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 14 ---

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 0.3200

THR 3 ILE 4 0.0000

ILE 4 ILE 5 0.1946

ILE 5 ARG 6 -0.0001

ARG 6 ALA 7 0.3150

ALA 7 ARG 8 0.0000

ARG 8 ALA 9 0.2771

ALA 9 PRO 10 0.0003

PRO 10 LEU 11 0.3058

LEU 11 ARG 12 -0.0002

ARG 12 LEU 13 0.2072

LEU 13 GLY 14 -0.0002

GLY 14 LEU 15 0.0376

LEU 15 ALA 16 0.0002

ALA 16 GLY 17 0.0722

GLY 17 GLY 18 0.0002

GLY 18 GLY 19 -0.0865

GLY 19 THR 20 -0.0003

THR 20 ASP 21 0.1302

ASP 21 VAL 22 -0.0003

VAL 22 ALA 23 -0.0958

ALA 23 PRO 24 -0.0003

PRO 24 TYR 25 0.0878

TYR 25 ALA 26 -0.0002

ALA 26 ASP 27 0.0378

ASP 27 THR 28 -0.0001

THR 28 PHE 29 0.0180

PHE 29 GLY 30 0.0000

GLY 30 GLY 31 -0.0444

GLY 31 TYR 32 -0.0001

TYR 32 VAL 33 -0.0329

VAL 33 LEU 34 0.0004

LEU 34 ASN 35 0.0263

ASN 35 ALA 36 0.0002

ALA 36 THR 37 0.0677

THR 37 ILE 38 0.0001

ILE 38 ASP 39 -0.0095

ASP 39 ARG 40 -0.0002

ARG 40 TYR 41 0.1160

TYR 41 ALA 42 -0.0002

ALA 42 TYR 43 0.1702

TYR 43 ALA 44 -0.0002

ALA 44 VAL 45 0.1359

VAL 45 ILE 46 0.0002

ILE 46 LYS 47 0.1106

LYS 47 THR 48 -0.0003

THR 48 LEU 49 0.1825

LEU 49 THR 50 -0.0001

THR 50 ILE 51 -0.0411

ILE 51 PRO 52 0.0000

PRO 52 ALA 53 -0.0207

ALA 53 VAL 54 -0.0004

VAL 54 ARG 55 -0.0209

ARG 55 PHE 56 -0.0001

PHE 56 VAL 57 0.0176

VAL 57 SER 58 -0.0001

SER 58 THR 59 0.0262

THR 59 ASP 60 0.0001

ASP 60 GLN 61 -0.1615

GLN 61 GLN 62 -0.0001

GLN 62 VAL 63 0.0361

VAL 63 GLU 64 0.0001

GLU 64 LYS 65 -0.0311

LYS 65 HIS 66 -0.0002

HIS 66 GLN 67 0.0030

GLN 67 LEU 68 0.0003

LEU 68 ILE 69 0.0605

ILE 69 SER 70 -0.0003

SER 70 GLU 71 0.0092

GLU 71 PRO 72 0.0002

PRO 72 LEU 73 0.0130

LEU 73 GLU 74 -0.0002

GLU 74 LEU 75 -0.0400

LEU 75 ASN 76 -0.0004

ASN 76 GLY 77 0.0200

GLY 77 THR 78 0.0000

THR 78 LEU 79 -0.0792

LEU 79 ASN 80 -0.0003

ASN 80 LEU 81 -0.1327

LEU 81 HIS 82 0.0001

HIS 82 LYS 83 -0.0059

LYS 83 ALA 84 0.0001

ALA 84 VAL 85 -0.0210

VAL 85 TYR 86 -0.0003

TYR 86 ASN 87 0.0051

ASN 87 HIS 88 -0.0002

HIS 88 MET 89 -0.0148

MET 89 ILE 90 0.0002

ILE 90 ARG 91 -0.0276

ARG 91 ASN 92 -0.0001

ASN 92 TYR 93 -0.0530

TYR 93 ASN 94 -0.0000

ASN 94 HIS 95 0.0009

HIS 95 GLY 96 -0.0000

GLY 96 LYS 97 -0.0083

LYS 97 PRO 98 -0.0002

PRO 98 ILE 99 -0.0513

ILE 99 ALA 100 0.0002

ALA 100 LEU 101 0.0529

LEU 101 GLU 102 0.0002

GLU 102 LEU 103 0.0750

LEU 103 SER 104 0.0001

SER 104 THR 105 0.1090

THR 105 PHE 106 -0.0004

PHE 106 CYS 107 0.1139

CYS 107 ASP 108 -0.0000

ASP 108 ALA 109 0.3235

ALA 109 PRO 110 -0.0000

PRO 110 ALA 111 -0.0374

ALA 111 GLY 112 0.0002

GLY 112 SER 113 -0.0506

SER 113 GLY 114 0.0002

GLY 114 LEU 115 0.1093

LEU 115 GLY 116 0.0003

GLY 116 SER 117 -0.0260

SER 117 SER 118 -0.0000

SER 118 SER 119 0.0441

SER 119 THR 120 -0.0001

THR 120 LEU 121 -0.0181

LEU 121 VAL 122 0.0002

VAL 122 VAL 123 -0.0531

VAL 123 VAL 124 0.0001

VAL 124 MET 125 0.0428

MET 125 ILE 126 -0.0001

ILE 126 LYS 127 -0.0698

LYS 127 ALA 128 0.0001

ALA 128 PHE 129 0.0172

PHE 129 VAL 130 0.0005

VAL 130 GLU 131 -0.0197

GLU 131 LEU 132 0.0001

LEU 132 LEU 133 -0.0234

LEU 133 ASN 134 -0.0001

ASN 134 LEU 135 0.0287

LEU 135 PRO 136 -0.0001

PRO 136 LEU 137 0.1278

LEU 137 ASP 138 -0.0005

ASP 138 ASP 139 0.1675

ASP 139 TYR 140 -0.0002

TYR 140 ALA 141 0.1978

ALA 141 ILE 142 -0.0000

ILE 142 ALA 143 0.1077

ALA 143 GLN 144 0.0001

GLN 144 LEU 145 0.1786

LEU 145 ALA 146 -0.0004

ALA 146 TYR 147 0.0384

TYR 147 ARG 148 -0.0003

ARG 148 ILE 149 -0.0004

ILE 149 GLU 150 -0.0004

GLU 150 ARG 151 0.0221

ARG 151 VAL 152 -0.0002

VAL 152 ASP 153 0.0274

ASP 153 CYS 154 -0.0001

CYS 154 GLY 155 0.0704

GLY 155 LEU 156 -0.0003

LEU 156 ALA 157 0.0215

ALA 157 GLY 158 -0.0002

GLY 158 GLY 159 0.0903

GLY 159 ARG 160 -0.0001

ARG 160 GLN 161 -0.0297

GLN 161 ASP 162 0.0002

ASP 162 GLN 163 0.1861

GLN 163 TYR 164 0.0002

TYR 164 SER 165 -0.0601

SER 165 ALA 166 -0.0000

ALA 166 THR 167 0.0886

THR 167 PHE 168 -0.0001

PHE 168 GLY 169 -0.0342

GLY 169 GLY 170 0.0001

GLY 170 PHE 171 0.0824

PHE 171 ASN 172 0.0001

ASN 172 PHE 173 -0.0070

PHE 173 MET 174 0.0002

MET 174 GLU 175 -0.1035

GLU 175 PHE 176 -0.0002

PHE 176 TYR 177 -0.0201

TYR 177 GLU 178 -0.0002

GLU 178 GLU 179 -0.0326

GLU 179 GLU 180 0.0002

GLU 180 ARG 181 -0.0104

ARG 181 THR 182 0.0002

THR 182 ILE 183 -0.0746

ILE 183 VAL 184 0.0004

VAL 184 ASN 185 0.0284

ASN 185 PRO 186 -0.0002

PRO 186 LEU 187 0.0858

LEU 187 ARG 188 0.0001

ARG 188 ILE 189 -0.0840

ILE 189 LYS 190 -0.0002

LYS 190 ASN 191 -0.0201

ASN 191 TRP 192 0.0000

TRP 192 VAL 193 0.0057

VAL 193 LEU 194 0.0002

LEU 194 CYS 195 -0.1100

CYS 195 GLU 196 0.0002

GLU 196 LEU 197 0.0662

LEU 197 GLU 198 0.0001

GLU 198 ALA 199 -0.2540

ALA 199 SER 200 -0.0000

SER 200 LEU 201 -0.0188

LEU 201 VAL 202 -0.0000

VAL 202 LEU 203 -0.0880

LEU 203 PHE 204 -0.0001

PHE 204 TYR 205 -0.1136

TYR 205 THR 206 -0.0001

THR 206 GLY 207 -0.0525

GLY 207 VAL 208 0.0000

VAL 208 SER 209 0.0213

SER 209 ARG 210 0.0001

ARG 210 GLU 211 -0.2648

GLU 211 SER 212 -0.0001

SER 212 ALA 213 -0.0655

ALA 213 LYS 214 -0.0001

LYS 214 ILE 215 0.0527

ILE 215 ILE 216 0.0003

ILE 216 GLN 217 0.0268

GLN 217 ASP 218 -0.0001

ASP 218 GLN 219 -0.0416

GLN 219 SER 220 0.0000

SER 220 ASP 221 0.0663

ASP 221 ASN 222 -0.0001

ASN 222 VAL 223 -0.0317

VAL 223 VAL 224 0.0001

VAL 224 SER 225 -0.0005

SER 225 HIS 226 0.0002

HIS 226 LYS 227 0.0926

LYS 227 THR 228 0.0000

THR 228 ALA 229 0.2205

ALA 229 ALA 230 -0.0001

ALA 230 ILE 231 -0.0675

ILE 231 GLU 232 -0.0002

GLU 232 ALA 233 0.0924

ALA 233 MET 234 -0.0001

MET 234 HIS 235 -0.0809

HIS 235 GLY 236 -0.0000

GLY 236 ILE 237 0.0440

ILE 237 LYS 238 -0.0003

LYS 238 ARG 239 -0.0226

ARG 239 GLU 240 0.0001

GLU 240 ALA 241 0.0625

ALA 241 LEU 242 -0.0002

LEU 242 VAL 243 0.1530

VAL 243 MET 244 -0.0000

MET 244 LYS 245 -0.0943

LYS 245 GLU 246 -0.0001

GLU 246 ALA 247 0.0682

ALA 247 LEU 248 0.0002

LEU 248 LEU 249 -0.0274

LEU 249 LYS 250 -0.0000

LYS 250 GLY 251 -0.0016

GLY 251 ASP 252 0.0001

ASP 252 PHE 253 -0.0820

PHE 253 LYS 254 -0.0002

LYS 254 ALA 255 0.2512

ALA 255 PHE 256 -0.0002

PHE 256 VAL 257 -0.1391

VAL 257 ALA 258 0.0003

ALA 258 SER 259 0.1110

SER 259 MET 260 0.0003

MET 260 ARG 261 -0.0788

ARG 261 LEU 262 0.0002

LEU 262 GLY 263 0.1619

GLY 263 TRP 264 -0.0000

TRP 264 ASP 265 0.0253

ASP 265 ASN 266 -0.0004

ASN 266 LYS 267 -0.0436

LYS 267 LYS 268 -0.0000

LYS 268 ASN 269 0.2052

ASN 269 SER 270 0.0005

SER 270 ALA 271 -0.1737

ALA 271 ARG 272 -0.0001

ARG 272 THR 273 0.0695

THR 273 VAL 274 0.0001

VAL 274 SER 275 0.1365

SER 275 ASN 276 0.0000

ASN 276 ALA 277 0.2558

ALA 277 HIS 278 -0.0002

HIS 278 ILE 279 -0.1134

ILE 279 ASP 280 -0.0001

ASP 280 GLU 281 0.1093

GLU 281 ILE 282 0.0002

ILE 282 TYR 283 -0.1299

TYR 283 ASP 284 -0.0001

ASP 284 ALA 285 0.1139

ALA 285 ALA 286 0.0003

ALA 286 ILE 287 -0.0400

ILE 287 ARG 288 -0.0000

ARG 288 ALA 289 0.0806

ALA 289 GLY 290 0.0001

GLY 290 ALA 291 0.1564

ALA 291 GLN 292 -0.0002

GLN 292 ALA 293 0.2505

ALA 293 GLY 294 -0.0001

GLY 294 LYS 295 0.1307

LYS 295 VAL 296 0.0003

VAL 296 SER 297 0.3571

SER 297 GLY 298 0.0000

GLY 298 ALA 299 -0.0904

ALA 299 GLY 300 -0.0000

GLY 300 GLY 301 0.0071

GLY 301 GLY 302 0.0003

GLY 302 GLY 303 -0.0130

GLY 303 PHE 304 0.0000

PHE 304 MET 305 0.2028

MET 305 LEU 306 -0.0000

LEU 306 PHE 307 0.0546

PHE 307 PHE 308 0.0002

PHE 308 VAL 309 0.1726

VAL 309 PRO 310 0.0000

PRO 310 THR 311 0.1335

THR 311 GLU 312 -0.0002

GLU 312 LYS 313 0.0009

LYS 313 ARG 314 -0.0001

ARG 314 MET 315 0.0706

MET 315 ASP 316 0.0002

ASP 316 LEU 317 0.0490

LEU 317 ILE 318 -0.0000

ILE 318 ARG 319 -0.0412

ARG 319 THR 320 -0.0001

THR 320 LEU 321 0.0054

LEU 321 GLY 322 -0.0002

GLY 322 GLU 323 -0.0018

GLU 323 TYR 324 -0.0002

TYR 324 ASP 325 -0.1016

ASP 325 GLY 326 0.0003

GLY 326 GLN 327 0.2276

GLN 327 VAL 328 -0.0001

VAL 328 SER 329 0.1675

SER 329 ASN 330 0.0001

ASN 330 CYS 331 0.0573

CYS 331 HIS 332 0.0000

HIS 332 PHE 333 0.0052

PHE 333 THR 334 0.0001

THR 334 LYS 335 0.0501

LYS 335 ASN 336 0.0002

ASN 336 GLY 337 -0.0112

GLY 337 THR 338 0.0001

THR 338 GLN 339 0.2099

GLN 339 ALA 340 -0.0002

ALA 340 TRP 341 0.2668

TRP 341 ARG 342 -0.0001

ARG 342 ILE 343 0.0472

ILE 343 ALA 344 -0.0001

ALA 344 ASN 345 0.1722

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 14 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *