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

* *

CA strain for 230101190352136506

--- normal mode 31 ---

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
PHE 1 ASP 2 0.0001

ASP 2 MET 3 -0.1331

MET 3 ILE 4 0.0001

ILE 4 ARG 5 -0.0333

ARG 5 LEU 6 -0.0001

LEU 6 ALA 7 0.0341

ALA 7 THR 8 0.0000

THR 8 ASN 9 0.0246

ASN 9 LYS 10 0.0005

LYS 10 PHE 11 -0.0414

PHE 11 SER 12 -0.0003

SER 12 GLU 13 0.0670

GLU 13 ASP 14 -0.0001

ASP 14 ASN 15 -0.0352

ASN 15 LYS 16 -0.0001

LYS 16 ILE 17 -0.0421

ILE 17 GLY 18 -0.0002

GLY 18 GLU 19 -0.0846

GLU 19 GLY 20 0.0004

GLY 20 GLY 21 0.2242

GLY 21 PHE 22 0.0003

PHE 22 GLY 23 0.0237

GLY 23 ASP 24 0.0001

ASP 24 VAL 25 0.0962

VAL 25 TYR 26 -0.0002

TYR 26 LYS 27 0.0845

LYS 27 GLY 28 0.0003

GLY 28 MET 29 -0.0001

MET 29 PHE 30 -0.0002

PHE 30 PRO 31 0.0551

PRO 31 ASN 32 -0.0003

ASN 32 GLY 33 -0.0133

GLY 33 TYR 34 0.0002

TYR 34 GLU 35 0.0337

GLU 35 ILE 36 0.0001

ILE 36 ALA 37 0.0175

ALA 37 VAL 38 0.0004

VAL 38 LYS 39 0.1753

LYS 39 ARG 40 -0.0001

ARG 40 LEU 41 -0.0317

LEU 41 ILE 42 -0.0000

ILE 42 ARG 43 0.2070

ARG 43 ASN 44 -0.0001

ASN 44 SER 45 -0.0041

SER 45 SER 46 0.0002

SER 46 GLN 47 -0.0492

GLN 47 GLY 48 0.0002

GLY 48 ALA 49 -0.0670

ALA 49 VAL 50 -0.0001

VAL 50 GLU 51 0.0170

GLU 51 PHE 52 -0.0002

PHE 52 LYS 53 -0.0623

LYS 53 ASN 54 0.0000

ASN 54 GLU 55 0.0904

GLU 55 VAL 56 -0.0000

VAL 56 LEU 57 -0.1732

LEU 57 LEU 58 -0.0000

LEU 58 ILE 59 0.0631

ILE 59 ALA 60 0.0000

ALA 60 LYS 61 -0.1661

LYS 61 LEU 62 0.0001

LEU 62 GLN 63 0.0427

GLN 63 HIS 64 0.0001

HIS 64 ARG 65 -0.0052

ARG 65 ASN 66 -0.0001

ASN 66 LEU 67 -0.0404

LEU 67 VAL 68 0.0001

VAL 68 ARG 69 0.0616

ARG 69 LEU 70 0.0001

LEU 70 LEU 71 0.0659

LEU 71 GLY 72 -0.0002

GLY 72 PHE 73 -0.0849

PHE 73 CYS 74 0.0003

CYS 74 ILE 75 -0.0592

ILE 75 GLN 76 0.0001

GLN 76 ARG 77 -0.0309

ARG 77 ASN 78 -0.0002

ASN 78 GLU 79 0.0317

GLU 79 LYS 80 -0.0000

LYS 80 ILE 81 -0.0061

ILE 81 LEU 82 -0.0001

LEU 82 ILE 83 0.0548

ILE 83 TYR 84 -0.0003

TYR 84 GLU 85 0.1072

GLU 85 TYR 86 0.0004

TYR 86 MET 87 0.1145

MET 87 HIS 88 0.0002

HIS 88 ASN 89 0.1113

ASN 89 LYS 90 0.0002

LYS 90 SER 91 0.1335

SER 91 LEU 92 -0.0000

LEU 92 ASP 93 -0.0935

ASP 93 TYR 94 0.0000

TYR 94 TYR 95 0.0161

TYR 95 LEU 96 0.0003

LEU 96 PHE 97 -0.0720

PHE 97 SER 98 0.0001

SER 98 PRO 99 -0.0059

PRO 99 GLU 100 0.0001

GLU 100 ASN 101 -0.1032

ASN 101 HIS 102 -0.0001

HIS 102 ARG 103 0.0635

ARG 103 LYS 104 -0.0002

LYS 104 LEU 105 -0.0832

LEU 105 THR 106 0.0002

THR 106 TRP 107 -0.0565

TRP 107 HIS 108 -0.0002

HIS 108 ALA 109 0.1172

ALA 109 ARG 110 -0.0001

ARG 110 TYR 111 -0.2512

TYR 111 LYS 112 -0.0002

LYS 112 ILE 113 0.0300

ILE 113 ILE 114 0.0002

ILE 114 ARG 115 0.0150

ARG 115 GLY 116 -0.0002

GLY 116 ILE 117 -0.0402

ILE 117 ALA 118 0.0000

ALA 118 ARG 119 -0.0429

ARG 119 GLY 120 0.0006

GLY 120 ILE 121 0.0106

ILE 121 LEU 122 0.0002

LEU 122 TYR 123 -0.1264

TYR 123 LEU 124 -0.0001

LEU 124 HIS 125 -0.0275

HIS 125 GLU 126 0.0003

GLU 126 ASP 127 -0.0250

ASP 127 SER 128 -0.0000

SER 128 HIS 129 -0.0281

HIS 129 LEU 130 -0.0001

LEU 130 LYS 131 -0.0526

LYS 131 ILE 132 0.0003

ILE 132 ILE 133 0.0148

ILE 133 HIS 134 0.0001

HIS 134 CYS 135 0.1005

CYS 135 ASP 136 -0.0001

ASP 136 LEU 137 0.1631

LEU 137 LYS 138 -0.0002

LYS 138 PRO 139 0.1862

PRO 139 SER 140 -0.0001

SER 140 ASN 141 0.0206

ASN 141 ILE 142 -0.0004

ILE 142 LEU 143 0.1227

LEU 143 LEU 144 -0.0002

LEU 144 ASP 145 0.0582

ASP 145 ASP 146 0.0001

ASP 146 LYS 147 0.0612

LYS 147 MET 148 -0.0001

MET 148 ASN 149 -0.1062

ASN 149 ALA 150 -0.0003

ALA 150 LYS 151 0.0577

LYS 151 ILE 152 0.0000

ILE 152 SER 153 -0.0133

SER 153 ASP 154 0.0003

ASP 154 PHE 155 -0.0144

PHE 155 GLY 156 0.0001

GLY 156 LEU 157 0.1497

LEU 157 ALA 158 -0.0000

ALA 158 ARG 159 -0.0356

ARG 159 ILE 160 0.0003

ILE 160 VAL 161 -0.1870

VAL 161 ALA 162 0.0002

ALA 162 ILE 163 -0.0385

ILE 163 ASP 164 -0.0001

ASP 164 GLN 165 0.0222

GLN 165 MET 166 0.0000

MET 166 GLN 167 -0.0478

GLN 167 GLY 168 -0.0003

GLY 168 ASN 169 -0.0653

ASN 169 THR 170 -0.0001

THR 170 SER 171 0.0964

SER 171 ILE 172 -0.0003

ILE 172 ILE 173 0.1055

ILE 173 ALA 174 -0.0000

ALA 174 GLY 175 0.4317

GLY 175 THR 176 0.0003

THR 176 TYR 177 -0.1466

TYR 177 GLY 178 -0.0005

GLY 178 TYR 179 0.0163

TYR 179 MET 180 -0.0000

MET 180 SER 181 0.0559

SER 181 PRO 182 0.0001

PRO 182 GLU 183 -0.1429

GLU 183 TYR 184 -0.0001

TYR 184 ALA 185 0.0744

ALA 185 MET 186 -0.0001

MET 186 LEU 187 0.0916

LEU 187 GLY 188 0.0001

GLY 188 GLN 189 0.0099

GLN 189 PHE 190 0.0002

PHE 190 SER 191 0.0858

SER 191 VAL 192 0.0000

VAL 192 LYS 193 -0.0935

LYS 193 SER 194 -0.0002

SER 194 ASP 195 0.0405

ASP 195 VAL 196 0.0001

VAL 196 PHE 197 0.0361

PHE 197 SER 198 0.0003

SER 198 PHE 199 0.0372

PHE 199 GLY 200 -0.0000

GLY 200 VAL 201 0.0061

VAL 201 ILE 202 -0.0003

ILE 202 MET 203 0.0654

MET 203 LEU 204 -0.0001

LEU 204 GLU 205 0.0268

GLU 205 ILE 206 0.0003

ILE 206 VAL 207 0.0804

VAL 207 SER 208 0.0002

SER 208 GLY 209 -0.0350

GLY 209 LYS 210 0.0001

LYS 210 ARG 211 0.0876

ARG 211 ASN 212 -0.0000

ASN 212 VAL 213 -0.0334

VAL 213 ASP 214 0.0001

ASP 214 TYR 215 -0.1230

TYR 215 ASN 216 -0.0001

ASN 216 GLY 217 -0.3966

GLY 217 VAL 218 0.0000

VAL 218 ASN 219 -0.0194

ASN 219 SER 220 -0.0001

SER 220 ILE 221 0.3872

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 -0.0371

ASP 223 LEU 224 -0.0001

LEU 224 VAL 225 0.1511

VAL 225 SER 226 -0.0002

SER 226 HIS 227 -0.0371

HIS 227 ALA 228 -0.0003

ALA 228 TRP 229 0.0707

TRP 229 LYS 230 0.0003

LYS 230 LYS 231 -0.0320

LYS 231 TRP 232 0.0000

TRP 232 THR 233 0.0876

THR 233 GLU 234 -0.0003

GLU 234 ASN 235 -0.0174

ASN 235 LYS 236 -0.0002

LYS 236 GLN 237 0.0855

GLN 237 MET 238 -0.0001

MET 238 GLU 239 -0.0357

GLU 239 LEU 240 -0.0001

LEU 240 LEU 241 0.3807

LEU 241 ASP 242 0.0000

ASP 242 PRO 243 0.0467

PRO 243 ALA 244 0.0001

ALA 244 LEU 245 -0.0735

LEU 245 THR 246 0.0001

THR 246 TYR 247 0.1896

TYR 247 SER 248 0.0001

SER 248 PHE 249 -0.0706

PHE 249 SER 250 0.0001

SER 250 GLU 251 -0.0543

GLU 251 THR 252 -0.0003

THR 252 GLU 253 0.1826

GLU 253 VAL 254 -0.0002

VAL 254 SER 255 0.0677

SER 255 ARG 256 0.0001

ARG 256 CYS 257 -0.0269

CYS 257 ILE 258 0.0000

ILE 258 GLN 259 0.0293

GLN 259 LEU 260 -0.0001

LEU 260 GLY 261 0.0566

GLY 261 LEU 262 0.0001

LEU 262 LEU 263 0.0216

LEU 263 CYS 264 -0.0003

CYS 264 VAL 265 0.0336

VAL 265 GLN 266 -0.0000

GLN 266 GLU 267 -0.0830

GLU 267 ASN 268 -0.0000

ASN 268 PRO 269 -0.0756

PRO 269 ASP 270 0.0001

ASP 270 GLN 271 -0.0966

GLN 271 ARG 272 0.0003

ARG 272 PRO 273 -0.0041

PRO 273 THR 274 -0.0000

THR 274 MET 275 -0.1350

MET 275 ALA 276 -0.0001

ALA 276 THR 277 0.0003

THR 277 ILE 278 -0.0001

ILE 278 ALA 279 -0.0063

ALA 279 LEU 280 0.0003

LEU 280 TYR 281 0.0046

TYR 281 PHE 282 -0.0002

PHE 282 ASN 283 -0.0141

ASN 283 ILE 284 0.0003

ILE 284 ASP 285 -0.0186

ASP 285 SER 286 0.0002

SER 286 ILE 287 0.0021

ILE 287 ASP 288 0.0001

ASP 288 LEU 289 0.0365

LEU 289 PRO 290 0.0002

PRO 290 LEU 291 0.0513

LEU 291 PRO 292 0.0000

PRO 292 GLN 293 0.0149

GLN 293 GLN 294 0.0001

GLN 294 PRO 295 0.0403

PRO 295 PRO 296 0.0000

PRO 296 PHE 297 0.2527

PHE 297 TYR 298 -0.0002

TYR 298 MET 299 0.1467

MET 299 ARG 300 -0.0001

ARG 300 GLY 301 -0.1205

GLY 301 LYS 302 -0.0002

LYS 302 ILE 303 0.1381

ILE 303 GLU 304 0.0001

GLU 304 SER 305 0.1956

SER 305 LYS 306 0.0002

LYS 306 VAL 307 -0.1131

VAL 307 ALA 308 -0.0001

ALA 308 SER 309 0.0652

SER 309 LYS 310 0.0001

LYS 310 LYS 311 0.3416

LYS 311 THR 312 -0.0005

THR 312 MET 313 0.0256

MET 313 SER 314 0.0002

SER 314 GLY 315 -0.1285

GLY 315 ARG 316 -0.0001

ARG 316 PRO 317 -0.1605

PRO 317 ARG 318 0.0003

ARG 318 SER 319 -0.0282

SER 319 TYR 320 0.0001

TYR 320 SER 321 -0.0138

SER 321 VAL 322 0.0001

VAL 322 THR 323 -0.0773

THR 323 ARG 324 -0.0001

ARG 324 PHE 325 -0.2877

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: October 18th, 2018.

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

*** ***

CA strain for 230101190352136506

--- normal mode 31 ---

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

* *