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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA strain for 24021912210317154

--- normal mode 12 ---

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
ASN 1 PRO 2 -0.0000

PRO 2 THR 3 0.1590

THR 3 ILE 4 0.0000

ILE 4 ILE 5 0.1520

ILE 5 ARG 6 0.0002

ARG 6 ALA 7 0.2535

ALA 7 ARG 8 0.0001

ARG 8 ALA 9 0.2501

ALA 9 PRO 10 0.0002

PRO 10 LEU 11 0.0229

LEU 11 ARG 12 0.0002

ARG 12 LEU 13 0.2618

LEU 13 GLY 14 -0.0001

GLY 14 LEU 15 0.1785

LEU 15 ALA 16 -0.0000

ALA 16 GLY 17 -0.0524

GLY 17 GLY 18 0.0001

GLY 18 GLY 19 -0.0504

GLY 19 THR 20 0.0004

THR 20 ASP 21 0.1448

ASP 21 VAL 22 0.0002

VAL 22 ALA 23 0.0352

ALA 23 PRO 24 0.0004

PRO 24 TYR 25 -0.0884

TYR 25 ALA 26 0.0000

ALA 26 ASP 27 0.0166

ASP 27 THR 28 0.0003

THR 28 PHE 29 -0.0220

PHE 29 GLY 30 0.0002

GLY 30 GLY 31 -0.0444

GLY 31 TYR 32 -0.0000

TYR 32 VAL 33 -0.0380

VAL 33 LEU 34 0.0001

LEU 34 ASN 35 0.0389

ASN 35 ALA 36 0.0000

ALA 36 THR 37 0.0930

THR 37 ILE 38 0.0001

ILE 38 ASP 39 -0.0489

ASP 39 ARG 40 -0.0002

ARG 40 TYR 41 0.4575

TYR 41 ALA 42 -0.0001

ALA 42 TYR 43 0.1615

TYR 43 ALA 44 -0.0001

ALA 44 VAL 45 0.1723

VAL 45 ILE 46 0.0000

ILE 46 LYS 47 0.1463

LYS 47 THR 48 -0.0001

THR 48 LEU 49 0.0752

LEU 49 THR 50 0.0001

THR 50 ILE 51 -0.0783

ILE 51 PRO 52 -0.0000

PRO 52 ALA 53 0.0621

ALA 53 VAL 54 0.0000

VAL 54 ARG 55 0.0418

ARG 55 PHE 56 0.0001

PHE 56 VAL 57 0.0393

VAL 57 SER 58 0.0001

SER 58 THR 59 -0.0792

THR 59 ASP 60 0.0003

ASP 60 GLN 61 -0.0074

GLN 61 GLN 62 0.0002

GLN 62 VAL 63 -0.1039

VAL 63 GLU 64 -0.0004

GLU 64 LYS 65 0.0883

LYS 65 HIS 66 0.0002

HIS 66 GLN 67 0.0419

GLN 67 LEU 68 -0.0002

LEU 68 ILE 69 0.0445

ILE 69 SER 70 0.0001

SER 70 GLU 71 -0.0236

GLU 71 PRO 72 0.0003

PRO 72 LEU 73 -0.0697

LEU 73 GLU 74 -0.0002

GLU 74 LEU 75 0.1334

LEU 75 ASN 76 0.0001

ASN 76 GLY 77 -0.0660

GLY 77 THR 78 0.0000

THR 78 LEU 79 0.0613

LEU 79 ASN 80 -0.0002

ASN 80 LEU 81 0.2073

LEU 81 HIS 82 -0.0003

HIS 82 LYS 83 0.0953

LYS 83 ALA 84 -0.0001

ALA 84 VAL 85 0.0302

VAL 85 TYR 86 -0.0002

TYR 86 ASN 87 0.0797

ASN 87 HIS 88 -0.0002

HIS 88 MET 89 0.0290

MET 89 ILE 90 0.0002

ILE 90 ARG 91 -0.0417

ARG 91 ASN 92 -0.0003

ASN 92 TYR 93 -0.0157

TYR 93 ASN 94 0.0002

ASN 94 HIS 95 -0.0234

HIS 95 GLY 96 -0.0003

GLY 96 LYS 97 0.0202

LYS 97 PRO 98 0.0000

PRO 98 ILE 99 -0.0893

ILE 99 ALA 100 -0.0005

ALA 100 LEU 101 0.0712

LEU 101 GLU 102 0.0002

GLU 102 LEU 103 0.1420

LEU 103 SER 104 -0.0001

SER 104 THR 105 0.1967

THR 105 PHE 106 0.0001

PHE 106 CYS 107 0.2371

CYS 107 ASP 108 -0.0002

ASP 108 ALA 109 -0.0334

ALA 109 PRO 110 0.0001

PRO 110 ALA 111 0.0543

ALA 111 GLY 112 0.0005

GLY 112 SER 113 0.0608

SER 113 GLY 114 0.0003

GLY 114 LEU 115 0.0105

LEU 115 GLY 116 -0.0003

GLY 116 SER 117 0.0018

SER 117 SER 118 0.0001

SER 118 SER 119 -0.0576

SER 119 THR 120 0.0003

THR 120 LEU 121 0.1973

LEU 121 VAL 122 0.0004

VAL 122 VAL 123 0.0780

VAL 123 VAL 124 -0.0003

VAL 124 MET 125 0.2017

MET 125 ILE 126 -0.0002

ILE 126 LYS 127 -0.0019

LYS 127 ALA 128 0.0002

ALA 128 PHE 129 0.0399

PHE 129 VAL 130 -0.0001

VAL 130 GLU 131 0.0272

GLU 131 LEU 132 0.0000

LEU 132 LEU 133 -0.0295

LEU 133 ASN 134 -0.0002

ASN 134 LEU 135 0.0446

LEU 135 PRO 136 -0.0001

PRO 136 LEU 137 0.0723

LEU 137 ASP 138 -0.0002

ASP 138 ASP 139 0.1017

ASP 139 TYR 140 0.0001

TYR 140 ALA 141 0.2251

ALA 141 ILE 142 -0.0000

ILE 142 ALA 143 0.0389

ALA 143 GLN 144 -0.0002

GLN 144 LEU 145 0.3283

LEU 145 ALA 146 0.0000

ALA 146 TYR 147 0.1034

TYR 147 ARG 148 -0.0000

ARG 148 ILE 149 0.2398

ILE 149 GLU 150 0.0001

GLU 150 ARG 151 0.0457

ARG 151 VAL 152 0.0003

VAL 152 ASP 153 0.0836

ASP 153 CYS 154 0.0002

CYS 154 GLY 155 0.1614

GLY 155 LEU 156 -0.0000

LEU 156 ALA 157 0.4318

ALA 157 GLY 158 0.0002

GLY 158 GLY 159 -0.1393

GLY 159 ARG 160 0.0003

ARG 160 GLN 161 0.0490

GLN 161 ASP 162 -0.0001

ASP 162 GLN 163 0.0691

GLN 163 TYR 164 -0.0002

TYR 164 SER 165 0.0466

SER 165 ALA 166 0.0000

ALA 166 THR 167 -0.0011

THR 167 PHE 168 -0.0002

PHE 168 GLY 169 0.0854

GLY 169 GLY 170 -0.0002

GLY 170 PHE 171 0.2138

PHE 171 ASN 172 0.0002

ASN 172 PHE 173 -0.0562

PHE 173 MET 174 -0.0002

MET 174 GLU 175 -0.0982

GLU 175 PHE 176 -0.0000

PHE 176 TYR 177 -0.0592

TYR 177 GLU 178 -0.0001

GLU 178 GLU 179 0.0898

GLU 179 GLU 180 0.0001

GLU 180 ARG 181 0.0847

ARG 181 THR 182 -0.0004

THR 182 ILE 183 0.0232

ILE 183 VAL 184 0.0001

VAL 184 ASN 185 0.1504

ASN 185 PRO 186 0.0004

PRO 186 LEU 187 0.3421

LEU 187 ARG 188 -0.0000

ARG 188 ILE 189 -0.0014

ILE 189 LYS 190 -0.0000

LYS 190 ASN 191 -0.1024

ASN 191 TRP 192 0.0003

TRP 192 VAL 193 -0.0158

VAL 193 LEU 194 0.0000

LEU 194 CYS 195 -0.0056

CYS 195 GLU 196 -0.0000

GLU 196 LEU 197 0.0305

LEU 197 GLU 198 0.0001

GLU 198 ALA 199 0.2210

ALA 199 SER 200 -0.0000

SER 200 LEU 201 0.0347

LEU 201 VAL 202 -0.0003

VAL 202 LEU 203 0.1016

LEU 203 PHE 204 -0.0000

PHE 204 TYR 205 0.0510

TYR 205 THR 206 -0.0001

THR 206 GLY 207 -0.0049

GLY 207 VAL 208 0.0003

VAL 208 SER 209 -0.0440

SER 209 ARG 210 -0.0003

ARG 210 GLU 211 0.1641

GLU 211 SER 212 -0.0002

SER 212 ALA 213 0.0609

ALA 213 LYS 214 -0.0004

LYS 214 ILE 215 -0.0302

ILE 215 ILE 216 0.0001

ILE 216 GLN 217 -0.0312

GLN 217 ASP 218 0.0001

ASP 218 GLN 219 -0.0487

GLN 219 SER 220 0.0002

SER 220 ASP 221 -0.0350

ASP 221 ASN 222 -0.0002

ASN 222 VAL 223 0.0264

VAL 223 VAL 224 -0.0002

VAL 224 SER 225 -0.0253

SER 225 HIS 226 0.0001

HIS 226 LYS 227 -0.0524

LYS 227 THR 228 -0.0001

THR 228 ALA 229 -0.1134

ALA 229 ALA 230 0.0002

ALA 230 ILE 231 0.0796

ILE 231 GLU 232 0.0002

GLU 232 ALA 233 -0.0194

ALA 233 MET 234 -0.0005

MET 234 HIS 235 0.0021

HIS 235 GLY 236 -0.0001

GLY 236 ILE 237 0.0553

ILE 237 LYS 238 0.0002

LYS 238 ARG 239 0.0433

ARG 239 GLU 240 0.0002

GLU 240 ALA 241 0.1088

ALA 241 LEU 242 0.0002

LEU 242 VAL 243 0.0921

VAL 243 MET 244 -0.0002

MET 244 LYS 245 0.0363

LYS 245 GLU 246 -0.0003

GLU 246 ALA 247 0.1433

ALA 247 LEU 248 -0.0001

LEU 248 LEU 249 0.0095

LEU 249 LYS 250 -0.0001

LYS 250 GLY 251 0.0040

GLY 251 ASP 252 0.0002

ASP 252 PHE 253 0.0508

PHE 253 LYS 254 0.0000

LYS 254 ALA 255 -0.0300

ALA 255 PHE 256 -0.0003

PHE 256 VAL 257 0.0941

VAL 257 ALA 258 0.0002

ALA 258 SER 259 0.0764

SER 259 MET 260 0.0002

MET 260 ARG 261 0.1353

ARG 261 LEU 262 0.0002

LEU 262 GLY 263 -0.0157

GLY 263 TRP 264 0.0000

TRP 264 ASP 265 0.0676

ASP 265 ASN 266 -0.0002

ASN 266 LYS 267 0.0274

LYS 267 LYS 268 -0.0003

LYS 268 ASN 269 -0.0240

ASN 269 SER 270 0.0002

SER 270 ALA 271 0.0361

ALA 271 ARG 272 -0.0001

ARG 272 THR 273 0.0636

THR 273 VAL 274 -0.0000

VAL 274 SER 275 -0.0381

SER 275 ASN 276 0.0004

ASN 276 ALA 277 -0.0744

ALA 277 HIS 278 0.0002

HIS 278 ILE 279 0.0272

ILE 279 ASP 280 0.0000

ASP 280 GLU 281 -0.0093

GLU 281 ILE 282 -0.0000

ILE 282 TYR 283 0.0212

TYR 283 ASP 284 0.0003

ASP 284 ALA 285 -0.0232

ALA 285 ALA 286 0.0000

ALA 286 ILE 287 0.0228

ILE 287 ARG 288 -0.0002

ARG 288 ALA 289 -0.0224

ALA 289 GLY 290 -0.0001

GLY 290 ALA 291 -0.0426

ALA 291 GLN 292 -0.0002

GLN 292 ALA 293 -0.0946

ALA 293 GLY 294 -0.0001

GLY 294 LYS 295 0.0165

LYS 295 VAL 296 -0.0004

VAL 296 SER 297 0.1095

SER 297 GLY 298 0.0001

GLY 298 ALA 299 0.0416

ALA 299 GLY 300 0.0002

GLY 300 GLY 301 -0.0445

GLY 301 GLY 302 -0.0003

GLY 302 GLY 303 0.0500

GLY 303 PHE 304 -0.0001

PHE 304 MET 305 0.0870

MET 305 LEU 306 0.0002

LEU 306 PHE 307 0.0858

PHE 307 PHE 308 0.0000

PHE 308 VAL 309 -0.0853

VAL 309 PRO 310 0.0000

PRO 310 THR 311 -0.0958

THR 311 GLU 312 0.0002

GLU 312 LYS 313 -0.0126

LYS 313 ARG 314 -0.0002

ARG 314 MET 315 -0.0436

MET 315 ASP 316 -0.0003

ASP 316 LEU 317 -0.0009

LEU 317 ILE 318 0.0004

ILE 318 ARG 319 0.0157

ARG 319 THR 320 -0.0002

THR 320 LEU 321 0.0321

LEU 321 GLY 322 -0.0001

GLY 322 GLU 323 -0.0046

GLU 323 TYR 324 0.0000

TYR 324 ASP 325 0.0187

ASP 325 GLY 326 0.0001

GLY 326 GLN 327 -0.1016

GLN 327 VAL 328 -0.0003

VAL 328 SER 329 -0.0580

SER 329 ASN 330 0.0002

ASN 330 CYS 331 -0.0952

CYS 331 HIS 332 0.0002

HIS 332 PHE 333 -0.0978

PHE 333 THR 334 -0.0002

THR 334 LYS 335 -0.0102

LYS 335 ASN 336 -0.0000

ASN 336 GLY 337 0.2639

GLY 337 THR 338 -0.0002

THR 338 GLN 339 0.1318

GLN 339 ALA 340 0.0000

ALA 340 TRP 341 0.1946

TRP 341 ARG 342 -0.0002

ARG 342 ILE 343 0.0608

ILE 343 ALA 344 0.0001

ALA 344 ASN 345 0.1094

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.

*** EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA strain for 24021912210317154

--- normal mode 12 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *