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 16 ---

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 0.2981

THR 3 ILE 4 -0.0002

ILE 4 ILE 5 0.0164

ILE 5 ARG 6 0.0002

ARG 6 ALA 7 0.0297

ALA 7 ARG 8 -0.0001

ARG 8 ALA 9 0.0464

ALA 9 PRO 10 -0.0004

PRO 10 LEU 11 0.1496

LEU 11 ARG 12 0.0001

ARG 12 LEU 13 -0.0627

LEU 13 GLY 14 0.0002

GLY 14 LEU 15 -0.0376

LEU 15 ALA 16 0.0002

ALA 16 GLY 17 -0.0912

GLY 17 GLY 18 0.0002

GLY 18 GLY 19 0.0327

GLY 19 THR 20 -0.0003

THR 20 ASP 21 0.0078

ASP 21 VAL 22 -0.0001

VAL 22 ALA 23 0.0163

ALA 23 PRO 24 -0.0001

PRO 24 TYR 25 -0.0622

TYR 25 ALA 26 -0.0000

ALA 26 ASP 27 0.0330

ASP 27 THR 28 0.0002

THR 28 PHE 29 0.0031

PHE 29 GLY 30 0.0000

GLY 30 GLY 31 -0.0985

GLY 31 TYR 32 0.0001

TYR 32 VAL 33 -0.0569

VAL 33 LEU 34 -0.0002

LEU 34 ASN 35 -0.0908

ASN 35 ALA 36 0.0003

ALA 36 THR 37 -0.0786

THR 37 ILE 38 -0.0002

ILE 38 ASP 39 -0.0102

ASP 39 ARG 40 -0.0002

ARG 40 TYR 41 0.1136

TYR 41 ALA 42 -0.0001

ALA 42 TYR 43 0.0532

TYR 43 ALA 44 -0.0002

ALA 44 VAL 45 -0.1337

VAL 45 ILE 46 -0.0001

ILE 46 LYS 47 -0.1753

LYS 47 THR 48 0.0001

THR 48 LEU 49 0.1132

LEU 49 THR 50 -0.0003

THR 50 ILE 51 -0.0215

ILE 51 PRO 52 0.0001

PRO 52 ALA 53 -0.1422

ALA 53 VAL 54 0.0002

VAL 54 ARG 55 -0.1220

ARG 55 PHE 56 0.0003

PHE 56 VAL 57 -0.0925

VAL 57 SER 58 0.0003

SER 58 THR 59 0.1483

THR 59 ASP 60 -0.0003

ASP 60 GLN 61 -0.0873

GLN 61 GLN 62 -0.0003

GLN 62 VAL 63 0.1493

VAL 63 GLU 64 0.0002

GLU 64 LYS 65 -0.1306

LYS 65 HIS 66 -0.0000

HIS 66 GLN 67 -0.0592

GLN 67 LEU 68 0.0002

LEU 68 ILE 69 -0.0036

ILE 69 SER 70 -0.0002

SER 70 GLU 71 -0.0049

GLU 71 PRO 72 0.0002

PRO 72 LEU 73 0.0695

LEU 73 GLU 74 0.0004

GLU 74 LEU 75 -0.1012

LEU 75 ASN 76 0.0003

ASN 76 GLY 77 0.0729

GLY 77 THR 78 -0.0001

THR 78 LEU 79 -0.0899

LEU 79 ASN 80 0.0002

ASN 80 LEU 81 -0.3260

LEU 81 HIS 82 -0.0000

HIS 82 LYS 83 -0.0075

LYS 83 ALA 84 0.0003

ALA 84 VAL 85 -0.1147

VAL 85 TYR 86 -0.0000

TYR 86 ASN 87 -0.0024

ASN 87 HIS 88 -0.0001

HIS 88 MET 89 -0.0270

MET 89 ILE 90 -0.0002

ILE 90 ARG 91 0.0176

ARG 91 ASN 92 0.0002

ASN 92 TYR 93 -0.1206

TYR 93 ASN 94 -0.0004

ASN 94 HIS 95 -0.0704

HIS 95 GLY 96 0.0001

GLY 96 LYS 97 0.0447

LYS 97 PRO 98 0.0001

PRO 98 ILE 99 0.0343

ILE 99 ALA 100 -0.0001

ALA 100 LEU 101 -0.0516

LEU 101 GLU 102 0.0001

GLU 102 LEU 103 -0.1762

LEU 103 SER 104 -0.0004

SER 104 THR 105 -0.2241

THR 105 PHE 106 -0.0000

PHE 106 CYS 107 -0.0991

CYS 107 ASP 108 0.0002

ASP 108 ALA 109 0.2192

ALA 109 PRO 110 -0.0003

PRO 110 ALA 111 0.0479

ALA 111 GLY 112 -0.0000

GLY 112 SER 113 -0.0311

SER 113 GLY 114 0.0000

GLY 114 LEU 115 0.1229

LEU 115 GLY 116 0.0002

GLY 116 SER 117 -0.0601

SER 117 SER 118 -0.0001

SER 118 SER 119 0.0649

SER 119 THR 120 -0.0004

THR 120 LEU 121 -0.2654

LEU 121 VAL 122 -0.0001

VAL 122 VAL 123 -0.1873

VAL 123 VAL 124 -0.0001

VAL 124 MET 125 -0.1411

MET 125 ILE 126 -0.0001

ILE 126 LYS 127 -0.0651

LYS 127 ALA 128 -0.0001

ALA 128 PHE 129 -0.0402

PHE 129 VAL 130 0.0000

VAL 130 GLU 131 -0.1855

GLU 131 LEU 132 -0.0000

LEU 132 LEU 133 -0.0296

LEU 133 ASN 134 -0.0002

ASN 134 LEU 135 -0.0727

LEU 135 PRO 136 0.0000

PRO 136 LEU 137 -0.0053

LEU 137 ASP 138 0.0003

ASP 138 ASP 139 0.0622

ASP 139 TYR 140 -0.0001

TYR 140 ALA 141 -0.1030

ALA 141 ILE 142 0.0004

ILE 142 ALA 143 0.0678

ALA 143 GLN 144 -0.0001

GLN 144 LEU 145 -0.1687

LEU 145 ALA 146 0.0003

ALA 146 TYR 147 0.0747

TYR 147 ARG 148 -0.0002

ARG 148 ILE 149 -0.1795

ILE 149 GLU 150 0.0002

GLU 150 ARG 151 0.0441

ARG 151 VAL 152 0.0001

VAL 152 ASP 153 -0.0191

ASP 153 CYS 154 0.0001

CYS 154 GLY 155 -0.0204

GLY 155 LEU 156 -0.0000

LEU 156 ALA 157 0.0725

ALA 157 GLY 158 0.0001

GLY 158 GLY 159 -0.0039

GLY 159 ARG 160 -0.0003

ARG 160 GLN 161 -0.0350

GLN 161 ASP 162 0.0004

ASP 162 GLN 163 0.0604

GLN 163 TYR 164 0.0002

TYR 164 SER 165 -0.0275

SER 165 ALA 166 0.0001

ALA 166 THR 167 0.0255

THR 167 PHE 168 0.0001

PHE 168 GLY 169 -0.0091

GLY 169 GLY 170 0.0002

GLY 170 PHE 171 -0.1113

PHE 171 ASN 172 -0.0003

ASN 172 PHE 173 -0.1897

PHE 173 MET 174 -0.0002

MET 174 GLU 175 -0.0543

GLU 175 PHE 176 0.0003

PHE 176 TYR 177 0.0231

TYR 177 GLU 178 -0.0003

GLU 178 GLU 179 -0.0183

GLU 179 GLU 180 -0.0001

GLU 180 ARG 181 -0.0755

ARG 181 THR 182 0.0003

THR 182 ILE 183 -0.0443

ILE 183 VAL 184 -0.0002

VAL 184 ASN 185 -0.1846

ASN 185 PRO 186 0.0002

PRO 186 LEU 187 -0.3223

LEU 187 ARG 188 0.0001

ARG 188 ILE 189 -0.1281

ILE 189 LYS 190 -0.0002

LYS 190 ASN 191 -0.0605

ASN 191 TRP 192 -0.0002

TRP 192 VAL 193 -0.0096

VAL 193 LEU 194 -0.0002

LEU 194 CYS 195 -0.0714

CYS 195 GLU 196 -0.0001

GLU 196 LEU 197 -0.0308

LEU 197 GLU 198 -0.0001

GLU 198 ALA 199 -0.0268

ALA 199 SER 200 -0.0000

SER 200 LEU 201 0.0238

LEU 201 VAL 202 0.0001

VAL 202 LEU 203 0.1242

LEU 203 PHE 204 0.0002

PHE 204 TYR 205 0.1413

TYR 205 THR 206 0.0004

THR 206 GLY 207 -0.1510

GLY 207 VAL 208 0.0000

VAL 208 SER 209 0.1954

SER 209 ARG 210 0.0003

ARG 210 GLU 211 0.5161

GLU 211 SER 212 0.0000

SER 212 ALA 213 0.0721

ALA 213 LYS 214 0.0003

LYS 214 ILE 215 -0.1590

ILE 215 ILE 216 0.0000

ILE 216 GLN 217 0.0407

GLN 217 ASP 218 0.0002

ASP 218 GLN 219 -0.0662

GLN 219 SER 220 0.0002

SER 220 ASP 221 -0.0700

ASP 221 ASN 222 0.0002

ASN 222 VAL 223 0.0261

VAL 223 VAL 224 -0.0001

VAL 224 SER 225 -0.1735

SER 225 HIS 226 -0.0000

HIS 226 LYS 227 0.0941

LYS 227 THR 228 0.0002

THR 228 ALA 229 0.2126

ALA 229 ALA 230 0.0002

ALA 230 ILE 231 0.1358

ILE 231 GLU 232 -0.0002

GLU 232 ALA 233 0.1528

ALA 233 MET 234 0.0001

MET 234 HIS 235 0.0360

HIS 235 GLY 236 -0.0000

GLY 236 ILE 237 0.0004

ILE 237 LYS 238 -0.0004

LYS 238 ARG 239 0.0391

ARG 239 GLU 240 -0.0000

GLU 240 ALA 241 0.0013

ALA 241 LEU 242 0.0001

LEU 242 VAL 243 -0.1180

VAL 243 MET 244 -0.0003

MET 244 LYS 245 0.1104

LYS 245 GLU 246 0.0001

GLU 246 ALA 247 -0.1236

ALA 247 LEU 248 0.0000

LEU 248 LEU 249 0.0481

LEU 249 LYS 250 0.0000

LYS 250 GLY 251 -0.0379

GLY 251 ASP 252 0.0001

ASP 252 PHE 253 -0.0079

PHE 253 LYS 254 -0.0001

LYS 254 ALA 255 -0.2307

ALA 255 PHE 256 -0.0005

PHE 256 VAL 257 0.0495

VAL 257 ALA 258 -0.0000

ALA 258 SER 259 -0.0214

SER 259 MET 260 -0.0001

MET 260 ARG 261 0.0419

ARG 261 LEU 262 -0.0003

LEU 262 GLY 263 0.0200

GLY 263 TRP 264 -0.0002

TRP 264 ASP 265 0.0248

ASP 265 ASN 266 0.0002

ASN 266 LYS 267 -0.0791

LYS 267 LYS 268 0.0000

LYS 268 ASN 269 0.3972

ASN 269 SER 270 -0.0003

SER 270 ALA 271 -0.0009

ALA 271 ARG 272 0.0003

ARG 272 THR 273 0.2989

THR 273 VAL 274 0.0001

VAL 274 SER 275 0.3444

SER 275 ASN 276 0.0000

ASN 276 ALA 277 0.1792

ALA 277 HIS 278 -0.0002

HIS 278 ILE 279 -0.0379

ILE 279 ASP 280 -0.0003

ASP 280 GLU 281 0.2086

GLU 281 ILE 282 -0.0000

ILE 282 TYR 283 0.0438

TYR 283 ASP 284 0.0003

ASP 284 ALA 285 0.0635

ALA 285 ALA 286 -0.0002

ALA 286 ILE 287 0.0200

ILE 287 ARG 288 -0.0002

ARG 288 ALA 289 -0.0943

ALA 289 GLY 290 -0.0003

GLY 290 ALA 291 0.0050

ALA 291 GLN 292 0.0001

GLN 292 ALA 293 -0.0903

ALA 293 GLY 294 -0.0000

GLY 294 LYS 295 -0.0398

LYS 295 VAL 296 -0.0002

VAL 296 SER 297 0.0670

SER 297 GLY 298 -0.0003

GLY 298 ALA 299 0.1170

ALA 299 GLY 300 -0.0005

GLY 300 GLY 301 -0.0365

GLY 301 GLY 302 0.0001

GLY 302 GLY 303 0.3392

GLY 303 PHE 304 0.0002

PHE 304 MET 305 -0.0710

MET 305 LEU 306 -0.0000

LEU 306 PHE 307 0.0092

PHE 307 PHE 308 -0.0002

PHE 308 VAL 309 -0.0519

VAL 309 PRO 310 0.0002

PRO 310 THR 311 -0.0022

THR 311 GLU 312 0.0002

GLU 312 LYS 313 -0.0384

LYS 313 ARG 314 -0.0002

ARG 314 MET 315 -0.1852

MET 315 ASP 316 0.0003

ASP 316 LEU 317 0.0639

LEU 317 ILE 318 -0.0003

ILE 318 ARG 319 -0.0987

ARG 319 THR 320 0.0001

THR 320 LEU 321 0.0887

LEU 321 GLY 322 0.0001

GLY 322 GLU 323 -0.0256

GLU 323 TYR 324 -0.0003

TYR 324 ASP 325 0.0172

ASP 325 GLY 326 -0.0000

GLY 326 GLN 327 -0.1727

GLN 327 VAL 328 0.0003

VAL 328 SER 329 -0.2250

SER 329 ASN 330 0.0003

ASN 330 CYS 331 -0.1805

CYS 331 HIS 332 0.0001

HIS 332 PHE 333 -0.1545

PHE 333 THR 334 0.0002

THR 334 LYS 335 -0.1161

LYS 335 ASN 336 0.0002

ASN 336 GLY 337 -0.0716

GLY 337 THR 338 0.0002

THR 338 GLN 339 -0.0731

GLN 339 ALA 340 -0.0002

ALA 340 TRP 341 -0.0852

TRP 341 ARG 342 -0.0002

ARG 342 ILE 343 -0.3053

ILE 343 ALA 344 -0.0000

ALA 344 ASN 345 -0.2311

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 16 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *