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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA strain for 24021912300225903

--- normal mode 15 ---

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 -0.0002

PRO 2 THR 3 -0.1424

THR 3 ILE 4 -0.0003

ILE 4 ILE 5 0.0919

ILE 5 ARG 6 -0.0002

ARG 6 ALA 7 0.1501

ALA 7 ARG 8 0.0001

ARG 8 ALA 9 0.0558

ALA 9 PRO 10 0.0000

PRO 10 LEU 11 -0.0100

LEU 11 ARG 12 -0.0001

ARG 12 LEU 13 0.0036

LEU 13 GLY 14 -0.0003

GLY 14 LEU 15 0.1090

LEU 15 ALA 16 -0.0002

ALA 16 GLY 17 -0.0210

GLY 17 GLY 18 0.0004

GLY 18 GLY 19 0.0497

GLY 19 THR 20 -0.0000

THR 20 ASP 21 0.1058

ASP 21 VAL 22 -0.0003

VAL 22 ALA 23 -0.0104

ALA 23 PRO 24 0.0002

PRO 24 TYR 25 -0.0563

TYR 25 ALA 26 0.0000

ALA 26 ASP 27 0.0417

ASP 27 THR 28 0.0000

THR 28 PHE 29 -0.0804

PHE 29 GLY 30 0.0001

GLY 30 GLY 31 -0.0035

GLY 31 TYR 32 0.0001

TYR 32 VAL 33 -0.0257

VAL 33 LEU 34 -0.0001

LEU 34 ASN 35 0.0576

ASN 35 ALA 36 0.0001

ALA 36 THR 37 0.0131

THR 37 ILE 38 0.0001

ILE 38 ASP 39 0.0006

ASP 39 ARG 40 0.0001

ARG 40 TYR 41 -0.0449

TYR 41 ALA 42 0.0001

ALA 42 TYR 43 0.0634

TYR 43 ALA 44 0.0001

ALA 44 VAL 45 0.2302

VAL 45 ILE 46 0.0003

ILE 46 LYS 47 0.1755

LYS 47 THR 48 0.0001

THR 48 LEU 49 0.0520

LEU 49 THR 50 -0.0001

THR 50 ILE 51 0.0805

ILE 51 PRO 52 0.0006

PRO 52 ALA 53 0.0114

ALA 53 VAL 54 0.0002

VAL 54 ARG 55 -0.1050

ARG 55 PHE 56 0.0004

PHE 56 VAL 57 -0.0265

VAL 57 SER 58 -0.0001

SER 58 THR 59 0.1053

THR 59 ASP 60 -0.0001

ASP 60 GLN 61 -0.2196

GLN 61 GLN 62 -0.0002

GLN 62 VAL 63 0.1516

VAL 63 GLU 64 -0.0002

GLU 64 LYS 65 -0.0295

LYS 65 HIS 66 -0.0001

HIS 66 GLN 67 -0.0346

GLN 67 LEU 68 0.0002

LEU 68 ILE 69 -0.0211

ILE 69 SER 70 0.0000

SER 70 GLU 71 -0.0279

GLU 71 PRO 72 -0.0001

PRO 72 LEU 73 0.0571

LEU 73 GLU 74 -0.0002

GLU 74 LEU 75 -0.0052

LEU 75 ASN 76 0.0002

ASN 76 GLY 77 0.0126

GLY 77 THR 78 0.0005

THR 78 LEU 79 -0.1267

LEU 79 ASN 80 -0.0003

ASN 80 LEU 81 -0.1690

LEU 81 HIS 82 -0.0001

HIS 82 LYS 83 -0.1495

LYS 83 ALA 84 -0.0004

ALA 84 VAL 85 0.0032

VAL 85 TYR 86 0.0004

TYR 86 ASN 87 -0.1047

ASN 87 HIS 88 -0.0001

HIS 88 MET 89 -0.0294

MET 89 ILE 90 -0.0001

ILE 90 ARG 91 -0.0747

ARG 91 ASN 92 -0.0002

ASN 92 TYR 93 0.0199

TYR 93 ASN 94 -0.0003

ASN 94 HIS 95 -0.0003

HIS 95 GLY 96 -0.0003

GLY 96 LYS 97 -0.0494

LYS 97 PRO 98 -0.0001

PRO 98 ILE 99 -0.0457

ILE 99 ALA 100 -0.0001

ALA 100 LEU 101 -0.0357

LEU 101 GLU 102 0.0000

GLU 102 LEU 103 0.1764

LEU 103 SER 104 0.0002

SER 104 THR 105 0.1677

THR 105 PHE 106 0.0001

PHE 106 CYS 107 0.0205

CYS 107 ASP 108 -0.0000

ASP 108 ALA 109 -0.0970

ALA 109 PRO 110 0.0003

PRO 110 ALA 111 -0.0258

ALA 111 GLY 112 0.0001

GLY 112 SER 113 0.0549

SER 113 GLY 114 -0.0002

GLY 114 LEU 115 -0.1065

LEU 115 GLY 116 -0.0000

GLY 116 SER 117 0.1104

SER 117 SER 118 0.0001

SER 118 SER 119 0.1624

SER 119 THR 120 -0.0001

THR 120 LEU 121 0.0935

LEU 121 VAL 122 0.0000

VAL 122 VAL 123 -0.0419

VAL 123 VAL 124 -0.0000

VAL 124 MET 125 -0.0678

MET 125 ILE 126 0.0001

ILE 126 LYS 127 -0.0357

LYS 127 ALA 128 -0.0001

ALA 128 PHE 129 -0.0620

PHE 129 VAL 130 0.0001

VAL 130 GLU 131 0.0902

GLU 131 LEU 132 -0.0000

LEU 132 LEU 133 -0.0545

LEU 133 ASN 134 0.0001

ASN 134 LEU 135 0.0160

LEU 135 PRO 136 -0.0001

PRO 136 LEU 137 0.0537

LEU 137 ASP 138 0.0001

ASP 138 ASP 139 0.0018

ASP 139 TYR 140 0.0003

TYR 140 ALA 141 0.1534

ALA 141 ILE 142 -0.0003

ILE 142 ALA 143 0.0240

ALA 143 GLN 144 0.0001

GLN 144 LEU 145 0.3821

LEU 145 ALA 146 0.0000

ALA 146 TYR 147 0.1699

TYR 147 ARG 148 0.0000

ARG 148 ILE 149 0.4985

ILE 149 GLU 150 0.0004

GLU 150 ARG 151 0.0470

ARG 151 VAL 152 -0.0002

VAL 152 ASP 153 0.2049

ASP 153 CYS 154 -0.0001

CYS 154 GLY 155 0.1657

GLY 155 LEU 156 0.0001

LEU 156 ALA 157 -0.0369

ALA 157 GLY 158 0.0002

GLY 158 GLY 159 -0.2310

GLY 159 ARG 160 -0.0001

ARG 160 GLN 161 0.0042

GLN 161 ASP 162 0.0001

ASP 162 GLN 163 0.0854

GLN 163 TYR 164 0.0001

TYR 164 SER 165 -0.0610

SER 165 ALA 166 0.0002

ALA 166 THR 167 0.0300

THR 167 PHE 168 0.0001

PHE 168 GLY 169 -0.1288

GLY 169 GLY 170 0.0002

GLY 170 PHE 171 -0.0323

PHE 171 ASN 172 -0.0001

ASN 172 PHE 173 -0.0126

PHE 173 MET 174 0.0001

MET 174 GLU 175 -0.1555

GLU 175 PHE 176 0.0002

PHE 176 TYR 177 -0.0873

TYR 177 GLU 178 0.0001

GLU 178 GLU 179 0.2563

GLU 179 GLU 180 -0.0000

GLU 180 ARG 181 0.0956

ARG 181 THR 182 -0.0001

THR 182 ILE 183 -0.2169

ILE 183 VAL 184 0.0000

VAL 184 ASN 185 -0.1468

ASN 185 PRO 186 0.0004

PRO 186 LEU 187 -0.3043

LEU 187 ARG 188 -0.0002

ARG 188 ILE 189 -0.1730

ILE 189 LYS 190 0.0000

LYS 190 ASN 191 0.0285

ASN 191 TRP 192 -0.0000

TRP 192 VAL 193 0.0146

VAL 193 LEU 194 -0.0003

LEU 194 CYS 195 -0.0709

CYS 195 GLU 196 0.0000

GLU 196 LEU 197 -0.0359

LEU 197 GLU 198 -0.0002

GLU 198 ALA 199 -0.0791

ALA 199 SER 200 -0.0000

SER 200 LEU 201 -0.0109

LEU 201 VAL 202 -0.0000

VAL 202 LEU 203 0.0690

LEU 203 PHE 204 -0.0001

PHE 204 TYR 205 0.0681

TYR 205 THR 206 0.0003

THR 206 GLY 207 -0.1492

GLY 207 VAL 208 0.0002

VAL 208 SER 209 0.3713

SER 209 ARG 210 -0.0001

ARG 210 GLU 211 0.0954

GLU 211 SER 212 0.0001

SER 212 ALA 213 -0.0398

ALA 213 LYS 214 -0.0001

LYS 214 ILE 215 0.0491

ILE 215 ILE 216 0.0002

ILE 216 GLN 217 -0.0824

GLN 217 ASP 218 -0.0000

ASP 218 GLN 219 -0.0340

GLN 219 SER 220 0.0001

SER 220 ASP 221 -0.1931

ASP 221 ASN 222 0.0000

ASN 222 VAL 223 -0.0002

VAL 223 VAL 224 -0.0001

VAL 224 SER 225 -0.1364

SER 225 HIS 226 -0.0001

HIS 226 LYS 227 -0.0554

LYS 227 THR 228 0.0002

THR 228 ALA 229 -0.2143

ALA 229 ALA 230 -0.0003

ALA 230 ILE 231 0.0674

ILE 231 GLU 232 -0.0001

GLU 232 ALA 233 -0.1935

ALA 233 MET 234 -0.0002

MET 234 HIS 235 0.0256

HIS 235 GLY 236 -0.0000

GLY 236 ILE 237 -0.0245

ILE 237 LYS 238 0.0002

LYS 238 ARG 239 -0.0847

ARG 239 GLU 240 -0.0003

GLU 240 ALA 241 0.0452

ALA 241 LEU 242 -0.0002

LEU 242 VAL 243 -0.2482

VAL 243 MET 244 -0.0002

MET 244 LYS 245 -0.0097

LYS 245 GLU 246 0.0001

GLU 246 ALA 247 -0.2389

ALA 247 LEU 248 0.0002

LEU 248 LEU 249 -0.0119

LEU 249 LYS 250 0.0002

LYS 250 GLY 251 -0.0518

GLY 251 ASP 252 -0.0003

ASP 252 PHE 253 -0.1373

PHE 253 LYS 254 -0.0000

LYS 254 ALA 255 -0.1004

ALA 255 PHE 256 -0.0003

PHE 256 VAL 257 -0.1479

VAL 257 ALA 258 0.0003

ALA 258 SER 259 -0.2087

SER 259 MET 260 0.0001

MET 260 ARG 261 0.0235

ARG 261 LEU 262 0.0000

LEU 262 GLY 263 -0.0424

GLY 263 TRP 264 -0.0002

TRP 264 ASP 265 -0.0492

ASP 265 ASN 266 -0.0001

ASN 266 LYS 267 0.0151

LYS 267 LYS 268 0.0002

LYS 268 ASN 269 -0.1879

ASN 269 SER 270 -0.0002

SER 270 ALA 271 0.1763

ALA 271 ARG 272 -0.0000

ARG 272 THR 273 -0.4485

THR 273 VAL 274 -0.0002

VAL 274 SER 275 0.1879

SER 275 ASN 276 0.0004

ASN 276 ALA 277 0.1926

ALA 277 HIS 278 0.0002

HIS 278 ILE 279 -0.0417

ILE 279 ASP 280 -0.0001

ASP 280 GLU 281 -0.0190

GLU 281 ILE 282 0.0004

ILE 282 TYR 283 -0.1664

TYR 283 ASP 284 0.0002

ASP 284 ALA 285 -0.1017

ALA 285 ALA 286 0.0003

ALA 286 ILE 287 -0.0774

ILE 287 ARG 288 -0.0002

ARG 288 ALA 289 0.0363

ALA 289 GLY 290 -0.0002

GLY 290 ALA 291 -0.0507

ALA 291 GLN 292 0.0002

GLN 292 ALA 293 0.0684

ALA 293 GLY 294 -0.0001

GLY 294 LYS 295 0.1499

LYS 295 VAL 296 -0.0001

VAL 296 SER 297 -0.0240

SER 297 GLY 298 0.0000

GLY 298 ALA 299 -0.1624

ALA 299 GLY 300 0.0001

GLY 300 GLY 301 0.0624

GLY 301 GLY 302 -0.0003

GLY 302 GLY 303 -0.0751

GLY 303 PHE 304 -0.0000

PHE 304 MET 305 0.0650

MET 305 LEU 306 0.0000

LEU 306 PHE 307 0.0462

PHE 307 PHE 308 -0.0002

PHE 308 VAL 309 -0.0506

VAL 309 PRO 310 0.0003

PRO 310 THR 311 0.0841

THR 311 GLU 312 -0.0001

GLU 312 LYS 313 0.0459

LYS 313 ARG 314 -0.0000

ARG 314 MET 315 -0.1144

MET 315 ASP 316 -0.0002

ASP 316 LEU 317 0.0198

LEU 317 ILE 318 0.0000

ILE 318 ARG 319 -0.0226

ARG 319 THR 320 -0.0005

THR 320 LEU 321 0.0842

LEU 321 GLY 322 0.0001

GLY 322 GLU 323 -0.0516

GLU 323 TYR 324 -0.0001

TYR 324 ASP 325 0.0148

ASP 325 GLY 326 -0.0002

GLY 326 GLN 327 -0.0720

GLN 327 VAL 328 -0.0002

VAL 328 SER 329 -0.0294

SER 329 ASN 330 0.0001

ASN 330 CYS 331 -0.0367

CYS 331 HIS 332 -0.0002

HIS 332 PHE 333 -0.0466

PHE 333 THR 334 0.0002

THR 334 LYS 335 -0.0201

LYS 335 ASN 336 -0.0001

ASN 336 GLY 337 -0.1776

GLY 337 THR 338 0.0001

THR 338 GLN 339 0.1608

GLN 339 ALA 340 -0.0002

ALA 340 TRP 341 0.1404

TRP 341 ARG 342 0.0003

ARG 342 ILE 343 0.1897

ILE 343 ALA 344 -0.0001

ALA 344 ASN 345 0.0784

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 24021912300225903

--- normal mode 15 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *