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 8 ---

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 0.0003

PRO 2 THR 3 0.0898

THR 3 ILE 4 -0.0001

ILE 4 ILE 5 0.0560

ILE 5 ARG 6 -0.0000

ARG 6 ALA 7 0.0742

ALA 7 ARG 8 -0.0003

ARG 8 ALA 9 0.0615

ALA 9 PRO 10 0.0001

PRO 10 LEU 11 0.0016

LEU 11 ARG 12 0.0003

ARG 12 LEU 13 0.0118

LEU 13 GLY 14 -0.0002

GLY 14 LEU 15 -0.0671

LEU 15 ALA 16 -0.0002

ALA 16 GLY 17 -0.0112

GLY 17 GLY 18 0.0001

GLY 18 GLY 19 0.0001

GLY 19 THR 20 0.0003

THR 20 ASP 21 -0.0430

ASP 21 VAL 22 0.0002

VAL 22 ALA 23 0.0028

ALA 23 PRO 24 0.0000

PRO 24 TYR 25 -0.0129

TYR 25 ALA 26 0.0003

ALA 26 ASP 27 -0.0001

ASP 27 THR 28 0.0002

THR 28 PHE 29 -0.0111

PHE 29 GLY 30 0.0003

GLY 30 GLY 31 0.0132

GLY 31 TYR 32 0.0003

TYR 32 VAL 33 -0.0045

VAL 33 LEU 34 0.0001

LEU 34 ASN 35 0.0309

ASN 35 ALA 36 -0.0001

ALA 36 THR 37 0.0695

THR 37 ILE 38 -0.0003

ILE 38 ASP 39 -0.0004

ASP 39 ARG 40 -0.0001

ARG 40 TYR 41 0.0219

TYR 41 ALA 42 -0.0003

ALA 42 TYR 43 -0.0906

TYR 43 ALA 44 -0.0001

ALA 44 VAL 45 -0.0566

VAL 45 ILE 46 -0.0002

ILE 46 LYS 47 0.0055

LYS 47 THR 48 -0.0003

THR 48 LEU 49 0.0856

LEU 49 THR 50 0.0002

THR 50 ILE 51 0.0125

ILE 51 PRO 52 0.0002

PRO 52 ALA 53 -0.0391

ALA 53 VAL 54 -0.0000

VAL 54 ARG 55 -0.0258

ARG 55 PHE 56 0.0002

PHE 56 VAL 57 -0.0237

VAL 57 SER 58 0.0001

SER 58 THR 59 0.0630

THR 59 ASP 60 0.0001

ASP 60 GLN 61 0.0744

GLN 61 GLN 62 0.0005

GLN 62 VAL 63 0.1320

VAL 63 GLU 64 -0.0001

GLU 64 LYS 65 -0.0183

LYS 65 HIS 66 0.0002

HIS 66 GLN 67 0.0055

GLN 67 LEU 68 0.0002

LEU 68 ILE 69 0.0210

ILE 69 SER 70 0.0002

SER 70 GLU 71 0.0201

GLU 71 PRO 72 -0.0002

PRO 72 LEU 73 0.0282

LEU 73 GLU 74 -0.0000

GLU 74 LEU 75 -0.1040

LEU 75 ASN 76 -0.0000

ASN 76 GLY 77 0.0179

GLY 77 THR 78 0.0001

THR 78 LEU 79 -0.0137

LEU 79 ASN 80 -0.0000

ASN 80 LEU 81 -0.0612

LEU 81 HIS 82 0.0000

HIS 82 LYS 83 0.0117

LYS 83 ALA 84 -0.0004

ALA 84 VAL 85 -0.0042

VAL 85 TYR 86 -0.0001

TYR 86 ASN 87 -0.0042

ASN 87 HIS 88 -0.0000

HIS 88 MET 89 -0.0389

MET 89 ILE 90 0.0000

ILE 90 ARG 91 0.0178

ARG 91 ASN 92 -0.0001

ASN 92 TYR 93 -0.0112

TYR 93 ASN 94 0.0001

ASN 94 HIS 95 0.0135

HIS 95 GLY 96 -0.0000

GLY 96 LYS 97 -0.0139

LYS 97 PRO 98 0.0000

PRO 98 ILE 99 0.0128

ILE 99 ALA 100 -0.0001

ALA 100 LEU 101 -0.0060

LEU 101 GLU 102 -0.0003

GLU 102 LEU 103 -0.0330

LEU 103 SER 104 0.0004

SER 104 THR 105 -0.0761

THR 105 PHE 106 -0.0001

PHE 106 CYS 107 -0.1220

CYS 107 ASP 108 -0.0001

ASP 108 ALA 109 -0.1170

ALA 109 PRO 110 0.0001

PRO 110 ALA 111 -0.0276

ALA 111 GLY 112 0.0002

GLY 112 SER 113 -0.0439

SER 113 GLY 114 -0.0003

GLY 114 LEU 115 -0.0175

LEU 115 GLY 116 0.0001

GLY 116 SER 117 -0.0347

SER 117 SER 118 0.0005

SER 118 SER 119 0.0079

SER 119 THR 120 -0.0002

THR 120 LEU 121 -0.0367

LEU 121 VAL 122 0.0002

VAL 122 VAL 123 0.0163

VAL 123 VAL 124 0.0001

VAL 124 MET 125 0.0592

MET 125 ILE 126 0.0003

ILE 126 LYS 127 -0.0156

LYS 127 ALA 128 -0.0001

ALA 128 PHE 129 0.0359

PHE 129 VAL 130 -0.0001

VAL 130 GLU 131 0.0286

GLU 131 LEU 132 -0.0002

LEU 132 LEU 133 0.0007

LEU 133 ASN 134 0.0000

ASN 134 LEU 135 0.0254

LEU 135 PRO 136 -0.0000

PRO 136 LEU 137 0.0695

LEU 137 ASP 138 0.0002

ASP 138 ASP 139 0.0522

ASP 139 TYR 140 -0.0002

TYR 140 ALA 141 0.0753

ALA 141 ILE 142 -0.0004

ILE 142 ALA 143 0.0169

ALA 143 GLN 144 0.0000

GLN 144 LEU 145 0.0307

LEU 145 ALA 146 0.0000

ALA 146 TYR 147 -0.0333

TYR 147 ARG 148 -0.0002

ARG 148 ILE 149 -0.1193

ILE 149 GLU 150 0.0001

GLU 150 ARG 151 -0.0488

ARG 151 VAL 152 0.0000

VAL 152 ASP 153 -0.0887

ASP 153 CYS 154 -0.0002

CYS 154 GLY 155 -0.2987

GLY 155 LEU 156 0.0001

LEU 156 ALA 157 -0.5137

ALA 157 GLY 158 0.0005

GLY 158 GLY 159 -0.0234

GLY 159 ARG 160 0.0001

ARG 160 GLN 161 -0.0335

GLN 161 ASP 162 -0.0000

ASP 162 GLN 163 -0.0029

GLN 163 TYR 164 0.0000

TYR 164 SER 165 -0.0092

SER 165 ALA 166 0.0002

ALA 166 THR 167 0.0066

THR 167 PHE 168 -0.0000

PHE 168 GLY 169 -0.0283

GLY 169 GLY 170 -0.0003

GLY 170 PHE 171 0.1346

PHE 171 ASN 172 0.0002

ASN 172 PHE 173 0.0822

PHE 173 MET 174 -0.0002

MET 174 GLU 175 -0.0197

GLU 175 PHE 176 -0.0000

PHE 176 TYR 177 -0.0151

TYR 177 GLU 178 0.0000

GLU 178 GLU 179 -0.0368

GLU 179 GLU 180 0.0001

GLU 180 ARG 181 -0.0831

ARG 181 THR 182 0.0001

THR 182 ILE 183 -0.0882

ILE 183 VAL 184 0.0002

VAL 184 ASN 185 -0.0055

ASN 185 PRO 186 0.0001

PRO 186 LEU 187 0.0683

LEU 187 ARG 188 0.0003

ARG 188 ILE 189 -0.0382

ILE 189 LYS 190 -0.0001

LYS 190 ASN 191 -0.0308

ASN 191 TRP 192 0.0002

TRP 192 VAL 193 0.0006

VAL 193 LEU 194 -0.0001

LEU 194 CYS 195 -0.0148

CYS 195 GLU 196 -0.0003

GLU 196 LEU 197 0.0045

LEU 197 GLU 198 0.0000

GLU 198 ALA 199 0.0296

ALA 199 SER 200 -0.0002

SER 200 LEU 201 -0.0098

LEU 201 VAL 202 0.0001

VAL 202 LEU 203 -0.0233

LEU 203 PHE 204 -0.0004

PHE 204 TYR 205 -0.0109

TYR 205 THR 206 -0.0000

THR 206 GLY 207 0.0176

GLY 207 VAL 208 -0.0002

VAL 208 SER 209 -0.0049

SER 209 ARG 210 0.0001

ARG 210 GLU 211 -0.0200

GLU 211 SER 212 0.0000

SER 212 ALA 213 -0.0385

ALA 213 LYS 214 0.0001

LYS 214 ILE 215 -0.0038

ILE 215 ILE 216 0.0002

ILE 216 GLN 217 0.0208

GLN 217 ASP 218 -0.0001

ASP 218 GLN 219 0.0440

GLN 219 SER 220 0.0000

SER 220 ASP 221 -0.0002

ASP 221 ASN 222 -0.0003

ASN 222 VAL 223 0.0266

VAL 223 VAL 224 -0.0003

VAL 224 SER 225 0.0012

SER 225 HIS 226 0.0001

HIS 226 LYS 227 0.0155

LYS 227 THR 228 -0.0000

THR 228 ALA 229 0.0090

ALA 229 ALA 230 -0.0003

ALA 230 ILE 231 0.0048

ILE 231 GLU 232 0.0001

GLU 232 ALA 233 -0.0023

ALA 233 MET 234 0.0002

MET 234 HIS 235 -0.0047

HIS 235 GLY 236 -0.0001

GLY 236 ILE 237 -0.0129

ILE 237 LYS 238 0.0002

LYS 238 ARG 239 -0.0330

ARG 239 GLU 240 0.0001

GLU 240 ALA 241 0.0384

ALA 241 LEU 242 0.0002

LEU 242 VAL 243 -0.0223

VAL 243 MET 244 -0.0000

MET 244 LYS 245 0.0203

LYS 245 GLU 246 0.0004

GLU 246 ALA 247 0.0040

ALA 247 LEU 248 -0.0000

LEU 248 LEU 249 -0.0076

LEU 249 LYS 250 0.0000

LYS 250 GLY 251 -0.0027

GLY 251 ASP 252 -0.0002

ASP 252 PHE 253 -0.0063

PHE 253 LYS 254 0.0001

LYS 254 ALA 255 -0.0029

ALA 255 PHE 256 0.0001

PHE 256 VAL 257 0.0115

VAL 257 ALA 258 -0.0000

ALA 258 SER 259 -0.0007

SER 259 MET 260 -0.0002

MET 260 ARG 261 0.0118

ARG 261 LEU 262 0.0003

LEU 262 GLY 263 0.0064

GLY 263 TRP 264 0.0001

TRP 264 ASP 265 -0.0047

ASP 265 ASN 266 -0.0003

ASN 266 LYS 267 -0.0401

LYS 267 LYS 268 0.0002

LYS 268 ASN 269 0.0220

ASN 269 SER 270 -0.0003

SER 270 ALA 271 0.0132

ALA 271 ARG 272 -0.0000

ARG 272 THR 273 -0.0363

THR 273 VAL 274 0.0001

VAL 274 SER 275 0.0313

SER 275 ASN 276 0.0000

ASN 276 ALA 277 -0.0103

ALA 277 HIS 278 -0.0005

HIS 278 ILE 279 0.0093

ILE 279 ASP 280 0.0001

ASP 280 GLU 281 0.0155

GLU 281 ILE 282 0.0004

ILE 282 TYR 283 0.0121

TYR 283 ASP 284 0.0001

ASP 284 ALA 285 0.0144

ALA 285 ALA 286 -0.0003

ALA 286 ILE 287 -0.0010

ILE 287 ARG 288 0.0004

ARG 288 ALA 289 -0.0044

ALA 289 GLY 290 -0.0004

GLY 290 ALA 291 -0.0052

ALA 291 GLN 292 0.0000

GLN 292 ALA 293 -0.0245

ALA 293 GLY 294 -0.0001

GLY 294 LYS 295 -0.0469

LYS 295 VAL 296 -0.0001

VAL 296 SER 297 -0.0291

SER 297 GLY 298 0.0004

GLY 298 ALA 299 0.0170

ALA 299 GLY 300 -0.0004

GLY 300 GLY 301 0.0296

GLY 301 GLY 302 -0.0004

GLY 302 GLY 303 -0.0048

GLY 303 PHE 304 -0.0003

PHE 304 MET 305 -0.0960

MET 305 LEU 306 -0.0004

LEU 306 PHE 307 -0.0320

PHE 307 PHE 308 0.0000

PHE 308 VAL 309 -0.0185

VAL 309 PRO 310 -0.0002

PRO 310 THR 311 -0.0040

THR 311 GLU 312 0.0000

GLU 312 LYS 313 -0.0031

LYS 313 ARG 314 -0.0002

ARG 314 MET 315 -0.0089

MET 315 ASP 316 0.0000

ASP 316 LEU 317 0.0004

LEU 317 ILE 318 -0.0002

ILE 318 ARG 319 -0.0045

ARG 319 THR 320 0.0003

THR 320 LEU 321 -0.0120

LEU 321 GLY 322 -0.0001

GLY 322 GLU 323 0.0032

GLU 323 TYR 324 0.0001

TYR 324 ASP 325 0.0028

ASP 325 GLY 326 -0.0001

GLY 326 GLN 327 -0.0285

GLN 327 VAL 328 -0.0000

VAL 328 SER 329 -0.0270

SER 329 ASN 330 -0.0001

ASN 330 CYS 331 -0.0200

CYS 331 HIS 332 -0.0001

HIS 332 PHE 333 -0.0499

PHE 333 THR 334 -0.0004

THR 334 LYS 335 -0.0171

LYS 335 ASN 336 -0.0002

ASN 336 GLY 337 0.0710

GLY 337 THR 338 -0.0001

THR 338 GLN 339 0.1335

GLN 339 ALA 340 0.0001

ALA 340 TRP 341 0.1530

TRP 341 ARG 342 -0.0001

ARG 342 ILE 343 0.0561

ILE 343 ALA 344 0.0000

ALA 344 ASN 345 0.0688

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 8 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *