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

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA strain for 24021912332929451

--- normal mode 12 ---

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
PRO 1 LEU 2 -0.0001

LEU 2 ILE 3 0.1856

ILE 3 ASN 4 -0.0001

ASN 4 SER 5 -0.1080

SER 5 ARG 6 -0.0001

ARG 6 THR 7 0.3201

THR 7 GLY 8 0.0001

GLY 8 SER 9 0.0123

SER 9 ILE 10 0.0001

ILE 10 TYR 11 0.1470

TYR 11 ILE 12 -0.0003

ILE 12 VAL 13 0.2487

VAL 13 LYS 14 0.0002

LYS 14 PRO 15 0.2069

PRO 15 LYS 16 -0.0000

LYS 16 MET 17 -0.0871

MET 17 HIS 18 -0.0001

HIS 18 GLY 19 -0.1800

GLY 19 PRO 20 -0.0005

PRO 20 ALA 21 0.0662

ALA 21 GLU 22 0.0001

GLU 22 VAL 23 0.0145

VAL 23 ALA 24 0.0001

ALA 24 PHE 25 -0.1041

PHE 25 THR 26 0.0003

THR 26 CYS 27 0.0191

CYS 27 GLU 28 -0.0002

GLU 28 LEU 29 -0.1031

LEU 29 PHE 30 -0.0002

PHE 30 SER 31 0.0598

SER 31 ARG 32 -0.0004

ARG 32 VAL 33 -0.0467

VAL 33 GLU 34 0.0001

GLU 34 ASP 35 -0.0237

ASP 35 VAL 36 0.0002

VAL 36 LEU 37 -0.0253

LEU 37 GLY 38 0.0004

GLY 38 LEU 39 -0.0216

LEU 39 PRO 40 -0.0000

PRO 40 GLN 41 -0.0658

GLN 41 ASN 42 0.0001

ASN 42 THR 43 -0.0044

THR 43 MET 44 -0.0001

MET 44 LYS 45 -0.0467

LYS 45 ILE 46 -0.0001

ILE 46 GLY 47 -0.0336

GLY 47 ILE 48 -0.0001

ILE 48 MET 49 -0.0087

MET 49 ASP 50 -0.0004

ASP 50 GLU 51 -0.0571

GLU 51 GLU 52 0.0001

GLU 52 ARG 53 -0.0397

ARG 53 ARG 54 0.0001

ARG 54 THR 55 0.0108

THR 55 THR 56 0.0001

THR 56 VAL 57 0.0204

VAL 57 ASN 58 -0.0000

ASN 58 LEU 59 -0.0060

LEU 59 LYS 60 0.0002

LYS 60 ALA 61 0.0313

ALA 61 CYS 62 0.0001

CYS 62 ILE 63 -0.0324

ILE 63 LYS 64 -0.0004

LYS 64 ALA 65 -0.0462

ALA 65 ALA 66 -0.0003

ALA 66 ALA 67 0.0533

ALA 67 ASP 68 -0.0001

ASP 68 ARG 69 0.0227

ARG 69 VAL 70 0.0002

VAL 70 VAL 71 -0.0609

VAL 71 PHE 72 0.0002

PHE 72 ILE 73 -0.1018

ILE 73 ASN 74 -0.0001

ASN 74 THR 75 -0.0581

THR 75 GLY 76 -0.0003

GLY 76 PHE 77 0.0297

PHE 77 LEU 78 -0.0001

LEU 78 ASP 79 0.0668

ASP 79 ARG 80 -0.0004

ARG 80 THR 81 0.0464

THR 81 GLY 82 -0.0002

GLY 82 ASP 83 -0.0058

ASP 83 GLU 84 -0.0001

GLU 84 ILE 85 0.0798

ILE 85 HIS 86 -0.0003

HIS 86 THR 87 -0.0367

THR 87 SER 88 0.0000

SER 88 MET 89 0.0557

MET 89 GLU 90 -0.0003

GLU 90 ALA 91 -0.0160

ALA 91 GLY 92 -0.0002

GLY 92 PRO 93 -0.0044

PRO 93 MET 94 -0.0001

MET 94 VAL 95 -0.0083

VAL 95 ARG 96 -0.0002

ARG 96 LYS 97 -0.1167

LYS 97 GLY 98 -0.0001

GLY 98 THR 99 0.0006

THR 99 MET 100 -0.0001

MET 100 LYS 101 -0.0083

LYS 101 SER 102 -0.0000

SER 102 GLN 103 -0.0564

GLN 103 PRO 104 0.0000

PRO 104 TRP 105 -0.0112

TRP 105 ILE 106 0.0002

ILE 106 LEU 107 -0.0031

LEU 107 ALA 108 0.0002

ALA 108 TYR 109 -0.0315

TYR 109 GLU 110 0.0002

GLU 110 ASP 111 -0.0357

ASP 111 HIS 112 -0.0003

HIS 112 ASN 113 -0.0186

ASN 113 VAL 114 -0.0004

VAL 114 ASP 115 -0.0248

ASP 115 ALA 116 0.0002

ALA 116 GLY 117 -0.0057

GLY 117 LEU 118 -0.0004

LEU 118 ALA 119 0.0184

ALA 119 ALA 120 0.0002

ALA 120 GLY 121 -0.0117

GLY 121 PHE 122 -0.0001

PHE 122 SER 123 -0.0979

SER 123 GLY 124 -0.0000

GLY 124 ARG 125 -0.0961

ARG 125 ALA 126 0.0001

ALA 126 GLN 127 -0.0605

GLN 127 VAL 128 0.0001

VAL 128 GLY 129 -0.0224

GLY 129 LYS 130 -0.0001

LYS 130 GLY 131 -0.1048

GLY 131 MET 132 -0.0003

MET 132 TRP 133 0.0045

TRP 133 THR 134 0.0000

THR 134 MET 135 0.0088

MET 135 THR 136 0.0001

THR 136 GLU 137 0.0310

GLU 137 LEU 138 -0.0001

LEU 138 MET 139 0.0351

MET 139 ALA 140 0.0003

ALA 140 ASP 141 -0.0016

ASP 141 MET 142 0.0003

MET 142 VAL 143 0.0295

VAL 143 GLU 144 0.0002

GLU 144 THR 145 -0.0141

THR 145 LYS 146 -0.0002

LYS 146 ILE 147 0.0071

ILE 147 ALA 148 -0.0000

ALA 148 GLN 149 0.0173

GLN 149 PRO 150 0.0000

PRO 150 ARG 151 -0.0173

ARG 151 ALA 152 0.0002

ALA 152 GLY 153 -0.0119

GLY 153 ALA 154 0.0004

ALA 154 SER 155 -0.0026

SER 155 THR 156 -0.0003

THR 156 ALA 157 -0.0775

ALA 157 TRP 158 0.0004

TRP 158 VAL 159 0.0235

VAL 159 PRO 160 0.0000

PRO 160 SER 161 -0.0576

SER 161 PRO 162 0.0000

PRO 162 THR 163 -0.0046

THR 163 ALA 164 -0.0001

ALA 164 ALA 165 -0.0001

ALA 165 THR 166 0.0000

THR 166 LEU 167 -0.0028

LEU 167 HIS 168 0.0002

HIS 168 ALA 169 -0.0084

ALA 169 LEU 170 0.0000

LEU 170 HIS 171 0.0050

HIS 171 TYR 172 -0.0002

TYR 172 HIS 173 -0.0526

HIS 173 GLN 174 -0.0000

GLN 174 VAL 175 0.0114

VAL 175 ASP 176 0.0001

ASP 176 VAL 177 -0.0642

VAL 177 ALA 178 -0.0003

ALA 178 ALA 179 -0.0361

ALA 179 VAL 180 -0.0002

VAL 180 GLN 181 -0.0579

GLN 181 GLN 182 0.0003

GLN 182 GLY 183 0.0115

GLY 183 LEU 184 -0.0000

LEU 184 ALA 185 -0.0108

ALA 185 GLY 186 -0.0002

GLY 186 LYS 187 0.0053

LYS 187 ARG 188 0.0002

ARG 188 ARG 189 0.0060

ARG 189 ALA 190 -0.0002

ALA 190 THR 191 0.0474

THR 191 ILE 192 -0.0003

ILE 192 GLU 193 0.0214

GLU 193 GLN 194 0.0002

GLN 194 LEU 195 0.0100

LEU 195 LEU 196 -0.0001

LEU 196 THR 197 0.0794

THR 197 ILE 198 0.0001

ILE 198 PRO 199 0.1110

PRO 199 LEU 200 0.0001

LEU 200 ALA 201 0.1083

ALA 201 LYS 202 -0.0001

LYS 202 GLU 203 0.0396

GLU 203 LEU 204 0.0003

LEU 204 ALA 205 0.0336

ALA 205 TRP 206 -0.0000

TRP 206 ALA 207 0.0362

ALA 207 PRO 208 -0.0003

PRO 208 ASP 209 -0.0067

ASP 209 GLU 210 -0.0002

GLU 210 ILE 211 -0.0184

ILE 211 ARG 212 0.0001

ARG 212 GLU 213 0.0013

GLU 213 GLU 214 0.0002

GLU 214 VAL 215 0.0614

VAL 215 ASP 216 0.0001

ASP 216 ASN 217 -0.0010

ASN 217 ASN 218 -0.0002

ASN 218 CYS 219 0.0240

CYS 219 GLN 220 0.0000

GLN 220 SER 221 -0.0206

SER 221 ILE 222 0.0001

ILE 222 LEU 223 -0.0236

LEU 223 GLY 224 -0.0002

GLY 224 TYR 225 -0.0332

TYR 225 VAL 226 -0.0002

VAL 226 VAL 227 -0.0480

VAL 227 ARG 228 -0.0002

ARG 228 TRP 229 0.0052

TRP 229 VAL 230 -0.0003

VAL 230 ASP 231 -0.0342

ASP 231 GLN 232 -0.0000

GLN 232 GLY 233 -0.0182

GLY 233 VAL 234 -0.0003

VAL 234 GLY 235 -0.1139

GLY 235 CYS 236 -0.0004

CYS 236 SER 237 0.0215

SER 237 LYS 238 0.0000

LYS 238 VAL 239 -0.0341

VAL 239 PRO 240 0.0003

PRO 240 ASP 241 -0.0309

ASP 241 ILE 242 -0.0002

ILE 242 HIS 243 0.0127

HIS 243 ASP 244 -0.0000

ASP 244 VAL 245 0.0337

VAL 245 ALA 246 -0.0003

ALA 246 LEU 247 -0.0194

LEU 247 MET 248 0.0002

MET 248 GLU 249 -0.0492

GLU 249 ASP 250 -0.0001

ASP 250 ARG 251 0.0720

ARG 251 ALA 252 0.0000

ALA 252 THR 253 -0.0252

THR 253 LEU 254 -0.0006

LEU 254 ARG 255 -0.0389

ARG 255 ILE 256 0.0003

ILE 256 SER 257 0.0474

SER 257 SER 258 -0.0000

SER 258 GLN 259 0.0085

GLN 259 LEU 260 0.0000

LEU 260 LEU 261 0.0469

LEU 261 ALA 262 -0.0003

ALA 262 ASN 263 0.0390

ASN 263 TRP 264 0.0000

TRP 264 LEU 265 0.0351

LEU 265 ARG 266 0.0001

ARG 266 HIS 267 0.0064

HIS 267 GLY 268 0.0002

GLY 268 VAL 269 -0.0430

VAL 269 ILE 270 -0.0001

ILE 270 THR 271 0.0357

THR 271 SER 272 0.0002

SER 272 ALA 273 -0.0059

ALA 273 ASP 274 0.0001

ASP 274 VAL 275 -0.0336

VAL 275 ARG 276 0.0000

ARG 276 ALA 277 -0.0228

ALA 277 SER 278 -0.0003

SER 278 LEU 279 0.0324

LEU 279 GLU 280 0.0001

GLU 280 ARG 281 0.0331

ARG 281 MET 282 0.0001

MET 282 ALA 283 0.0447

ALA 283 PRO 284 -0.0003

PRO 284 LEU 285 -0.0271

LEU 285 VAL 286 0.0002

VAL 286 ASP 287 -0.0084

ASP 287 ARG 288 0.0001

ARG 288 GLN 289 -0.0032

GLN 289 ASN 290 -0.0004

ASN 290 ALA 291 -0.0334

ALA 291 GLY 292 0.0000

GLY 292 ASP 293 0.0010

ASP 293 VAL 294 -0.0002

VAL 294 ALA 295 -0.0257

ALA 295 TYR 296 -0.0000

TYR 296 ARG 297 0.0097

ARG 297 PRO 298 -0.0003

PRO 298 MET 299 0.0190

MET 299 ALA 300 0.0000

ALA 300 PRO 301 -0.0037

PRO 301 ASN 302 -0.0001

ASN 302 PHE 303 0.0099

PHE 303 ASP 304 0.0001

ASP 304 ASP 305 0.0723

ASP 305 SER 306 0.0000

SER 306 ILE 307 -0.0404

ILE 307 ALA 308 -0.0003

ALA 308 PHE 309 0.0322

PHE 309 LEU 310 -0.0001

LEU 310 ALA 311 -0.0492

ALA 311 ALA 312 -0.0000

ALA 312 GLN 313 0.0027

GLN 313 GLU 314 0.0002

GLU 314 LEU 315 -0.0124

LEU 315 ILE 316 0.0004

ILE 316 LEU 317 -0.0144

LEU 317 SER 318 -0.0003

SER 318 GLY 319 -0.0076

GLY 319 ALA 320 -0.0002

ALA 320 GLN 321 0.0030

GLN 321 GLN 322 -0.0002

GLN 322 PRO 323 -0.0365

PRO 323 ASN 324 -0.0003

ASN 324 GLY 325 -0.0112

GLY 325 TYR 326 0.0000

TYR 326 THR 327 -0.1372

THR 327 GLU 328 0.0001

GLU 328 PRO 329 -0.0065

PRO 329 ILE 330 -0.0001

ILE 330 LEU 331 0.0367

LEU 331 HIS 332 -0.0001

HIS 332 ARG 333 -0.0036

ARG 333 ARG 334 0.0004

ARG 334 ARG 335 0.0463

ARG 335 ARG 336 0.0002

ARG 336 GLU 337 -0.0128

GLU 337 PHE 338 0.0001

PHE 338 LYS 339 0.0646

LYS 339 ALA 340 0.0005

ALA 340 ARG 341 0.0363

ARG 341 ALA 342 0.0001

ALA 342 ALA 343 0.0631

ALA 343 GLU 344 0.0001

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_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA strain for 24021912332929451

--- normal mode 12 ---

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

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *