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

* *

CA strain for 2401161745071321422

--- normal mode 10 ---

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
MET 1 GLU 2 0.0003

GLU 2 LEU 3 0.0115

LEU 3 ARG 4 0.0001

ARG 4 HIS 5 0.0023

HIS 5 THR 6 0.0005

THR 6 PRO 7 -0.0135

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 0.0195

ARG 9 ASP 10 0.0000

ASP 10 LEU 11 -0.0675

LEU 11 ASP 12 0.0002

ASP 12 LYS 13 0.0570

LYS 13 PHE 14 -0.0001

PHE 14 ILE 15 -0.0426

ILE 15 GLU 16 -0.0003

GLU 16 ASP 17 0.0695

ASP 17 HIS 18 0.0001

HIS 18 LEU 19 -0.0287

LEU 19 LEU 20 0.0002

LEU 20 PRO 21 -0.2137

PRO 21 ASN 22 0.0003

ASN 22 THR 23 0.0363

THR 23 CYS 24 -0.0003

CYS 24 PHE 25 0.0928

PHE 25 ARG 26 0.0000

ARG 26 THR 27 -0.0195

THR 27 GLN 28 0.0001

GLN 28 VAL 29 -0.0033

VAL 29 LYS 30 0.0005

LYS 30 GLU 31 0.0183

GLU 31 ALA 32 -0.0001

ALA 32 ILE 33 -0.0345

ILE 33 ASP 34 -0.0002

ASP 34 ILE 35 0.0398

ILE 35 VAL 36 -0.0002

VAL 36 CYS 37 -0.0604

CYS 37 ARG 38 0.0002

ARG 38 PHE 39 0.0233

PHE 39 LEU 40 0.0004

LEU 40 LYS 41 -0.0057

LYS 41 GLU 42 -0.0001

GLU 42 ARG 43 0.0259

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 -0.0355

PHE 45 GLN 46 0.0000

GLN 46 GLY 47 0.0201

GLY 47 THR 48 -0.0001

THR 48 ALA 49 -0.0529

ALA 49 ASP 50 0.0000

ASP 50 PRO 51 0.0036

PRO 51 VAL 52 0.0003

VAL 52 ARG 53 -0.0063

ARG 53 VAL 54 -0.0001

VAL 54 SER 55 0.1204

SER 55 LYS 56 -0.0001

LYS 56 VAL 57 -0.0722

VAL 57 VAL 58 -0.0002

VAL 58 LYS 59 -0.0827

LYS 59 GLY 60 0.0000

GLY 60 GLY 61 0.0113

GLY 61 SER 62 -0.0000

SER 62 SER 63 0.0423

SER 63 GLY 64 -0.0004

GLY 64 LYS 65 -0.0480

LYS 65 GLY 66 0.0002

GLY 66 THR 67 -0.0468

THR 67 THR 68 -0.0003

THR 68 LEU 69 -0.0759

LEU 69 ARG 70 -0.0001

ARG 70 GLY 71 -0.0224

GLY 71 ARG 72 -0.0001

ARG 72 SER 73 -0.0416

SER 73 ASP 74 -0.0001

ASP 74 ALA 75 0.0406

ALA 75 ASP 76 0.0003

ASP 76 LEU 77 0.0155

LEU 77 VAL 78 -0.0001

VAL 78 VAL 79 -0.0112

VAL 79 PHE 80 0.0000

PHE 80 LEU 81 0.0332

LEU 81 THR 82 0.0001

THR 82 LYS 83 -0.0381

LYS 83 LEU 84 -0.0001

LEU 84 THR 85 0.0509

THR 85 SER 86 0.0000

SER 86 PHE 87 0.0428

PHE 87 GLU 88 -0.0001

GLU 88 ASP 89 0.0369

ASP 89 GLN 90 0.0000

GLN 90 LEU 91 -0.0281

LEU 91 ARG 92 0.0003

ARG 92 ARG 93 0.0324

ARG 93 ARG 94 -0.0001

ARG 94 GLY 95 0.0146

GLY 95 GLU 96 0.0002

GLU 96 PHE 97 -0.0040

PHE 97 ILE 98 -0.0000

ILE 98 GLN 99 -0.0479

GLN 99 GLU 100 0.0002

GLU 100 ILE 101 -0.0323

ILE 101 ARG 102 0.0002

ARG 102 ARG 103 -0.0619

ARG 103 GLN 104 -0.0003

GLN 104 LEU 105 -0.0507

LEU 105 GLU 106 0.0003

GLU 106 ALA 107 -0.0173

ALA 107 CYS 108 -0.0002

CYS 108 GLN 109 -0.0525

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 -0.0071

GLU 111 GLN 112 -0.0000

GLN 112 LYS 113 -0.0310

LYS 113 PHE 114 0.0001

PHE 114 LYS 115 -0.0602

LYS 115 VAL 116 -0.0002

VAL 116 THR 117 0.0762

THR 117 PHE 118 0.0001

PHE 118 GLY 119 0.0749

GLY 119 GLY 120 -0.0001

GLY 120 GLY 121 -0.0119

GLY 121 PHE 122 0.0001

PHE 122 VAL 123 0.0673

VAL 123 LEU 124 0.0000

LEU 124 SER 125 0.0245

SER 125 SER 126 0.0000

SER 126 PRO 127 -0.0236

PRO 127 GLN 128 -0.0001

GLN 128 LEU 129 -0.0204

LEU 129 GLN 130 -0.0000

GLN 130 GLN 131 0.0679

GLN 131 GLU 132 -0.0001

GLU 132 VAL 133 0.0870

VAL 133 GLU 134 -0.0003

GLU 134 PHE 135 0.0673

PHE 135 ASP 136 -0.0002

ASP 136 VAL 137 0.0178

VAL 137 LEU 138 -0.0001

LEU 138 PRO 139 0.0631

PRO 139 ALA 140 0.0004

ALA 140 PHE 141 0.0868

PHE 141 ASP 142 0.0003

ASP 142 ALA 143 0.0996

ALA 143 LEU 144 -0.0003

LEU 144 GLY 145 0.0464

GLY 145 GLN 146 0.0002

GLN 146 TRP 147 0.0137

TRP 147 THR 148 -0.0002

THR 148 PRO 149 -0.0509

PRO 149 GLY 150 -0.0002

GLY 150 TYR 151 -0.1103

TYR 151 LYS 152 0.0001

LYS 152 PRO 153 -0.0193

PRO 153 ASN 154 -0.0000

ASN 154 PRO 155 -0.0082

PRO 155 GLU 156 0.0002

GLU 156 ILE 157 0.0382

ILE 157 TYR 158 0.0003

TYR 158 VAL 159 -0.0650

VAL 159 GLN 160 -0.0002

GLN 160 LEU 161 0.0133

LEU 161 ILE 162 0.0002

ILE 162 LYS 163 0.0552

LYS 163 GLU 164 0.0003

GLU 164 CYS 165 0.0495

CYS 165 LYS 166 -0.0000

LYS 166 SER 167 0.1018

SER 167 ARG 168 0.0003

ARG 168 GLY 169 0.0271

GLY 169 LYS 170 -0.0001

LYS 170 GLU 171 0.0900

GLU 171 GLY 172 -0.0001

GLY 172 GLU 173 0.0017

GLU 173 PHE 174 -0.0000

PHE 174 SER 175 0.0223

SER 175 THR 176 -0.0005

THR 176 CYS 177 0.0464

CYS 177 PHE 178 -0.0001

PHE 178 THR 179 -0.0794

THR 179 GLU 180 -0.0004

GLU 180 LEU 181 0.0175

LEU 181 GLN 182 -0.0004

GLN 182 ARG 183 -0.0230

ARG 183 ASP 184 -0.0001

ASP 184 PHE 185 0.0213

PHE 185 LEU 186 0.0003

LEU 186 ARG 187 0.0242

ARG 187 ASN 188 0.0002

ASN 188 ARG 189 -0.1244

ARG 189 PRO 190 0.0001

PRO 190 THR 191 -0.0481

THR 191 LYS 192 -0.0005

LYS 192 LEU 193 0.0292

LEU 193 LYS 194 -0.0003

LYS 194 SER 195 -0.0849

SER 195 LEU 196 0.0001

LEU 196 ILE 197 0.0170

ILE 197 ARG 198 0.0002

ARG 198 LEU 199 -0.0647

LEU 199 VAL 200 -0.0001

VAL 200 LYS 201 0.0300

LYS 201 HIS 202 0.0000

HIS 202 TRP 203 0.0493

TRP 203 TYR 204 -0.0002

TYR 204 GLN 205 0.0442

GLN 205 THR 206 -0.0000

THR 206 CYS 207 0.0641

CYS 207 LYS 208 0.0004

LYS 208 LYS 209 -0.0217

LYS 209 THR 210 0.0001

THR 210 HIS 211 0.0359

HIS 211 GLY 212 -0.0001

GLY 212 ASN 213 -0.0722

ASN 213 LYS 214 0.0002

LYS 214 LEU 215 0.0249

LEU 215 PRO 216 -0.0004

PRO 216 PRO 217 0.1008

PRO 217 GLN 218 0.0004

GLN 218 TYR 219 0.0305

TYR 219 ALA 220 0.0001

ALA 220 LEU 221 0.0689

LEU 221 GLU 222 -0.0001

GLU 222 LEU 223 -0.0383

LEU 223 LEU 224 -0.0000

LEU 224 THR 225 0.0013

THR 225 VAL 226 0.0001

VAL 226 TYR 227 -0.0428

TYR 227 ALA 228 0.0004

ALA 228 TRP 229 -0.0323

TRP 229 GLU 230 -0.0001

GLU 230 GLN 231 0.0241

GLN 231 GLY 232 0.0001

GLY 232 SER 233 -0.0192

SER 233 ARG 234 -0.0002

ARG 234 LYS 235 0.0534

LYS 235 THR 236 -0.0002

THR 236 ASP 237 -0.0232

ASP 237 PHE 238 0.0002

PHE 238 SER 239 0.0022

SER 239 THR 240 -0.0002

THR 240 ALA 241 -0.0581

ALA 241 GLN 242 -0.0003

GLN 242 GLY 243 0.0052

GLY 243 PHE 244 0.0001

PHE 244 GLN 245 -0.0330

GLN 245 THR 246 0.0002

THR 246 VAL 247 0.0272

VAL 247 LEU 248 -0.0001

LEU 248 GLU 249 -0.0046

GLU 249 LEU 250 -0.0001

LEU 250 VAL 251 -0.1013

VAL 251 LEU 252 -0.0002

LEU 252 LYS 253 0.1068

LYS 253 HIS 254 -0.0001

HIS 254 GLN 255 0.0262

GLN 255 LYS 256 0.0003

LYS 256 LEU 257 -0.1014

LEU 257 CYS 258 -0.0001

CYS 258 ILE 259 -0.0735

ILE 259 PHE 260 -0.0001

PHE 260 TRP 261 -0.0057

TRP 261 GLU 262 -0.0000

GLU 262 ALA 263 0.0256

ALA 263 TYR 264 -0.0002

TYR 264 TYR 265 -0.1231

TYR 265 ASP 266 0.0004

ASP 266 PHE 267 -0.0251

PHE 267 THR 268 0.0001

THR 268 ASN 269 -0.0072

ASN 269 PRO 270 -0.0001

PRO 270 VAL 271 -0.0154

VAL 271 VAL 272 -0.0002

VAL 272 GLY 273 0.0093

GLY 273 ARG 274 -0.0002

ARG 274 CYS 275 0.0088

CYS 275 MET 276 0.0004

MET 276 LEU 277 -0.0141

LEU 277 GLN 278 -0.0000

GLN 278 GLN 279 0.0305

GLN 279 LEU 280 -0.0002

LEU 280 LYS 281 -0.0806

LYS 281 LYS 282 0.0001

LYS 282 PRO 283 0.2361

PRO 283 ARG 284 -0.0002

ARG 284 PRO 285 -0.0240

PRO 285 VAL 286 0.0000

VAL 286 ILE 287 -0.0237

ILE 287 LEU 288 -0.0000

LEU 288 ASP 289 -0.0321

ASP 289 PRO 290 0.0002

PRO 290 ALA 291 0.0260

ALA 291 ASP 292 -0.0002

ASP 292 PRO 293 -0.0575

PRO 293 THR 294 -0.0002

THR 294 GLY 295 0.1998

GLY 295 ASN 296 -0.0002

ASN 296 VAL 297 0.0474

VAL 297 GLY 298 -0.0001

GLY 298 GLY 299 -0.0380

GLY 299 GLY 300 -0.0001

GLY 300 ASP 301 0.1116

ASP 301 THR 302 -0.0001

THR 302 HIS 303 0.0275

HIS 303 SER 304 0.0001

SER 304 TRP 305 -0.0308

TRP 305 GLN 306 -0.0002

GLN 306 ARG 307 0.0396

ARG 307 LEU 308 0.0002

LEU 308 ALA 309 -0.0277

ALA 309 GLN 310 -0.0002

GLN 310 GLU 311 0.0496

GLU 311 ALA 312 -0.0001

ALA 312 ARG 313 -0.0149

ARG 313 VAL 314 -0.0000

VAL 314 TRP 315 -0.0130

TRP 315 LEU 316 -0.0004

LEU 316 GLY 317 0.0374

GLY 317 TYR 318 -0.0001

TYR 318 PRO 319 0.0239

PRO 319 CYS 320 -0.0001

CYS 320 CYS 321 -0.0026

CYS 321 LYS 322 -0.0000

LYS 322 ASN 323 0.0692

ASN 323 LEU 324 -0.0001

LEU 324 ASP 325 -0.0910

ASP 325 GLY 326 -0.0000

GLY 326 SER 327 0.0374

SER 327 LEU 328 0.0003

LEU 328 VAL 329 -0.0757

VAL 329 GLY 330 -0.0000

GLY 330 ALA 331 0.0764

ALA 331 TRP 332 0.0001

TRP 332 THR 333 -0.0360

THR 333 MET 334 -0.0003

MET 334 LEU 335 -0.1678

LEU 335 GLN 336 0.0000

GLN 336 LYS 337 0.1076

LYS 337 ILE 338 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.

*** ***

CA strain for 2401161745071321422

--- normal mode 10 ---

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

* *