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

* *

CA strain for 230101190352136506

--- normal mode 29 ---

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 0.0004

ASP 2 MET 3 0.0209

MET 3 ILE 4 -0.0003

ILE 4 ARG 5 0.0389

ARG 5 LEU 6 -0.0001

LEU 6 ALA 7 0.0011

ALA 7 THR 8 -0.0000

THR 8 ASN 9 0.0358

ASN 9 LYS 10 0.0001

LYS 10 PHE 11 0.0231

PHE 11 SER 12 0.0003

SER 12 GLU 13 -0.0690

GLU 13 ASP 14 0.0001

ASP 14 ASN 15 0.0357

ASN 15 LYS 16 0.0003

LYS 16 ILE 17 0.0966

ILE 17 GLY 18 0.0001

GLY 18 GLU 19 0.1767

GLU 19 GLY 20 -0.0001

GLY 20 GLY 21 -0.1747

GLY 21 PHE 22 0.0001

PHE 22 GLY 23 0.0430

GLY 23 ASP 24 -0.0001

ASP 24 VAL 25 -0.0752

VAL 25 TYR 26 -0.0001

TYR 26 LYS 27 -0.1241

LYS 27 GLY 28 -0.0002

GLY 28 MET 29 -0.1002

MET 29 PHE 30 0.0001

PHE 30 PRO 31 0.0018

PRO 31 ASN 32 -0.0000

ASN 32 GLY 33 -0.1403

GLY 33 TYR 34 -0.0000

TYR 34 GLU 35 -0.0908

GLU 35 ILE 36 -0.0001

ILE 36 ALA 37 -0.0222

ALA 37 VAL 38 -0.0003

VAL 38 LYS 39 -0.1189

LYS 39 ARG 40 -0.0001

ARG 40 LEU 41 0.0437

LEU 41 ILE 42 -0.0001

ILE 42 ARG 43 -0.1110

ARG 43 ASN 44 0.0001

ASN 44 SER 45 0.0776

SER 45 SER 46 -0.0003

SER 46 GLN 47 0.0103

GLN 47 GLY 48 -0.0000

GLY 48 ALA 49 -0.0473

ALA 49 VAL 50 -0.0001

VAL 50 GLU 51 -0.0532

GLU 51 PHE 52 -0.0001

PHE 52 LYS 53 0.0744

LYS 53 ASN 54 0.0003

ASN 54 GLU 55 0.0269

GLU 55 VAL 56 -0.0001

VAL 56 LEU 57 0.3092

LEU 57 LEU 58 -0.0004

LEU 58 ILE 59 0.1911

ILE 59 ALA 60 -0.0001

ALA 60 LYS 61 0.2244

LYS 61 LEU 62 0.0003

LEU 62 GLN 63 0.0789

GLN 63 HIS 64 0.0001

HIS 64 ARG 65 0.0411

ARG 65 ASN 66 0.0001

ASN 66 LEU 67 0.0371

LEU 67 VAL 68 0.0004

VAL 68 ARG 69 -0.0721

ARG 69 LEU 70 0.0000

LEU 70 LEU 71 0.1239

LEU 71 GLY 72 0.0000

GLY 72 PHE 73 -0.0941

PHE 73 CYS 74 0.0001

CYS 74 ILE 75 -0.0261

ILE 75 GLN 76 -0.0005

GLN 76 ARG 77 0.0188

ARG 77 ASN 78 0.0001

ASN 78 GLU 79 -0.0428

GLU 79 LYS 80 0.0004

LYS 80 ILE 81 -0.0294

ILE 81 LEU 82 -0.0001

LEU 82 ILE 83 -0.0267

ILE 83 TYR 84 0.0003

TYR 84 GLU 85 -0.0948

GLU 85 TYR 86 -0.0000

TYR 86 MET 87 -0.0767

MET 87 HIS 88 0.0001

HIS 88 ASN 89 -0.0918

ASN 89 LYS 90 -0.0000

LYS 90 SER 91 -0.0337

SER 91 LEU 92 0.0005

LEU 92 ASP 93 0.0617

ASP 93 TYR 94 -0.0002

TYR 94 TYR 95 0.0009

TYR 95 LEU 96 -0.0002

LEU 96 PHE 97 0.0176

PHE 97 SER 98 0.0001

SER 98 PRO 99 -0.1274

PRO 99 GLU 100 0.0001

GLU 100 ASN 101 -0.0254

ASN 101 HIS 102 0.0001

HIS 102 ARG 103 -0.0866

ARG 103 LYS 104 0.0000

LYS 104 LEU 105 0.0012

LEU 105 THR 106 0.0000

THR 106 TRP 107 0.0526

TRP 107 HIS 108 -0.0002

HIS 108 ALA 109 0.0472

ALA 109 ARG 110 -0.0002

ARG 110 TYR 111 -0.0182

TYR 111 LYS 112 0.0002

LYS 112 ILE 113 0.0069

ILE 113 ILE 114 0.0006

ILE 114 ARG 115 0.0331

ARG 115 GLY 116 -0.0000

GLY 116 ILE 117 0.0752

ILE 117 ALA 118 -0.0001

ALA 118 ARG 119 0.0888

ARG 119 GLY 120 -0.0001

GLY 120 ILE 121 0.0229

ILE 121 LEU 122 -0.0000

LEU 122 TYR 123 0.0603

TYR 123 LEU 124 0.0003

LEU 124 HIS 125 -0.0826

HIS 125 GLU 126 -0.0002

GLU 126 ASP 127 -0.0371

ASP 127 SER 128 -0.0000

SER 128 HIS 129 0.1197

HIS 129 LEU 130 -0.0000

LEU 130 LYS 131 0.0442

LYS 131 ILE 132 0.0001

ILE 132 ILE 133 -0.0654

ILE 133 HIS 134 -0.0001

HIS 134 CYS 135 0.0588

CYS 135 ASP 136 0.0002

ASP 136 LEU 137 0.0086

LEU 137 LYS 138 0.0003

LYS 138 PRO 139 -0.1254

PRO 139 SER 140 -0.0003

SER 140 ASN 141 -0.0280

ASN 141 ILE 142 -0.0002

ILE 142 LEU 143 -0.0233

LEU 143 LEU 144 -0.0001

LEU 144 ASP 145 0.0008

ASP 145 ASP 146 -0.0002

ASP 146 LYS 147 0.0335

LYS 147 MET 148 0.0002

MET 148 ASN 149 -0.0499

ASN 149 ALA 150 0.0005

ALA 150 LYS 151 0.0489

LYS 151 ILE 152 -0.0001

ILE 152 SER 153 0.0428

SER 153 ASP 154 -0.0004

ASP 154 PHE 155 0.0175

PHE 155 GLY 156 0.0003

GLY 156 LEU 157 -0.0169

LEU 157 ALA 158 -0.0002

ALA 158 ARG 159 0.2360

ARG 159 ILE 160 -0.0002

ILE 160 VAL 161 0.6299

VAL 161 ALA 162 -0.0001

ALA 162 ILE 163 0.0325

ILE 163 ASP 164 0.0002

ASP 164 GLN 165 -0.0434

GLN 165 MET 166 0.0002

MET 166 GLN 167 0.2234

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 0.5005

ASN 169 THR 170 0.0001

THR 170 SER 171 0.3375

SER 171 ILE 172 0.0002

ILE 172 ILE 173 -0.0444

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 0.0159

GLY 175 THR 176 -0.0002

THR 176 TYR 177 0.1260

TYR 177 GLY 178 -0.0001

GLY 178 TYR 179 0.0409

TYR 179 MET 180 0.0000

MET 180 SER 181 -0.0239

SER 181 PRO 182 0.0002

PRO 182 GLU 183 -0.2316

GLU 183 TYR 184 0.0002

TYR 184 ALA 185 0.1444

ALA 185 MET 186 0.0000

MET 186 LEU 187 0.0070

LEU 187 GLY 188 -0.0003

GLY 188 GLN 189 0.0665

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 0.1360

SER 191 VAL 192 -0.0002

VAL 192 LYS 193 -0.3828

LYS 193 SER 194 -0.0002

SER 194 ASP 195 0.1009

ASP 195 VAL 196 -0.0003

VAL 196 PHE 197 0.0428

PHE 197 SER 198 0.0000

SER 198 PHE 199 0.1453

PHE 199 GLY 200 -0.0000

GLY 200 VAL 201 0.0483

VAL 201 ILE 202 0.0005

ILE 202 MET 203 0.0593

MET 203 LEU 204 0.0000

LEU 204 GLU 205 0.0620

GLU 205 ILE 206 0.0003

ILE 206 VAL 207 0.0455

VAL 207 SER 208 -0.0001

SER 208 GLY 209 0.0982

GLY 209 LYS 210 -0.0002

LYS 210 ARG 211 -0.0881

ARG 211 ASN 212 0.0001

ASN 212 VAL 213 -0.0160

VAL 213 ASP 214 -0.0000

ASP 214 TYR 215 0.0410

TYR 215 ASN 216 -0.0002

ASN 216 GLY 217 0.1639

GLY 217 VAL 218 -0.0002

VAL 218 ASN 219 0.0053

ASN 219 SER 220 -0.0001

SER 220 ILE 221 -0.2432

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 0.0158

ASP 223 LEU 224 0.0002

LEU 224 VAL 225 0.0265

VAL 225 SER 226 -0.0000

SER 226 HIS 227 -0.0782

HIS 227 ALA 228 0.0001

ALA 228 TRP 229 0.0619

TRP 229 LYS 230 -0.0000

LYS 230 LYS 231 -0.0354

LYS 231 TRP 232 0.0004

TRP 232 THR 233 0.0048

THR 233 GLU 234 -0.0001

GLU 234 ASN 235 0.0310

ASN 235 LYS 236 -0.0002

LYS 236 GLN 237 0.0066

GLN 237 MET 238 0.0001

MET 238 GLU 239 -0.1598

GLU 239 LEU 240 0.0000

LEU 240 LEU 241 0.1874

LEU 241 ASP 242 0.0002

ASP 242 PRO 243 -0.0241

PRO 243 ALA 244 -0.0001

ALA 244 LEU 245 0.0610

LEU 245 THR 246 0.0002

THR 246 TYR 247 0.0941

TYR 247 SER 248 -0.0000

SER 248 PHE 249 0.0831

PHE 249 SER 250 -0.0002

SER 250 GLU 251 -0.0332

GLU 251 THR 252 0.0001

THR 252 GLU 253 0.0315

GLU 253 VAL 254 0.0004

VAL 254 SER 255 0.0615

SER 255 ARG 256 -0.0001

ARG 256 CYS 257 0.0217

CYS 257 ILE 258 0.0000

ILE 258 GLN 259 0.0482

GLN 259 LEU 260 -0.0001

LEU 260 GLY 261 0.0393

GLY 261 LEU 262 -0.0002

LEU 262 LEU 263 -0.1015

LEU 263 CYS 264 0.0002

CYS 264 VAL 265 0.0110

VAL 265 GLN 266 -0.0004

GLN 266 GLU 267 0.0721

GLU 267 ASN 268 -0.0000

ASN 268 PRO 269 -0.1901

PRO 269 ASP 270 0.0000

ASP 270 GLN 271 -0.0111

GLN 271 ARG 272 -0.0003

ARG 272 PRO 273 0.1527

PRO 273 THR 274 -0.0001

THR 274 MET 275 0.0005

MET 275 ALA 276 0.0003

ALA 276 THR 277 -0.1029

THR 277 ILE 278 0.0000

ILE 278 ALA 279 0.0866

ALA 279 LEU 280 0.0003

LEU 280 TYR 281 -0.0499

TYR 281 PHE 282 0.0003

PHE 282 ASN 283 0.0119

ASN 283 ILE 284 -0.0002

ILE 284 ASP 285 -0.0136

ASP 285 SER 286 0.0003

SER 286 ILE 287 0.0268

ILE 287 ASP 288 -0.0000

ASP 288 LEU 289 0.0449

LEU 289 PRO 290 -0.0001

PRO 290 LEU 291 -0.0615

LEU 291 PRO 292 -0.0003

PRO 292 GLN 293 0.1070

GLN 293 GLN 294 0.0000

GLN 294 PRO 295 0.0438

PRO 295 PRO 296 0.0001

PRO 296 PHE 297 -0.0078

PHE 297 TYR 298 0.0000

TYR 298 MET 299 -0.0500

MET 299 ARG 300 0.0001

ARG 300 GLY 301 -0.0242

GLY 301 LYS 302 0.0002

LYS 302 ILE 303 0.1387

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 0.1003

SER 305 LYS 306 0.0000

LYS 306 VAL 307 0.0342

VAL 307 ALA 308 0.0004

ALA 308 SER 309 -0.0379

SER 309 LYS 310 -0.0000

LYS 310 LYS 311 0.0038

LYS 311 THR 312 0.0001

THR 312 MET 313 0.2915

MET 313 SER 314 0.0002

SER 314 GLY 315 0.3369

GLY 315 ARG 316 -0.0002

ARG 316 PRO 317 -0.0113

PRO 317 ARG 318 -0.0001

ARG 318 SER 319 -0.1368

SER 319 TYR 320 -0.0001

TYR 320 SER 321 0.0328

SER 321 VAL 322 -0.0002

VAL 322 THR 323 -0.0193

THR 323 ARG 324 -0.0000

ARG 324 PHE 325 0.0747

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 29 ---

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

* *