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

* *

CA strain for 230101190352136506

--- normal mode 27 ---

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 -0.0027

MET 3 ILE 4 -0.0003

ILE 4 ARG 5 -0.0359

ARG 5 LEU 6 -0.0004

LEU 6 ALA 7 -0.0952

ALA 7 THR 8 -0.0003

THR 8 ASN 9 -0.1059

ASN 9 LYS 10 0.0001

LYS 10 PHE 11 0.0163

PHE 11 SER 12 0.0002

SER 12 GLU 13 0.0430

GLU 13 ASP 14 0.0001

ASP 14 ASN 15 -0.0435

ASN 15 LYS 16 -0.0002

LYS 16 ILE 17 -0.0234

ILE 17 GLY 18 -0.0001

GLY 18 GLU 19 0.0278

GLU 19 GLY 20 0.0001

GLY 20 GLY 21 -0.1084

GLY 21 PHE 22 0.0001

PHE 22 GLY 23 -0.0420

GLY 23 ASP 24 0.0001

ASP 24 VAL 25 0.0320

VAL 25 TYR 26 -0.0003

TYR 26 LYS 27 0.1365

LYS 27 GLY 28 -0.0000

GLY 28 MET 29 0.2022

MET 29 PHE 30 -0.0000

PHE 30 PRO 31 -0.0509

PRO 31 ASN 32 0.0005

ASN 32 GLY 33 0.1363

GLY 33 TYR 34 0.0001

TYR 34 GLU 35 0.0415

GLU 35 ILE 36 0.0001

ILE 36 ALA 37 0.0937

ALA 37 VAL 38 0.0002

VAL 38 LYS 39 0.0116

LYS 39 ARG 40 0.0003

ARG 40 LEU 41 -0.0010

LEU 41 ILE 42 0.0003

ILE 42 ARG 43 0.0142

ARG 43 ASN 44 0.0000

ASN 44 SER 45 -0.0238

SER 45 SER 46 -0.0000

SER 46 GLN 47 0.0283

GLN 47 GLY 48 -0.0001

GLY 48 ALA 49 0.0149

ALA 49 VAL 50 -0.0001

VAL 50 GLU 51 -0.0109

GLU 51 PHE 52 0.0000

PHE 52 LYS 53 0.0093

LYS 53 ASN 54 0.0000

ASN 54 GLU 55 -0.1084

GLU 55 VAL 56 0.0000

VAL 56 LEU 57 -0.1243

LEU 57 LEU 58 -0.0001

LEU 58 ILE 59 -0.2372

ILE 59 ALA 60 -0.0002

ALA 60 LYS 61 -0.1177

LYS 61 LEU 62 -0.0000

LEU 62 GLN 63 -0.0591

GLN 63 HIS 64 -0.0003

HIS 64 ARG 65 -0.0252

ARG 65 ASN 66 0.0001

ASN 66 LEU 67 0.0304

LEU 67 VAL 68 -0.0003

VAL 68 ARG 69 0.0539

ARG 69 LEU 70 0.0001

LEU 70 LEU 71 -0.1991

LEU 71 GLY 72 0.0001

GLY 72 PHE 73 0.0133

PHE 73 CYS 74 0.0002

CYS 74 ILE 75 0.0018

ILE 75 GLN 76 0.0002

GLN 76 ARG 77 -0.0135

ARG 77 ASN 78 0.0003

ASN 78 GLU 79 0.0237

GLU 79 LYS 80 0.0004

LYS 80 ILE 81 0.0459

ILE 81 LEU 82 0.0002

LEU 82 ILE 83 0.0379

ILE 83 TYR 84 0.0003

TYR 84 GLU 85 0.0645

GLU 85 TYR 86 0.0003

TYR 86 MET 87 -0.0847

MET 87 HIS 88 0.0001

HIS 88 ASN 89 -0.0443

ASN 89 LYS 90 0.0002

LYS 90 SER 91 -0.0549

SER 91 LEU 92 0.0001

LEU 92 ASP 93 0.0470

ASP 93 TYR 94 0.0003

TYR 94 TYR 95 0.0194

TYR 95 LEU 96 0.0000

LEU 96 PHE 97 -0.0368

PHE 97 SER 98 0.0003

SER 98 PRO 99 -0.0039

PRO 99 GLU 100 0.0003

GLU 100 ASN 101 -0.0420

ASN 101 HIS 102 -0.0002

HIS 102 ARG 103 0.0127

ARG 103 LYS 104 -0.0003

LYS 104 LEU 105 0.0723

LEU 105 THR 106 0.0001

THR 106 TRP 107 0.1059

TRP 107 HIS 108 -0.0002

HIS 108 ALA 109 -0.0229

ALA 109 ARG 110 0.0000

ARG 110 TYR 111 0.0011

TYR 111 LYS 112 0.0001

LYS 112 ILE 113 0.0276

ILE 113 ILE 114 -0.0000

ILE 114 ARG 115 0.0447

ARG 115 GLY 116 0.0004

GLY 116 ILE 117 0.0261

ILE 117 ALA 118 -0.0001

ALA 118 ARG 119 0.0399

ARG 119 GLY 120 0.0002

GLY 120 ILE 121 -0.0670

ILE 121 LEU 122 0.0004

LEU 122 TYR 123 0.0482

TYR 123 LEU 124 0.0003

LEU 124 HIS 125 -0.0762

HIS 125 GLU 126 0.0002

GLU 126 ASP 127 0.0201

ASP 127 SER 128 -0.0002

SER 128 HIS 129 -0.1282

HIS 129 LEU 130 0.0005

LEU 130 LYS 131 0.0126

LYS 131 ILE 132 -0.0004

ILE 132 ILE 133 -0.0053

ILE 133 HIS 134 0.0003

HIS 134 CYS 135 -0.0268

CYS 135 ASP 136 0.0002

ASP 136 LEU 137 -0.0152

LEU 137 LYS 138 0.0001

LYS 138 PRO 139 0.0039

PRO 139 SER 140 -0.0001

SER 140 ASN 141 0.0602

ASN 141 ILE 142 0.0003

ILE 142 LEU 143 -0.0977

LEU 143 LEU 144 0.0001

LEU 144 ASP 145 0.0275

ASP 145 ASP 146 0.0002

ASP 146 LYS 147 -0.0102

LYS 147 MET 148 -0.0000

MET 148 ASN 149 -0.1019

ASN 149 ALA 150 -0.0001

ALA 150 LYS 151 -0.0047

LYS 151 ILE 152 -0.0002

ILE 152 SER 153 0.1178

SER 153 ASP 154 -0.0002

ASP 154 PHE 155 0.0906

PHE 155 GLY 156 -0.0002

GLY 156 LEU 157 -0.1321

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 -0.0446

ARG 159 ILE 160 -0.0001

ILE 160 VAL 161 -0.2312

VAL 161 ALA 162 -0.0002

ALA 162 ILE 163 0.0232

ILE 163 ASP 164 0.0002

ASP 164 GLN 165 0.0715

GLN 165 MET 166 -0.0001

MET 166 GLN 167 0.0742

GLN 167 GLY 168 0.0002

GLY 168 ASN 169 0.1154

ASN 169 THR 170 0.0000

THR 170 SER 171 0.0734

SER 171 ILE 172 -0.0000

ILE 172 ILE 173 -0.0902

ILE 173 ALA 174 -0.0001

ALA 174 GLY 175 -0.1806

GLY 175 THR 176 0.0002

THR 176 TYR 177 0.0944

TYR 177 GLY 178 0.0001

GLY 178 TYR 179 0.0655

TYR 179 MET 180 0.0000

MET 180 SER 181 0.0223

SER 181 PRO 182 0.0001

PRO 182 GLU 183 0.0179

GLU 183 TYR 184 0.0004

TYR 184 ALA 185 0.0396

ALA 185 MET 186 -0.0000

MET 186 LEU 187 -0.0136

LEU 187 GLY 188 -0.0001

GLY 188 GLN 189 0.0575

GLN 189 PHE 190 0.0003

PHE 190 SER 191 0.0608

SER 191 VAL 192 -0.0002

VAL 192 LYS 193 -0.0603

LYS 193 SER 194 -0.0002

SER 194 ASP 195 -0.0478

ASP 195 VAL 196 -0.0001

VAL 196 PHE 197 -0.0202

PHE 197 SER 198 0.0001

SER 198 PHE 199 -0.0317

PHE 199 GLY 200 0.0000

GLY 200 VAL 201 -0.0306

VAL 201 ILE 202 -0.0001

ILE 202 MET 203 0.0048

MET 203 LEU 204 -0.0004

LEU 204 GLU 205 0.0019

GLU 205 ILE 206 -0.0001

ILE 206 VAL 207 -0.0061

VAL 207 SER 208 0.0001

SER 208 GLY 209 -0.0808

GLY 209 LYS 210 0.0003

LYS 210 ARG 211 0.0268

ARG 211 ASN 212 -0.0002

ASN 212 VAL 213 0.0630

VAL 213 ASP 214 -0.0000

ASP 214 TYR 215 0.1138

TYR 215 ASN 216 0.0001

ASN 216 GLY 217 0.4218

GLY 217 VAL 218 -0.0000

VAL 218 ASN 219 0.0068

ASN 219 SER 220 0.0001

SER 220 ILE 221 -0.4464

ILE 221 ASP 222 0.0003

ASP 222 ASP 223 -0.0030

ASP 223 LEU 224 -0.0000

LEU 224 VAL 225 0.0456

VAL 225 SER 226 0.0004

SER 226 HIS 227 0.0722

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 0.0317

TRP 229 LYS 230 -0.0003

LYS 230 LYS 231 0.1718

LYS 231 TRP 232 0.0002

TRP 232 THR 233 0.0061

THR 233 GLU 234 -0.0001

GLU 234 ASN 235 0.0075

ASN 235 LYS 236 -0.0000

LYS 236 GLN 237 -0.0161

GLN 237 MET 238 -0.0001

MET 238 GLU 239 -0.0202

GLU 239 LEU 240 -0.0003

LEU 240 LEU 241 0.4500

LEU 241 ASP 242 0.0000

ASP 242 PRO 243 0.0424

PRO 243 ALA 244 -0.0002

ALA 244 LEU 245 -0.0226

LEU 245 THR 246 -0.0002

THR 246 TYR 247 0.1614

TYR 247 SER 248 0.0001

SER 248 PHE 249 0.0227

PHE 249 SER 250 -0.0003

SER 250 GLU 251 -0.0652

GLU 251 THR 252 0.0000

THR 252 GLU 253 0.0935

GLU 253 VAL 254 -0.0001

VAL 254 SER 255 0.0148

SER 255 ARG 256 0.0001

ARG 256 CYS 257 -0.0225

CYS 257 ILE 258 0.0002

ILE 258 GLN 259 0.0128

GLN 259 LEU 260 0.0004

LEU 260 GLY 261 -0.0196

GLY 261 LEU 262 -0.0001

LEU 262 LEU 263 0.0121

LEU 263 CYS 264 -0.0002

CYS 264 VAL 265 -0.0362

VAL 265 GLN 266 0.0000

GLN 266 GLU 267 -0.0009

GLU 267 ASN 268 0.0001

ASN 268 PRO 269 -0.0373

PRO 269 ASP 270 0.0001

ASP 270 GLN 271 0.0909

GLN 271 ARG 272 0.0001

ARG 272 PRO 273 -0.1195

PRO 273 THR 274 0.0001

THR 274 MET 275 -0.1232

MET 275 ALA 276 0.0003

ALA 276 THR 277 0.0774

THR 277 ILE 278 0.0000

ILE 278 ALA 279 -0.0059

ALA 279 LEU 280 0.0002

LEU 280 TYR 281 -0.0259

TYR 281 PHE 282 0.0001

PHE 282 ASN 283 0.0126

ASN 283 ILE 284 0.0002

ILE 284 ASP 285 -0.0262

ASP 285 SER 286 -0.0001

SER 286 ILE 287 0.0030

ILE 287 ASP 288 -0.0003

ASP 288 LEU 289 -0.0610

LEU 289 PRO 290 0.0001

PRO 290 LEU 291 -0.0895

LEU 291 PRO 292 0.0002

PRO 292 GLN 293 -0.0921

GLN 293 GLN 294 -0.0000

GLN 294 PRO 295 -0.0112

PRO 295 PRO 296 0.0002

PRO 296 PHE 297 -0.1070

PHE 297 TYR 298 0.0003

TYR 298 MET 299 -0.1915

MET 299 ARG 300 0.0002

ARG 300 GLY 301 0.1161

GLY 301 LYS 302 -0.0001

LYS 302 ILE 303 -0.0396

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 -0.0110

SER 305 LYS 306 -0.0002

LYS 306 VAL 307 0.0743

VAL 307 ALA 308 -0.0002

ALA 308 SER 309 0.1341

SER 309 LYS 310 0.0003

LYS 310 LYS 311 -0.1599

LYS 311 THR 312 0.0003

THR 312 MET 313 0.1634

MET 313 SER 314 -0.0001

SER 314 GLY 315 0.2320

GLY 315 ARG 316 -0.0001

ARG 316 PRO 317 0.0682

PRO 317 ARG 318 -0.0003

ARG 318 SER 319 -0.1292

SER 319 TYR 320 -0.0001

TYR 320 SER 321 0.1677

SER 321 VAL 322 -0.0000

VAL 322 THR 323 0.1419

THR 323 ARG 324 -0.0002

ARG 324 PHE 325 0.1069

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 27 ---

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

* *