 212 0.0001

PHE 212 LEU 213 -0.0627

LEU 213 GLN 214 -0.0001

GLN 214 ALA 215 0.1727

ALA 215 ALA 216 -0.0002

ALA 216 ASN 217 -0.0734

ASN 217 ALA 218 0.0002

ALA 218 CYS 219 0.0890

CYS 219 ARG 220 0.0000

ARG 220 TYR 221 0.0423

TYR 221 TRP 222 0.0001

TRP 222 PRO 223 0.0871

PRO 223 THR 224 -0.0000

THR 224 GLY 225 -0.0043

GLY 225 ARG 226 0.0001

ARG 226 GLY 227 0.0934

GLY 227 ILE 228 0.0001

ILE 228 TYR 229 0.0292

TYR 229 HIS 230 0.0000

HIS 230 ASN 231 0.0181

ASN 231 ASP 232 -0.0002

ASP 232 ALA 233 0.0162

ALA 233 LYS 234 0.0004

LYS 234 THR 235 -0.0049

THR 235 PHE 236 -0.0001

PHE 236 LEU 237 0.0403

LEU 237 VAL 238 0.0001

VAL 238 TRP 239 0.0473

TRP 239 VAL 240 -0.0003

VAL 240 ASN 241 0.0630

ASN 241 GLU 242 -0.0002

GLU 242 GLU 243 -0.0093

GLU 243 ASP 244 -0.0000

ASP 244 HIS 245 -0.0179

HIS 245 LEU 246 0.0000

LEU 246 ARG 247 0.0037

ARG 247 ILE 248 -0.0001

ILE 248 ILE 249 0.0320

ILE 249 SER 250 -0.0002

SER 250 MET 251 0.0228

MET 251 GLN 252 -0.0002

GLN 252 GLN 253 0.0555

GLN 253 GLY 254 -0.0001

GLY 254 GLY 255 0.0157

GLY 255 ASP 256 -0.0002

ASP 256 LEU 257 -0.0375

LEU 257 LYS 258 -0.0002

LYS 258 GLN 259 0.0257

GLN 259 VAL 260 -0.0000

VAL 260 TYR 261 -0.0359

TYR 261 SER 262 0.0000

SER 262 ARG 263 0.0118

ARG 263 MET 264 -0.0003

MET 264 VAL 265 -0.0115

VAL 265 SER 266 0.0003

SER 266 GLY 267 0.0131

GLY 267 VAL 268 0.0001

VAL 268 LYS 269 -0.0046

LYS 269 GLU 270 -0.0004

GLU 270 ILE 271 0.0078

ILE 271 GLU 272 -0.0001

GLU 272 LYS 273 -0.0182

LYS 273 LYS 274 -0.0001

LYS 274 LEU 275 -0.0121

LEU 275 PRO 276 -0.0002

PRO 276 PHE 277 -0.0050

PHE 277 SER 278 0.0001

SER 278 ARG 279 0.0403

ARG 279 ASP 280 0.0000

ASP 280 ASP 281 0.0011

ASP 281 ARG 282 -0.0003

ARG 282 LEU 283 0.0168

LEU 283 GLY 284 0.0004

GLY 284 PHE 285 -0.0033

PHE 285 LEU 286 0.0002

LEU 286 THR 287 0.0250

THR 287 PHE 288 -0.0000

PHE 288 CYS 289 -0.0172

CYS 289 PRO 290 0.0003

PRO 290 THR 291 -0.0731

THR 291 ASN 292 -0.0003

ASN 292 LEU 293 0.0251

LEU 293 GLY 294 -0.0001

GLY 294 THR 295 -0.0934

THR 295 THR 296 0.0001

THR 296 ILE 297 -0.0259

ILE 297 ARG 298 0.0003

ARG 298 ALA 299 -0.0076

ALA 299 SER 300 -0.0001

SER 300 VAL 301 -0.0206

VAL 301 HIS 302 0.0001

HIS 302 ILE 303 0.0303

ILE 303 LYS 304 0.0002

LYS 304 LEU 305 0.0200

LEU 305 PRO 306 0.0001

PRO 306 LYS 307 0.0158

LYS 307 LEU 308 0.0001

LEU 308 ALA 309 0.0015

ALA 309 ALA 310 0.0001

ALA 310 ASP 311 -0.0003

ASP 311 LYS 312 -0.0002

LYS 312 ALA 313 -0.0328

ALA 313 LYS 314 0.0002

LYS 314 LEU 315 0.0079

LEU 315 ASP 316 0.0000

ASP 316 SER 317 -0.0283

SER 317 ILE 318 0.0001

ILE 318 ALA 319 -0.0284

ALA 319 ALA 320 0.0002

ALA 320 LYS 321 -0.0469

LYS 321 TYR 322 0.0002

TYR 322 ASN 323 -0.2052

ASN 323 LEU 324 0.0001

LEU 324 GLN 325 0.0321

GLN 325 VAL 326 -0.0001

VAL 326 ARG 327 -0.0433

ARG 327 GLY 328 0.0001

GLY 328 THR 329 -0.0440

THR 329 ARG 330 0.0000

ARG 330 GLY 331 0.0140

GLY 331 GLU 332 0.0002

GLU 332 HIS 333 0.0838

HIS 333 THR 334 -0.0000

THR 334 GLU 335 0.0567

GLU 335 SER 336 -0.0002

SER 336 GLU 337 -0.0104

GLU 337 GLY 338 0.0001

GLY 338 GLY 339 0.0326

GLY 339 VAL 340 -0.0001

VAL 340 TYR 341 -0.0111

TYR 341 ASP 342 -0.0001

ASP 342 ILE 343 -0.0110

ILE 343 SER 344 0.0000

SER 344 ASN 345 -0.0643

ASN 345 LYS 346 0.0002

LYS 346 ARG 347 0.0023

ARG 347 ARG 348 -0.0001

ARG 348 MET 349 -0.0474

MET 349 GLY 350 -0.0002

GLY 350 LEU 351 -0.1897

LEU 351 THR 352 0.0002

THR 352 GLU 353 -0.0276

GLU 353 TYR 354 -0.0000

TYR 354 GLN 355 -0.0141

GLN 355 ALA 356 -0.0001

ALA 356 VAL 357 -0.0846

VAL 357 ARG 358 -0.0001

ARG 358 GLU 359 0.0380

GLU 359 MET 360 0.0004

MET 360 GLN 361 -0.0745

GLN 361 ASP 362 -0.0001

ASP 362 GLY 363 0.0764

GLY 363 ILE 364 -0.0003

ILE 364 GLN 365 -0.0201

GLN 365 GLU 366 0.0004

GLU 366 LEU 367 0.0104

LEU 367 ILE 368 0.0002

ILE 368 LYS 369 0.0404

LYS 369 LEU 370 0.0001

LEU 370 GLU 371 -0.0028

GLU 371 GLN 372 -0.0004

GLN 372 ALA 373 0.0429

ALA 373 ALA 374 -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 2404232236172138714

--- normal mode 9 ---

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

* *