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 11 ---

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 0.1718

THR 3 ILE 4 -0.0000

ILE 4 ILE 5 -0.1245

ILE 5 ARG 6 0.0000

ARG 6 ALA 7 -0.4171

ALA 7 ARG 8 0.0000

ARG 8 ALA 9 -0.2184

ALA 9 PRO 10 0.0002

PRO 10 LEU 11 -0.0288

LEU 11 ARG 12 -0.0001

ARG 12 LEU 13 0.0512

LEU 13 GLY 14 0.0001

GLY 14 LEU 15 -0.0345

LEU 15 ALA 16 -0.0002

ALA 16 GLY 17 0.0142

GLY 17 GLY 18 -0.0003

GLY 18 GLY 19 0.0239

GLY 19 THR 20 -0.0002

THR 20 ASP 21 -0.0579

ASP 21 VAL 22 0.0003

VAL 22 ALA 23 -0.0351

ALA 23 PRO 24 -0.0004

PRO 24 TYR 25 0.0259

TYR 25 ALA 26 0.0003

ALA 26 ASP 27 -0.0130

ASP 27 THR 28 0.0001

THR 28 PHE 29 -0.0345

PHE 29 GLY 30 0.0001

GLY 30 GLY 31 0.0252

GLY 31 TYR 32 -0.0000

TYR 32 VAL 33 -0.0113

VAL 33 LEU 34 -0.0000

LEU 34 ASN 35 -0.0695

ASN 35 ALA 36 0.0002

ALA 36 THR 37 -0.0766

THR 37 ILE 38 -0.0003

ILE 38 ASP 39 -0.0538

ASP 39 ARG 40 0.0002

ARG 40 TYR 41 0.2480

TYR 41 ALA 42 -0.0003

ALA 42 TYR 43 -0.1035

TYR 43 ALA 44 0.0000

ALA 44 VAL 45 -0.2907

VAL 45 ILE 46 -0.0001

ILE 46 LYS 47 -0.1303

LYS 47 THR 48 0.0001

THR 48 LEU 49 -0.1931

LEU 49 THR 50 0.0000

THR 50 ILE 51 0.0262

ILE 51 PRO 52 -0.0001

PRO 52 ALA 53 -0.0368

ALA 53 VAL 54 -0.0002

VAL 54 ARG 55 -0.0475

ARG 55 PHE 56 -0.0002

PHE 56 VAL 57 -0.0525

VAL 57 SER 58 0.0004

SER 58 THR 59 0.0571

THR 59 ASP 60 -0.0002

ASP 60 GLN 61 0.0118

GLN 61 GLN 62 -0.0000

GLN 62 VAL 63 -0.0113

VAL 63 GLU 64 0.0001

GLU 64 LYS 65 -0.0460

LYS 65 HIS 66 0.0002

HIS 66 GLN 67 -0.0677

GLN 67 LEU 68 -0.0001

LEU 68 ILE 69 -0.0462

ILE 69 SER 70 0.0001

SER 70 GLU 71 -0.0270

GLU 71 PRO 72 0.0000

PRO 72 LEU 73 -0.1055

LEU 73 GLU 74 -0.0000

GLU 74 LEU 75 0.1042

LEU 75 ASN 76 0.0002

ASN 76 GLY 77 -0.0067

GLY 77 THR 78 -0.0002

THR 78 LEU 79 0.0002

LEU 79 ASN 80 -0.0002

ASN 80 LEU 81 0.0696

LEU 81 HIS 82 -0.0005

HIS 82 LYS 83 0.0223

LYS 83 ALA 84 -0.0001

ALA 84 VAL 85 0.0256

VAL 85 TYR 86 -0.0001

TYR 86 ASN 87 0.0911

ASN 87 HIS 88 -0.0005

HIS 88 MET 89 0.0208

MET 89 ILE 90 -0.0001

ILE 90 ARG 91 0.0388

ARG 91 ASN 92 0.0001

ASN 92 TYR 93 0.0587

TYR 93 ASN 94 0.0002

ASN 94 HIS 95 0.1000

HIS 95 GLY 96 -0.0001

GLY 96 LYS 97 0.0059

LYS 97 PRO 98 -0.0002

PRO 98 ILE 99 0.0944

ILE 99 ALA 100 -0.0004

ALA 100 LEU 101 -0.0772

LEU 101 GLU 102 0.0000

GLU 102 LEU 103 -0.0568

LEU 103 SER 104 -0.0002

SER 104 THR 105 -0.2017

THR 105 PHE 106 0.0002

PHE 106 CYS 107 -0.0972

CYS 107 ASP 108 -0.0000

ASP 108 ALA 109 -0.0109

ALA 109 PRO 110 0.0000

PRO 110 ALA 111 -0.0255

ALA 111 GLY 112 -0.0002

GLY 112 SER 113 -0.0188

SER 113 GLY 114 0.0002

GLY 114 LEU 115 -0.1001

LEU 115 GLY 116 -0.0003

GLY 116 SER 117 -0.0320

SER 117 SER 118 0.0002

SER 118 SER 119 0.0935

SER 119 THR 120 -0.0001

THR 120 LEU 121 -0.0882

LEU 121 VAL 122 0.0001

VAL 122 VAL 123 0.0095

VAL 123 VAL 124 0.0002

VAL 124 MET 125 0.0550

MET 125 ILE 126 0.0002

ILE 126 LYS 127 -0.0131

LYS 127 ALA 128 -0.0002

ALA 128 PHE 129 0.0016

PHE 129 VAL 130 -0.0006

VAL 130 GLU 131 0.0509

GLU 131 LEU 132 -0.0001

LEU 132 LEU 133 0.1867

LEU 133 ASN 134 0.0001

ASN 134 LEU 135 0.1274

LEU 135 PRO 136 0.0003

PRO 136 LEU 137 0.0071

LEU 137 ASP 138 0.0001

ASP 138 ASP 139 0.1956

ASP 139 TYR 140 0.0000

TYR 140 ALA 141 0.1889

ALA 141 ILE 142 0.0004

ILE 142 ALA 143 -0.0226

ALA 143 GLN 144 -0.0003

GLN 144 LEU 145 0.1728

LEU 145 ALA 146 -0.0002

ALA 146 TYR 147 -0.0590

TYR 147 ARG 148 0.0002

ARG 148 ILE 149 0.0846

ILE 149 GLU 150 -0.0001

GLU 150 ARG 151 -0.0205

ARG 151 VAL 152 0.0003

VAL 152 ASP 153 0.1045

ASP 153 CYS 154 0.0003

CYS 154 GLY 155 0.0093

GLY 155 LEU 156 -0.0001

LEU 156 ALA 157 -0.1838

ALA 157 GLY 158 0.0002

GLY 158 GLY 159 0.0488

GLY 159 ARG 160 0.0003

ARG 160 GLN 161 0.0604

GLN 161 ASP 162 0.0002

ASP 162 GLN 163 0.0993

GLN 163 TYR 164 -0.0003

TYR 164 SER 165 0.1376

SER 165 ALA 166 0.0002

ALA 166 THR 167 0.0971

THR 167 PHE 168 -0.0001

PHE 168 GLY 169 0.2248

GLY 169 GLY 170 0.0001

GLY 170 PHE 171 -0.0607

PHE 171 ASN 172 0.0004

ASN 172 PHE 173 -0.0498

PHE 173 MET 174 -0.0004

MET 174 GLU 175 0.0178

GLU 175 PHE 176 -0.0001

PHE 176 TYR 177 0.0250

TYR 177 GLU 178 -0.0001

GLU 178 GLU 179 -0.0375

GLU 179 GLU 180 -0.0003

GLU 180 ARG 181 0.0874

ARG 181 THR 182 -0.0005

THR 182 ILE 183 0.0546

ILE 183 VAL 184 -0.0001

VAL 184 ASN 185 0.0390

ASN 185 PRO 186 0.0003

PRO 186 LEU 187 0.0156

LEU 187 ARG 188 -0.0001

ARG 188 ILE 189 0.0703

ILE 189 LYS 190 0.0001

LYS 190 ASN 191 0.0633

ASN 191 TRP 192 0.0002

TRP 192 VAL 193 0.0290

VAL 193 LEU 194 0.0001

LEU 194 CYS 195 0.1080

CYS 195 GLU 196 0.0001

GLU 196 LEU 197 0.0053

LEU 197 GLU 198 -0.0002

GLU 198 ALA 199 0.2140

ALA 199 SER 200 0.0004

SER 200 LEU 201 -0.0270

LEU 201 VAL 202 -0.0002

VAL 202 LEU 203 -0.0125

LEU 203 PHE 204 0.0003

PHE 204 TYR 205 -0.0939

TYR 205 THR 206 -0.0003

THR 206 GLY 207 -0.0460

GLY 207 VAL 208 0.0001

VAL 208 SER 209 0.1112

SER 209 ARG 210 -0.0001

ARG 210 GLU 211 -0.0679

GLU 211 SER 212 0.0004

SER 212 ALA 213 -0.0535

ALA 213 LYS 214 -0.0003

LYS 214 ILE 215 0.0348

ILE 215 ILE 216 0.0000

ILE 216 GLN 217 -0.0216

GLN 217 ASP 218 -0.0003

ASP 218 GLN 219 0.0347

GLN 219 SER 220 -0.0000

SER 220 ASP 221 -0.0190

ASP 221 ASN 222 0.0000

ASN 222 VAL 223 -0.0300

VAL 223 VAL 224 0.0001

VAL 224 SER 225 0.0031

SER 225 HIS 226 0.0002

HIS 226 LYS 227 -0.0233

LYS 227 THR 228 -0.0002

THR 228 ALA 229 -0.0682

ALA 229 ALA 230 0.0001

ALA 230 ILE 231 -0.0548

ILE 231 GLU 232 -0.0000

GLU 232 ALA 233 -0.0808

ALA 233 MET 234 -0.0001

MET 234 HIS 235 0.0256

HIS 235 GLY 236 -0.0000

GLY 236 ILE 237 -0.0217

ILE 237 LYS 238 -0.0004

LYS 238 ARG 239 -0.0458

ARG 239 GLU 240 0.0003

GLU 240 ALA 241 -0.0405

ALA 241 LEU 242 0.0002

LEU 242 VAL 243 -0.1075

VAL 243 MET 244 0.0004

MET 244 LYS 245 -0.0053

LYS 245 GLU 246 0.0004

GLU 246 ALA 247 -0.0961

ALA 247 LEU 248 -0.0001

LEU 248 LEU 249 -0.0274

LEU 249 LYS 250 0.0002

LYS 250 GLY 251 -0.0281

GLY 251 ASP 252 -0.0001

ASP 252 PHE 253 -0.0698

PHE 253 LYS 254 -0.0001

LYS 254 ALA 255 -0.0267

ALA 255 PHE 256 0.0001

PHE 256 VAL 257 -0.0360

VAL 257 ALA 258 -0.0001

ALA 258 SER 259 -0.0889

SER 259 MET 260 0.0000

MET 260 ARG 261 0.0233

ARG 261 LEU 262 0.0001

LEU 262 GLY 263 -0.0577

GLY 263 TRP 264 0.0002

TRP 264 ASP 265 -0.0155

ASP 265 ASN 266 -0.0000

ASN 266 LYS 267 0.0259

LYS 267 LYS 268 0.0000

LYS 268 ASN 269 -0.1689

ASN 269 SER 270 0.0002

SER 270 ALA 271 0.0355

ALA 271 ARG 272 0.0003

ARG 272 THR 273 -0.1112

THR 273 VAL 274 0.0001

VAL 274 SER 275 -0.0857

SER 275 ASN 276 0.0001

ASN 276 ALA 277 -0.0351

ALA 277 HIS 278 0.0001

HIS 278 ILE 279 0.0135

ILE 279 ASP 280 0.0004

ASP 280 GLU 281 -0.0832

GLU 281 ILE 282 0.0003

ILE 282 TYR 283 -0.0400

TYR 283 ASP 284 -0.0001

ASP 284 ALA 285 -0.0758

ALA 285 ALA 286 -0.0003

ALA 286 ILE 287 -0.0045

ILE 287 ARG 288 -0.0002

ARG 288 ALA 289 0.0362

ALA 289 GLY 290 0.0003

GLY 290 ALA 291 -0.0426

ALA 291 GLN 292 0.0001

GLN 292 ALA 293 -0.0210

ALA 293 GLY 294 0.0000

GLY 294 LYS 295 0.0215

LYS 295 VAL 296 -0.0003

VAL 296 SER 297 -0.0034

SER 297 GLY 298 0.0001

GLY 298 ALA 299 -0.0840

ALA 299 GLY 300 0.0002

GLY 300 GLY 301 0.0390

GLY 301 GLY 302 -0.0000

GLY 302 GLY 303 -0.0974

GLY 303 PHE 304 0.0001

PHE 304 MET 305 0.0612

MET 305 LEU 306 -0.0002

LEU 306 PHE 307 0.0455

PHE 307 PHE 308 0.0000

PHE 308 VAL 309 -0.0607

VAL 309 PRO 310 -0.0004

PRO 310 THR 311 -0.0084

THR 311 GLU 312 -0.0001

GLU 312 LYS 313 0.0042

LYS 313 ARG 314 -0.0004

ARG 314 MET 315 0.0346

MET 315 ASP 316 0.0002

ASP 316 LEU 317 -0.0066

LEU 317 ILE 318 0.0002

ILE 318 ARG 319 0.1056

ARG 319 THR 320 0.0001

THR 320 LEU 321 0.0776

LEU 321 GLY 322 0.0002

GLY 322 GLU 323 0.0065

GLU 323 TYR 324 0.0005

TYR 324 ASP 325 0.0139

ASP 325 GLY 326 0.0001

GLY 326 GLN 327 0.0073

GLN 327 VAL 328 0.0001

VAL 328 SER 329 0.1279

SER 329 ASN 330 -0.0000

ASN 330 CYS 331 0.1258

CYS 331 HIS 332 -0.0002

HIS 332 PHE 333 0.2455

PHE 333 THR 334 0.0000

THR 334 LYS 335 0.0491

LYS 335 ASN 336 0.0001

ASN 336 GLY 337 0.1261

GLY 337 THR 338 0.0002

THR 338 GLN 339 -0.1854

GLN 339 ALA 340 0.0004

ALA 340 TRP 341 -0.0006

TRP 341 ARG 342 -0.0001

ARG 342 ILE 343 0.0586

ILE 343 ALA 344 0.0002

ALA 344 ASN 345 0.1460

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 11 ---

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

* EXP_4USM_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *