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 9 ---

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 0.0677

THR 3 ILE 4 -0.0002

ILE 4 ILE 5 -0.0372

ILE 5 ARG 6 -0.0001

ARG 6 ALA 7 -0.1626

ALA 7 ARG 8 0.0000

ARG 8 ALA 9 -0.1338

ALA 9 PRO 10 0.0004

PRO 10 LEU 11 -0.0669

LEU 11 ARG 12 0.0002

ARG 12 LEU 13 -0.1031

LEU 13 GLY 14 0.0002

GLY 14 LEU 15 -0.0568

LEU 15 ALA 16 0.0000

ALA 16 GLY 17 0.0036

GLY 17 GLY 18 0.0000

GLY 18 GLY 19 -0.0145

GLY 19 THR 20 -0.0000

THR 20 ASP 21 0.0866

ASP 21 VAL 22 -0.0003

VAL 22 ALA 23 0.0050

ALA 23 PRO 24 0.0000

PRO 24 TYR 25 -0.0021

TYR 25 ALA 26 -0.0002

ALA 26 ASP 27 0.0156

ASP 27 THR 28 -0.0004

THR 28 PHE 29 0.0264

PHE 29 GLY 30 0.0000

GLY 30 GLY 31 -0.0244

GLY 31 TYR 32 0.0000

TYR 32 VAL 33 -0.0539

VAL 33 LEU 34 0.0002

LEU 34 ASN 35 -0.0855

ASN 35 ALA 36 0.0002

ALA 36 THR 37 -0.0754

THR 37 ILE 38 -0.0002

ILE 38 ASP 39 -0.0061

ASP 39 ARG 40 -0.0004

ARG 40 TYR 41 -0.4258

TYR 41 ALA 42 0.0003

ALA 42 TYR 43 -0.1690

TYR 43 ALA 44 -0.0001

ALA 44 VAL 45 -0.1326

VAL 45 ILE 46 -0.0001

ILE 46 LYS 47 -0.0325

LYS 47 THR 48 0.0001

THR 48 LEU 49 -0.0313

LEU 49 THR 50 -0.0000

THR 50 ILE 51 -0.0117

ILE 51 PRO 52 0.0001

PRO 52 ALA 53 -0.0408

ALA 53 VAL 54 -0.0000

VAL 54 ARG 55 -0.0707

ARG 55 PHE 56 0.0002

PHE 56 VAL 57 -0.0913

VAL 57 SER 58 0.0001

SER 58 THR 59 0.0651

THR 59 ASP 60 -0.0001

ASP 60 GLN 61 0.0741

GLN 61 GLN 62 0.0001

GLN 62 VAL 63 0.0637

VAL 63 GLU 64 0.0001

GLU 64 LYS 65 -0.0377

LYS 65 HIS 66 -0.0002

HIS 66 GLN 67 -0.0312

GLN 67 LEU 68 0.0003

LEU 68 ILE 69 0.0073

ILE 69 SER 70 -0.0000

SER 70 GLU 71 -0.0129

GLU 71 PRO 72 -0.0000

PRO 72 LEU 73 -0.0241

LEU 73 GLU 74 -0.0002

GLU 74 LEU 75 0.0651

LEU 75 ASN 76 0.0001

ASN 76 GLY 77 0.0006

GLY 77 THR 78 0.0002

THR 78 LEU 79 0.0034

LEU 79 ASN 80 -0.0002

ASN 80 LEU 81 0.0128

LEU 81 HIS 82 -0.0003

HIS 82 LYS 83 -0.0217

LYS 83 ALA 84 -0.0001

ALA 84 VAL 85 -0.0106

VAL 85 TYR 86 -0.0000

TYR 86 ASN 87 0.0140

ASN 87 HIS 88 -0.0004

HIS 88 MET 89 0.0614

MET 89 ILE 90 0.0000

ILE 90 ARG 91 -0.0290

ARG 91 ASN 92 -0.0001

ASN 92 TYR 93 -0.0282

TYR 93 ASN 94 -0.0002

ASN 94 HIS 95 -0.0556

HIS 95 GLY 96 0.0001

GLY 96 LYS 97 0.0370

LYS 97 PRO 98 -0.0001

PRO 98 ILE 99 -0.0386

ILE 99 ALA 100 0.0001

ALA 100 LEU 101 -0.0669

LEU 101 GLU 102 -0.0000

GLU 102 LEU 103 -0.0558

LEU 103 SER 104 0.0000

SER 104 THR 105 -0.2135

THR 105 PHE 106 0.0002

PHE 106 CYS 107 -0.2466

CYS 107 ASP 108 -0.0002

ASP 108 ALA 109 -0.1101

ALA 109 PRO 110 -0.0000

PRO 110 ALA 111 -0.0012

ALA 111 GLY 112 0.0000

GLY 112 SER 113 -0.0169

SER 113 GLY 114 0.0001

GLY 114 LEU 115 0.0098

LEU 115 GLY 116 -0.0003

GLY 116 SER 117 -0.0291

SER 117 SER 118 0.0004

SER 118 SER 119 -0.0539

SER 119 THR 120 -0.0001

THR 120 LEU 121 -0.0154

LEU 121 VAL 122 -0.0004

VAL 122 VAL 123 -0.0012

VAL 123 VAL 124 0.0003

VAL 124 MET 125 -0.0264

MET 125 ILE 126 -0.0004

ILE 126 LYS 127 0.0054

LYS 127 ALA 128 0.0000

ALA 128 PHE 129 -0.1084

PHE 129 VAL 130 0.0002

VAL 130 GLU 131 0.1213

GLU 131 LEU 132 0.0003

LEU 132 LEU 133 0.0004

LEU 133 ASN 134 0.0001

ASN 134 LEU 135 0.0869

LEU 135 PRO 136 0.0001

PRO 136 LEU 137 0.1124

LEU 137 ASP 138 0.0001

ASP 138 ASP 139 -0.0356

ASP 139 TYR 140 0.0004

TYR 140 ALA 141 0.1468

ALA 141 ILE 142 0.0004

ILE 142 ALA 143 0.0464

ALA 143 GLN 144 0.0002

GLN 144 LEU 145 0.2621

LEU 145 ALA 146 -0.0003

ALA 146 TYR 147 0.0903

TYR 147 ARG 148 0.0001

ARG 148 ILE 149 0.1657

ILE 149 GLU 150 0.0002

GLU 150 ARG 151 0.0293

ARG 151 VAL 152 -0.0003

VAL 152 ASP 153 0.1095

ASP 153 CYS 154 0.0002

CYS 154 GLY 155 0.1139

GLY 155 LEU 156 -0.0003

LEU 156 ALA 157 0.2151

ALA 157 GLY 158 0.0002

GLY 158 GLY 159 -0.0755

GLY 159 ARG 160 0.0002

ARG 160 GLN 161 0.0537

GLN 161 ASP 162 -0.0000

ASP 162 GLN 163 0.0170

GLN 163 TYR 164 -0.0001

TYR 164 SER 165 0.0040

SER 165 ALA 166 -0.0002

ALA 166 THR 167 -0.0203

THR 167 PHE 168 0.0003

PHE 168 GLY 169 -0.0462

GLY 169 GLY 170 -0.0001

GLY 170 PHE 171 -0.0582

PHE 171 ASN 172 0.0000

ASN 172 PHE 173 -0.0590

PHE 173 MET 174 0.0001

MET 174 GLU 175 -0.0422

GLU 175 PHE 176 0.0001

PHE 176 TYR 177 -0.0496

TYR 177 GLU 178 -0.0001

GLU 178 GLU 179 0.1358

GLU 179 GLU 180 0.0000

GLU 180 ARG 181 0.0185

ARG 181 THR 182 -0.0002

THR 182 ILE 183 -0.0196

ILE 183 VAL 184 -0.0004

VAL 184 ASN 185 0.0524

ASN 185 PRO 186 -0.0002

PRO 186 LEU 187 0.0589

LEU 187 ARG 188 0.0003

ARG 188 ILE 189 0.0329

ILE 189 LYS 190 -0.0001

LYS 190 ASN 191 -0.0037

ASN 191 TRP 192 0.0001

TRP 192 VAL 193 -0.0081

VAL 193 LEU 194 0.0001

LEU 194 CYS 195 -0.0016

CYS 195 GLU 196 0.0004

GLU 196 LEU 197 -0.0077

LEU 197 GLU 198 -0.0002

GLU 198 ALA 199 -0.0812

ALA 199 SER 200 0.0002

SER 200 LEU 201 0.0010

LEU 201 VAL 202 -0.0001

VAL 202 LEU 203 -0.0306

LEU 203 PHE 204 0.0000

PHE 204 TYR 205 0.0150

TYR 205 THR 206 0.0004

THR 206 GLY 207 0.0345

GLY 207 VAL 208 0.0000

VAL 208 SER 209 -0.0364

SER 209 ARG 210 -0.0004

ARG 210 GLU 211 -0.0212

GLU 211 SER 212 0.0003

SER 212 ALA 213 0.0325

ALA 213 LYS 214 0.0002

LYS 214 ILE 215 0.0121

ILE 215 ILE 216 0.0002

ILE 216 GLN 217 0.0003

GLN 217 ASP 218 -0.0005

ASP 218 GLN 219 -0.0218

GLN 219 SER 220 0.0002

SER 220 ASP 221 0.0109

ASP 221 ASN 222 -0.0002

ASN 222 VAL 223 0.0132

VAL 223 VAL 224 0.0001

VAL 224 SER 225 0.0082

SER 225 HIS 226 0.0003

HIS 226 LYS 227 -0.0086

LYS 227 THR 228 -0.0002

THR 228 ALA 229 -0.0197

ALA 229 ALA 230 0.0000

ALA 230 ILE 231 0.0228

ILE 231 GLU 232 -0.0000

GLU 232 ALA 233 0.0078

ALA 233 MET 234 -0.0000

MET 234 HIS 235 -0.0165

HIS 235 GLY 236 -0.0001

GLY 236 ILE 237 -0.0087

ILE 237 LYS 238 0.0000

LYS 238 ARG 239 0.0387

ARG 239 GLU 240 -0.0001

GLU 240 ALA 241 0.0164

ALA 241 LEU 242 0.0002

LEU 242 VAL 243 0.0920

VAL 243 MET 244 -0.0002

MET 244 LYS 245 0.0150

LYS 245 GLU 246 0.0003

GLU 246 ALA 247 0.0681

ALA 247 LEU 248 0.0002

LEU 248 LEU 249 0.0122

LEU 249 LYS 250 -0.0001

LYS 250 GLY 251 0.0077

GLY 251 ASP 252 -0.0001

ASP 252 PHE 253 0.0261

PHE 253 LYS 254 -0.0003

LYS 254 ALA 255 0.0397

ALA 255 PHE 256 -0.0001

PHE 256 VAL 257 0.0297

VAL 257 ALA 258 -0.0001

ALA 258 SER 259 0.0475

SER 259 MET 260 -0.0003

MET 260 ARG 261 -0.0176

ARG 261 LEU 262 0.0003

LEU 262 GLY 263 0.0237

GLY 263 TRP 264 0.0003

TRP 264 ASP 265 -0.0206

ASP 265 ASN 266 -0.0001

ASN 266 LYS 267 -0.0243

LYS 267 LYS 268 0.0005

LYS 268 ASN 269 0.0119

ASN 269 SER 270 0.0002

SER 270 ALA 271 -0.0052

ALA 271 ARG 272 0.0000

ARG 272 THR 273 -0.0148

THR 273 VAL 274 0.0001

VAL 274 SER 275 0.0550

SER 275 ASN 276 -0.0003

ASN 276 ALA 277 0.0192

ALA 277 HIS 278 -0.0001

HIS 278 ILE 279 0.0021

ILE 279 ASP 280 0.0000

ASP 280 GLU 281 0.0342

GLU 281 ILE 282 0.0001

ILE 282 TYR 283 0.0227

TYR 283 ASP 284 0.0001

ASP 284 ALA 285 0.0345

ALA 285 ALA 286 0.0003

ALA 286 ILE 287 -0.0011

ILE 287 ARG 288 -0.0002

ARG 288 ALA 289 -0.0127

ALA 289 GLY 290 -0.0001

GLY 290 ALA 291 0.0171

ALA 291 GLN 292 -0.0005

GLN 292 ALA 293 0.0137

ALA 293 GLY 294 0.0001

GLY 294 LYS 295 0.0020

LYS 295 VAL 296 0.0002

VAL 296 SER 297 -0.0380

SER 297 GLY 298 0.0001

GLY 298 ALA 299 0.0086

ALA 299 GLY 300 0.0000

GLY 300 GLY 301 0.0046

GLY 301 GLY 302 -0.0005

GLY 302 GLY 303 -0.0064

GLY 303 PHE 304 -0.0002

PHE 304 MET 305 -0.1101

MET 305 LEU 306 -0.0000

LEU 306 PHE 307 -0.0243

PHE 307 PHE 308 0.0002

PHE 308 VAL 309 0.0392

VAL 309 PRO 310 -0.0002

PRO 310 THR 311 0.0103

THR 311 GLU 312 -0.0002

GLU 312 LYS 313 0.0070

LYS 313 ARG 314 -0.0002

ARG 314 MET 315 0.0112

MET 315 ASP 316 -0.0002

ASP 316 LEU 317 -0.0017

LEU 317 ILE 318 -0.0002

ILE 318 ARG 319 -0.0304

ARG 319 THR 320 0.0002

THR 320 LEU 321 -0.0410

LEU 321 GLY 322 -0.0003

GLY 322 GLU 323 0.0033

GLU 323 TYR 324 0.0000

TYR 324 ASP 325 0.0007

ASP 325 GLY 326 0.0002

GLY 326 GLN 327 -0.0009

GLN 327 VAL 328 -0.0003

VAL 328 SER 329 -0.0415

SER 329 ASN 330 -0.0002

ASN 330 CYS 331 0.0189

CYS 331 HIS 332 0.0002

HIS 332 PHE 333 -0.0251

PHE 333 THR 334 0.0001

THR 334 LYS 335 0.0036

LYS 335 ASN 336 -0.0001

ASN 336 GLY 337 -0.0464

GLY 337 THR 338 0.0002

THR 338 GLN 339 0.0502

GLN 339 ALA 340 0.0004

ALA 340 TRP 341 0.0346

TRP 341 ARG 342 0.0002

ARG 342 ILE 343 0.0493

ILE 343 ALA 344 0.0000

ALA 344 ASN 345 0.1295

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 9 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *