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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA strain for 24021912261023411

--- 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
ASN 1 PRO 2 0.0001

PRO 2 THR 3 0.2415

THR 3 ILE 4 0.0000

ILE 4 ILE 5 0.0608

ILE 5 ARG 6 -0.0002

ARG 6 ALA 7 -0.0279

ALA 7 ARG 8 0.0000

ARG 8 ALA 9 0.0199

ALA 9 PRO 10 0.0004

PRO 10 LEU 11 0.0497

LEU 11 ARG 12 0.0001

ARG 12 LEU 13 -0.0399

LEU 13 GLY 14 -0.0004

GLY 14 LEU 15 0.0323

LEU 15 ALA 16 0.0000

ALA 16 GLY 17 -0.0223

GLY 17 GLY 18 0.0000

GLY 18 GLY 19 -0.0164

GLY 19 THR 20 -0.0002

THR 20 ASP 21 -0.0027

ASP 21 VAL 22 0.0004

VAL 22 ALA 23 0.0353

ALA 23 PRO 24 0.0001

PRO 24 TYR 25 -0.0192

TYR 25 ALA 26 0.0001

ALA 26 ASP 27 -0.0118

ASP 27 THR 28 -0.0002

THR 28 PHE 29 0.0188

PHE 29 GLY 30 -0.0000

GLY 30 GLY 31 -0.0048

GLY 31 TYR 32 0.0000

TYR 32 VAL 33 0.0331

VAL 33 LEU 34 -0.0001

LEU 34 ASN 35 0.0579

ASN 35 ALA 36 -0.0001

ALA 36 THR 37 0.0446

THR 37 ILE 38 0.0000

ILE 38 ASP 39 0.0304

ASP 39 ARG 40 0.0000

ARG 40 TYR 41 -0.1328

TYR 41 ALA 42 0.0003

ALA 42 TYR 43 -0.0060

TYR 43 ALA 44 -0.0003

ALA 44 VAL 45 0.0274

VAL 45 ILE 46 0.0000

ILE 46 LYS 47 0.0462

LYS 47 THR 48 -0.0001

THR 48 LEU 49 -0.1426

LEU 49 THR 50 0.0000

THR 50 ILE 51 0.0725

ILE 51 PRO 52 0.0002

PRO 52 ALA 53 0.0935

ALA 53 VAL 54 -0.0001

VAL 54 ARG 55 0.0982

ARG 55 PHE 56 -0.0001

PHE 56 VAL 57 0.1569

VAL 57 SER 58 0.0002

SER 58 THR 59 0.0122

THR 59 ASP 60 -0.0004

ASP 60 GLN 61 -0.1524

GLN 61 GLN 62 0.0001

GLN 62 VAL 63 0.1042

VAL 63 GLU 64 0.0002

GLU 64 LYS 65 0.1602

LYS 65 HIS 66 -0.0001

HIS 66 GLN 67 0.1086

GLN 67 LEU 68 0.0002

LEU 68 ILE 69 -0.0659

ILE 69 SER 70 -0.0001

SER 70 GLU 71 -0.0286

GLU 71 PRO 72 0.0001

PRO 72 LEU 73 0.0922

LEU 73 GLU 74 0.0000

GLU 74 LEU 75 -0.1159

LEU 75 ASN 76 0.0001

ASN 76 GLY 77 0.0112

GLY 77 THR 78 -0.0002

THR 78 LEU 79 -0.0639

LEU 79 ASN 80 0.0002

ASN 80 LEU 81 -0.0860

LEU 81 HIS 82 -0.0002

HIS 82 LYS 83 -0.0847

LYS 83 ALA 84 -0.0002

ALA 84 VAL 85 0.0410

VAL 85 TYR 86 -0.0002

TYR 86 ASN 87 -0.1350

ASN 87 HIS 88 -0.0001

HIS 88 MET 89 0.0353

MET 89 ILE 90 -0.0002

ILE 90 ARG 91 0.0550

ARG 91 ASN 92 -0.0000

ASN 92 TYR 93 0.1022

TYR 93 ASN 94 0.0000

ASN 94 HIS 95 0.1083

HIS 95 GLY 96 0.0000

GLY 96 LYS 97 -0.0750

LYS 97 PRO 98 0.0000

PRO 98 ILE 99 0.2348

ILE 99 ALA 100 0.0002

ALA 100 LEU 101 -0.0013

LEU 101 GLU 102 0.0003

GLU 102 LEU 103 0.1575

LEU 103 SER 104 -0.0001

SER 104 THR 105 0.2326

THR 105 PHE 106 -0.0005

PHE 106 CYS 107 0.0925

CYS 107 ASP 108 -0.0002

ASP 108 ALA 109 0.0883

ALA 109 PRO 110 -0.0001

PRO 110 ALA 111 0.0187

ALA 111 GLY 112 -0.0003

GLY 112 SER 113 0.0541

SER 113 GLY 114 -0.0001

GLY 114 LEU 115 0.0728

LEU 115 GLY 116 0.0003

GLY 116 SER 117 0.0751

SER 117 SER 118 0.0001

SER 118 SER 119 -0.0528

SER 119 THR 120 -0.0005

THR 120 LEU 121 0.1019

LEU 121 VAL 122 -0.0001

VAL 122 VAL 123 0.0126

VAL 123 VAL 124 0.0001

VAL 124 MET 125 -0.0349

MET 125 ILE 126 0.0004

ILE 126 LYS 127 0.0173

LYS 127 ALA 128 -0.0002

ALA 128 PHE 129 0.0092

PHE 129 VAL 130 -0.0000

VAL 130 GLU 131 0.1716

GLU 131 LEU 132 0.0002

LEU 132 LEU 133 0.2023

LEU 133 ASN 134 -0.0004

ASN 134 LEU 135 0.1563

LEU 135 PRO 136 -0.0001

PRO 136 LEU 137 0.1358

LEU 137 ASP 138 0.0001

ASP 138 ASP 139 -0.1266

ASP 139 TYR 140 -0.0005

TYR 140 ALA 141 -0.2161

ALA 141 ILE 142 0.0003

ILE 142 ALA 143 0.0530

ALA 143 GLN 144 0.0003

GLN 144 LEU 145 -0.2984

LEU 145 ALA 146 0.0002

ALA 146 TYR 147 0.0149

TYR 147 ARG 148 0.0001

ARG 148 ILE 149 -0.0871

ILE 149 GLU 150 -0.0001

GLU 150 ARG 151 0.0025

ARG 151 VAL 152 -0.0000

VAL 152 ASP 153 -0.1218

ASP 153 CYS 154 -0.0002

CYS 154 GLY 155 -0.0247

GLY 155 LEU 156 0.0004

LEU 156 ALA 157 0.1247

ALA 157 GLY 158 0.0001

GLY 158 GLY 159 -0.0229

GLY 159 ARG 160 -0.0004

ARG 160 GLN 161 -0.0818

GLN 161 ASP 162 -0.0002

ASP 162 GLN 163 -0.1220

GLN 163 TYR 164 -0.0002

TYR 164 SER 165 -0.0895

SER 165 ALA 166 -0.0002

ALA 166 THR 167 -0.0679

THR 167 PHE 168 0.0001

PHE 168 GLY 169 -0.0897

GLY 169 GLY 170 0.0001

GLY 170 PHE 171 0.0109

PHE 171 ASN 172 0.0001

ASN 172 PHE 173 0.0349

PHE 173 MET 174 0.0004

MET 174 GLU 175 0.0281

GLU 175 PHE 176 0.0002

PHE 176 TYR 177 0.0071

TYR 177 GLU 178 -0.0001

GLU 178 GLU 179 -0.0120

GLU 179 GLU 180 -0.0002

GLU 180 ARG 181 -0.0109

ARG 181 THR 182 -0.0004

THR 182 ILE 183 0.0167

ILE 183 VAL 184 0.0000

VAL 184 ASN 185 -0.0071

ASN 185 PRO 186 0.0004

PRO 186 LEU 187 -0.0074

LEU 187 ARG 188 -0.0005

ARG 188 ILE 189 0.0074

ILE 189 LYS 190 0.0001

LYS 190 ASN 191 -0.0132

ASN 191 TRP 192 0.0001

TRP 192 VAL 193 -0.0160

VAL 193 LEU 194 0.0001

LEU 194 CYS 195 -0.0278

CYS 195 GLU 196 -0.0004

GLU 196 LEU 197 -0.0097

LEU 197 GLU 198 0.0003

GLU 198 ALA 199 -0.0819

ALA 199 SER 200 0.0002

SER 200 LEU 201 0.0076

LEU 201 VAL 202 0.0000

VAL 202 LEU 203 -0.0046

LEU 203 PHE 204 -0.0002

PHE 204 TYR 205 0.0428

TYR 205 THR 206 0.0005

THR 206 GLY 207 0.0427

GLY 207 VAL 208 0.0004

VAL 208 SER 209 -0.1041

SER 209 ARG 210 0.0002

ARG 210 GLU 211 0.0768

GLU 211 SER 212 0.0001

SER 212 ALA 213 0.0392

ALA 213 LYS 214 0.0002

LYS 214 ILE 215 -0.0433

ILE 215 ILE 216 0.0003

ILE 216 GLN 217 0.0061

GLN 217 ASP 218 -0.0002

ASP 218 GLN 219 -0.0112

GLN 219 SER 220 -0.0003

SER 220 ASP 221 0.0083

ASP 221 ASN 222 -0.0003

ASN 222 VAL 223 0.0059

VAL 223 VAL 224 -0.0003

VAL 224 SER 225 0.0087

SER 225 HIS 226 -0.0001

HIS 226 LYS 227 -0.0022

LYS 227 THR 228 0.0004

THR 228 ALA 229 0.0207

ALA 229 ALA 230 0.0000

ALA 230 ILE 231 0.0209

ILE 231 GLU 232 -0.0003

GLU 232 ALA 233 0.0343

ALA 233 MET 234 0.0001

MET 234 HIS 235 0.0001

HIS 235 GLY 236 0.0001

GLY 236 ILE 237 0.0186

ILE 237 LYS 238 0.0000

LYS 238 ARG 239 0.0328

ARG 239 GLU 240 -0.0002

GLU 240 ALA 241 0.0013

ALA 241 LEU 242 0.0005

LEU 242 VAL 243 0.0495

VAL 243 MET 244 0.0001

MET 244 LYS 245 0.0015

LYS 245 GLU 246 0.0004

GLU 246 ALA 247 0.0507

ALA 247 LEU 248 0.0000

LEU 248 LEU 249 0.0149

LEU 249 LYS 250 0.0001

LYS 250 GLY 251 0.0197

GLY 251 ASP 252 0.0002

ASP 252 PHE 253 0.0477

PHE 253 LYS 254 0.0001

LYS 254 ALA 255 -0.0033

ALA 255 PHE 256 0.0002

PHE 256 VAL 257 0.0266

VAL 257 ALA 258 0.0001

ALA 258 SER 259 0.0309

SER 259 MET 260 -0.0002

MET 260 ARG 261 -0.0007

ARG 261 LEU 262 0.0001

LEU 262 GLY 263 -0.0007

GLY 263 TRP 264 -0.0003

TRP 264 ASP 265 0.0239

ASP 265 ASN 266 -0.0002

ASN 266 LYS 267 0.0220

LYS 267 LYS 268 0.0001

LYS 268 ASN 269 0.0537

ASN 269 SER 270 -0.0001

SER 270 ALA 271 -0.0071

ALA 271 ARG 272 -0.0002

ARG 272 THR 273 0.1082

THR 273 VAL 274 -0.0000

VAL 274 SER 275 -0.0567

SER 275 ASN 276 -0.0001

ASN 276 ALA 277 -0.0503

ALA 277 HIS 278 0.0001

HIS 278 ILE 279 0.0099

ILE 279 ASP 280 0.0003

ASP 280 GLU 281 -0.0050

GLU 281 ILE 282 -0.0001

ILE 282 TYR 283 0.0303

TYR 283 ASP 284 -0.0003

ASP 284 ALA 285 0.0079

ALA 285 ALA 286 0.0003

ALA 286 ILE 287 0.0079

ILE 287 ARG 288 0.0001

ARG 288 ALA 289 -0.0185

ALA 289 GLY 290 -0.0003

GLY 290 ALA 291 -0.0023

ALA 291 GLN 292 0.0002

GLN 292 ALA 293 -0.0172

ALA 293 GLY 294 0.0005

GLY 294 LYS 295 -0.0275

LYS 295 VAL 296 0.0004

VAL 296 SER 297 -0.0189

SER 297 GLY 298 0.0005

GLY 298 ALA 299 0.0761

ALA 299 GLY 300 -0.0004

GLY 300 GLY 301 -0.0445

GLY 301 GLY 302 -0.0001

GLY 302 GLY 303 0.0731

GLY 303 PHE 304 -0.0000

PHE 304 MET 305 0.0018

MET 305 LEU 306 -0.0002

LEU 306 PHE 307 -0.0318

PHE 307 PHE 308 0.0002

PHE 308 VAL 309 0.0073

VAL 309 PRO 310 0.0001

PRO 310 THR 311 -0.0164

THR 311 GLU 312 0.0000

GLU 312 LYS 313 0.0023

LYS 313 ARG 314 0.0002

ARG 314 MET 315 -0.0031

MET 315 ASP 316 -0.0002

ASP 316 LEU 317 -0.0129

LEU 317 ILE 318 0.0001

ILE 318 ARG 319 -0.0352

ARG 319 THR 320 0.0003

THR 320 LEU 321 -0.0443

LEU 321 GLY 322 -0.0000

GLY 322 GLU 323 -0.0027

GLU 323 TYR 324 -0.0004

TYR 324 ASP 325 -0.0036

ASP 325 GLY 326 0.0002

GLY 326 GLN 327 0.0163

GLN 327 VAL 328 0.0002

VAL 328 SER 329 -0.0263

SER 329 ASN 330 0.0001

ASN 330 CYS 331 -0.0314

CYS 331 HIS 332 -0.0001

HIS 332 PHE 333 -0.0434

PHE 333 THR 334 -0.0000

THR 334 LYS 335 0.0073

LYS 335 ASN 336 -0.0000

ASN 336 GLY 337 -0.0643

GLY 337 THR 338 0.0000

THR 338 GLN 339 0.1885

GLN 339 ALA 340 -0.0004

ALA 340 TRP 341 0.2902

TRP 341 ARG 342 0.0003

ARG 342 ILE 343 0.3181

ILE 343 ALA 344 0.0003

ALA 344 ASN 345 0.2107

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 24021912261023411

--- normal mode 10 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *