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 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
PRO 1 LEU 2 0.0001

LEU 2 ILE 3 0.0364

ILE 3 ASN 4 -0.0000

ASN 4 SER 5 0.0216

SER 5 ARG 6 -0.0001

ARG 6 THR 7 0.0183

THR 7 GLY 8 -0.0002

GLY 8 SER 9 -0.0361

SER 9 ILE 10 0.0002

ILE 10 TYR 11 -0.0541

TYR 11 ILE 12 0.0000

ILE 12 VAL 13 -0.1761

VAL 13 LYS 14 0.0000

LYS 14 PRO 15 -0.1654

PRO 15 LYS 16 -0.0003

LYS 16 MET 17 -0.1140

MET 17 HIS 18 0.0002

HIS 18 GLY 19 -0.0775

GLY 19 PRO 20 -0.0001

PRO 20 ALA 21 0.0341

ALA 21 GLU 22 -0.0002

GLU 22 VAL 23 -0.0046

VAL 23 ALA 24 0.0004

ALA 24 PHE 25 -0.0052

PHE 25 THR 26 -0.0004

THR 26 CYS 27 -0.0354

CYS 27 GLU 28 0.0001

GLU 28 LEU 29 -0.0148

LEU 29 PHE 30 -0.0000

PHE 30 SER 31 -0.0564

SER 31 ARG 32 0.0002

ARG 32 VAL 33 0.0176

VAL 33 GLU 34 -0.0002

GLU 34 ASP 35 -0.0221

ASP 35 VAL 36 -0.0000

VAL 36 LEU 37 0.0046

LEU 37 GLY 38 0.0000

GLY 38 LEU 39 -0.0088

LEU 39 PRO 40 0.0001

PRO 40 GLN 41 0.0348

GLN 41 ASN 42 -0.0002

ASN 42 THR 43 0.0475

THR 43 MET 44 -0.0002

MET 44 LYS 45 -0.0598

LYS 45 ILE 46 -0.0001

ILE 46 GLY 47 -0.1285

GLY 47 ILE 48 0.0002

ILE 48 MET 49 -0.0554

MET 49 ASP 50 -0.0002

ASP 50 GLU 51 -0.0061

GLU 51 GLU 52 0.0001

GLU 52 ARG 53 -0.0678

ARG 53 ARG 54 0.0004

ARG 54 THR 55 0.0232

THR 55 THR 56 0.0000

THR 56 VAL 57 -0.0169

VAL 57 ASN 58 0.0001

ASN 58 LEU 59 -0.0031

LEU 59 LYS 60 0.0001

LYS 60 ALA 61 0.0176

ALA 61 CYS 62 0.0002

CYS 62 ILE 63 0.0114

ILE 63 LYS 64 0.0000

LYS 64 ALA 65 0.0032

ALA 65 ALA 66 -0.0001

ALA 66 ALA 67 -0.0684

ALA 67 ASP 68 0.0000

ASP 68 ARG 69 -0.0294

ARG 69 VAL 70 0.0002

VAL 70 VAL 71 -0.0768

VAL 71 PHE 72 0.0004

PHE 72 ILE 73 -0.0366

ILE 73 ASN 74 0.0001

ASN 74 THR 75 -0.0366

THR 75 GLY 76 0.0001

GLY 76 PHE 77 -0.0752

PHE 77 LEU 78 0.0002

LEU 78 ASP 79 -0.0128

ASP 79 ARG 80 0.0005

ARG 80 THR 81 -0.0085

THR 81 GLY 82 -0.0002

GLY 82 ASP 83 0.0044

ASP 83 GLU 84 -0.0002

GLU 84 ILE 85 0.0311

ILE 85 HIS 86 -0.0003

HIS 86 THR 87 -0.0363

THR 87 SER 88 0.0002

SER 88 MET 89 0.0088

MET 89 GLU 90 -0.0000

GLU 90 ALA 91 -0.0343

ALA 91 GLY 92 0.0003

GLY 92 PRO 93 0.0143

PRO 93 MET 94 0.0003

MET 94 VAL 95 -0.0025

VAL 95 ARG 96 -0.0001

ARG 96 LYS 97 -0.0473

LYS 97 GLY 98 -0.0003

GLY 98 THR 99 0.0339

THR 99 MET 100 0.0001

MET 100 LYS 101 -0.0072

LYS 101 SER 102 0.0001

SER 102 GLN 103 0.0058

GLN 103 PRO 104 -0.0000

PRO 104 TRP 105 -0.0133

TRP 105 ILE 106 0.0001

ILE 106 LEU 107 0.0139

LEU 107 ALA 108 -0.0000

ALA 108 TYR 109 -0.0111

TYR 109 GLU 110 -0.0000

GLU 110 ASP 111 0.0107

ASP 111 HIS 112 0.0000

HIS 112 ASN 113 -0.0199

ASN 113 VAL 114 0.0001

VAL 114 ASP 115 -0.0020

ASP 115 ALA 116 -0.0000

ALA 116 GLY 117 0.0016

GLY 117 LEU 118 0.0001

LEU 118 ALA 119 -0.0041

ALA 119 ALA 120 -0.0001

ALA 120 GLY 121 -0.0015

GLY 121 PHE 122 0.0001

PHE 122 SER 123 0.0202

SER 123 GLY 124 0.0002

GLY 124 ARG 125 0.0081

ARG 125 ALA 126 -0.0003

ALA 126 GLN 127 -0.0060

GLN 127 VAL 128 0.0001

VAL 128 GLY 129 -0.0270

GLY 129 LYS 130 -0.0001

LYS 130 GLY 131 -0.0095

GLY 131 MET 132 -0.0001

MET 132 TRP 133 -0.0516

TRP 133 THR 134 -0.0001

THR 134 MET 135 -0.0216

MET 135 THR 136 0.0003

THR 136 GLU 137 -0.0141

GLU 137 LEU 138 -0.0000

LEU 138 MET 139 -0.0321

MET 139 ALA 140 0.0000

ALA 140 ASP 141 -0.0059

ASP 141 MET 142 -0.0003

MET 142 VAL 143 0.0057

VAL 143 GLU 144 0.0004

GLU 144 THR 145 -0.0109

THR 145 LYS 146 -0.0002

LYS 146 ILE 147 0.0176

ILE 147 ALA 148 0.0003

ALA 148 GLN 149 -0.0255

GLN 149 PRO 150 -0.0003

PRO 150 ARG 151 -0.0227

ARG 151 ALA 152 -0.0000

ALA 152 GLY 153 -0.0045

GLY 153 ALA 154 -0.0004

ALA 154 SER 155 0.0009

SER 155 THR 156 -0.0002

THR 156 ALA 157 -0.0602

ALA 157 TRP 158 -0.0003

TRP 158 VAL 159 -0.0805

VAL 159 PRO 160 -0.0001

PRO 160 SER 161 0.0164

SER 161 PRO 162 0.0001

PRO 162 THR 163 0.0043

THR 163 ALA 164 -0.0004

ALA 164 ALA 165 -0.0108

ALA 165 THR 166 0.0000

THR 166 LEU 167 0.0002

LEU 167 HIS 168 -0.0001

HIS 168 ALA 169 0.0009

ALA 169 LEU 170 0.0000

LEU 170 HIS 171 -0.0029

HIS 171 TYR 172 0.0000

TYR 172 HIS 173 0.0012

HIS 173 GLN 174 -0.0002

GLN 174 VAL 175 0.0132

VAL 175 ASP 176 0.0001

ASP 176 VAL 177 0.0072

VAL 177 ALA 178 -0.0001

ALA 178 ALA 179 -0.0017

ALA 179 VAL 180 0.0002

VAL 180 GLN 181 0.0251

GLN 181 GLN 182 0.0003

GLN 182 GLY 183 -0.0237

GLY 183 LEU 184 -0.0001

LEU 184 ALA 185 0.0116

ALA 185 GLY 186 -0.0004

GLY 186 LYS 187 0.0094

LYS 187 ARG 188 -0.0003

ARG 188 ARG 189 0.0069

ARG 189 ALA 190 0.0002

ALA 190 THR 191 -0.0358

THR 191 ILE 192 0.0001

ILE 192 GLU 193 0.0264

GLU 193 GLN 194 -0.0002

GLN 194 LEU 195 0.0102

LEU 195 LEU 196 0.0003

LEU 196 THR 197 0.0880

THR 197 ILE 198 -0.0002

ILE 198 PRO 199 0.0835

PRO 199 LEU 200 0.0001

LEU 200 ALA 201 0.0378

ALA 201 LYS 202 0.0003

LYS 202 GLU 203 0.0032

GLU 203 LEU 204 0.0000

LEU 204 ALA 205 0.0235

ALA 205 TRP 206 0.0002

TRP 206 ALA 207 0.0071

ALA 207 PRO 208 -0.0002

PRO 208 ASP 209 -0.0012

ASP 209 GLU 210 0.0000

GLU 210 ILE 211 -0.0019

ILE 211 ARG 212 -0.0001

ARG 212 GLU 213 0.0080

GLU 213 GLU 214 -0.0001

GLU 214 VAL 215 0.0182

VAL 215 ASP 216 0.0002

ASP 216 ASN 217 0.0010

ASN 217 ASN 218 -0.0001

ASN 218 CYS 219 0.0162

CYS 219 GLN 220 -0.0001

GLN 220 SER 221 -0.0120

SER 221 ILE 222 -0.0001

ILE 222 LEU 223 -0.0066

LEU 223 GLY 224 -0.0003

GLY 224 TYR 225 -0.0234

TYR 225 VAL 226 0.0001

VAL 226 VAL 227 -0.0121

VAL 227 ARG 228 0.0001

ARG 228 TRP 229 -0.0197

TRP 229 VAL 230 -0.0002

VAL 230 ASP 231 -0.0221

ASP 231 GLN 232 -0.0003

GLN 232 GLY 233 -0.0022

GLY 233 VAL 234 -0.0001

VAL 234 GLY 235 -0.0182

GLY 235 CYS 236 0.0001

CYS 236 SER 237 -0.0052

SER 237 LYS 238 -0.0001

LYS 238 VAL 239 0.0044

VAL 239 PRO 240 0.0001

PRO 240 ASP 241 0.0078

ASP 241 ILE 242 -0.0002

ILE 242 HIS 243 0.0013

HIS 243 ASP 244 -0.0001

ASP 244 VAL 245 -0.0206

VAL 245 ALA 246 -0.0001

ALA 246 LEU 247 -0.0049

LEU 247 MET 248 0.0002

MET 248 GLU 249 0.0272

GLU 249 ASP 250 -0.0002

ASP 250 ARG 251 0.0104

ARG 251 ALA 252 -0.0004

ALA 252 THR 253 -0.0448

THR 253 LEU 254 -0.0001

LEU 254 ARG 255 -0.0202

ARG 255 ILE 256 0.0002

ILE 256 SER 257 -0.0202

SER 257 SER 258 -0.0000

SER 258 GLN 259 0.0041

GLN 259 LEU 260 -0.0004

LEU 260 LEU 261 0.0073

LEU 261 ALA 262 -0.0001

ALA 262 ASN 263 -0.0052

ASN 263 TRP 264 -0.0000

TRP 264 LEU 265 -0.0017

LEU 265 ARG 266 -0.0004

ARG 266 HIS 267 -0.0057

HIS 267 GLY 268 0.0000

GLY 268 VAL 269 -0.0014

VAL 269 ILE 270 0.0002

ILE 270 THR 271 -0.0018

THR 271 SER 272 0.0002

SER 272 ALA 273 0.0001

ALA 273 ASP 274 0.0002

ASP 274 VAL 275 -0.0043

VAL 275 ARG 276 -0.0001

ARG 276 ALA 277 -0.0014

ALA 277 SER 278 -0.0001

SER 278 LEU 279 0.0089

LEU 279 GLU 280 -0.0000

GLU 280 ARG 281 0.0095

ARG 281 MET 282 0.0001

MET 282 ALA 283 0.0177

ALA 283 PRO 284 -0.0001

PRO 284 LEU 285 -0.0203

LEU 285 VAL 286 -0.0000

VAL 286 ASP 287 0.0002

ASP 287 ARG 288 0.0001

ARG 288 GLN 289 -0.0052

GLN 289 ASN 290 0.0001

ASN 290 ALA 291 -0.0028

ALA 291 GLY 292 0.0003

GLY 292 ASP 293 -0.0046

ASP 293 VAL 294 0.0002

VAL 294 ALA 295 -0.0133

ALA 295 TYR 296 -0.0000

TYR 296 ARG 297 0.0056

ARG 297 PRO 298 -0.0002

PRO 298 MET 299 0.0027

MET 299 ALA 300 0.0002

ALA 300 PRO 301 -0.0001

PRO 301 ASN 302 -0.0000

ASN 302 PHE 303 0.0009

PHE 303 ASP 304 0.0000

ASP 304 ASP 305 0.0071

ASP 305 SER 306 0.0002

SER 306 ILE 307 -0.0083

ILE 307 ALA 308 0.0005

ALA 308 PHE 309 0.0098

PHE 309 LEU 310 0.0002

LEU 310 ALA 311 -0.0083

ALA 311 ALA 312 0.0003

ALA 312 GLN 313 0.0059

GLN 313 GLU 314 -0.0001

GLU 314 LEU 315 -0.0063

LEU 315 ILE 316 -0.0001

ILE 316 LEU 317 0.0033

LEU 317 SER 318 -0.0002

SER 318 GLY 319 -0.0057

GLY 319 ALA 320 -0.0001

ALA 320 GLN 321 -0.0063

GLN 321 GLN 322 -0.0005

GLN 322 PRO 323 0.0062

PRO 323 ASN 324 0.0003

ASN 324 GLY 325 -0.0035

GLY 325 TYR 326 -0.0000

TYR 326 THR 327 -0.0746

THR 327 GLU 328 -0.0001

GLU 328 PRO 329 0.0135

PRO 329 ILE 330 -0.0004

ILE 330 LEU 331 0.0015

LEU 331 HIS 332 -0.0002

HIS 332 ARG 333 0.0151

ARG 333 ARG 334 -0.0005

ARG 334 ARG 335 0.0033

ARG 335 ARG 336 0.0000

ARG 336 GLU 337 0.0092

GLU 337 PHE 338 0.0002

PHE 338 LYS 339 0.0012

LYS 339 ALA 340 0.0000

ALA 340 ARG 341 0.0116

ARG 341 ALA 342 0.0001

ALA 342 ALA 343 0.0184

ALA 343 GLU 344 0.0002

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 8 ---

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

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *