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

* *

CA strain for 230101190352136506

--- normal mode 23 ---

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 0.1337

MET 3 ILE 4 0.0001

ILE 4 ARG 5 0.0330

ARG 5 LEU 6 -0.0000

LEU 6 ALA 7 0.1185

ALA 7 THR 8 0.0000

THR 8 ASN 9 0.0941

ASN 9 LYS 10 0.0000

LYS 10 PHE 11 0.0182

PHE 11 SER 12 -0.0003

SER 12 GLU 13 -0.0831

GLU 13 ASP 14 0.0002

ASP 14 ASN 15 0.0537

ASN 15 LYS 16 0.0000

LYS 16 ILE 17 0.0389

ILE 17 GLY 18 -0.0001

GLY 18 GLU 19 0.0167

GLU 19 GLY 20 -0.0001

GLY 20 GLY 21 0.0838

GLY 21 PHE 22 -0.0000

PHE 22 GLY 23 0.2127

GLY 23 ASP 24 -0.0003

ASP 24 VAL 25 -0.0077

VAL 25 TYR 26 -0.0001

TYR 26 LYS 27 -0.1191

LYS 27 GLY 28 0.0003

GLY 28 MET 29 -0.2037

MET 29 PHE 30 0.0000

PHE 30 PRO 31 0.0266

PRO 31 ASN 32 0.0000

ASN 32 GLY 33 0.0079

GLY 33 TYR 34 0.0001

TYR 34 GLU 35 0.0440

GLU 35 ILE 36 -0.0002

ILE 36 ALA 37 -0.0985

ALA 37 VAL 38 0.0003

VAL 38 LYS 39 -0.0562

LYS 39 ARG 40 -0.0000

ARG 40 LEU 41 0.0972

LEU 41 ILE 42 0.0001

ILE 42 ARG 43 -0.0816

ARG 43 ASN 44 0.0001

ASN 44 SER 45 0.2013

SER 45 SER 46 0.0002

SER 46 GLN 47 -0.0917

GLN 47 GLY 48 0.0002

GLY 48 ALA 49 -0.0737

ALA 49 VAL 50 0.0001

VAL 50 GLU 51 0.0616

GLU 51 PHE 52 -0.0002

PHE 52 LYS 53 -0.0355

LYS 53 ASN 54 -0.0000

ASN 54 GLU 55 0.0762

GLU 55 VAL 56 0.0001

VAL 56 LEU 57 0.0331

LEU 57 LEU 58 -0.0001

LEU 58 ILE 59 0.0698

ILE 59 ALA 60 -0.0000

ALA 60 LYS 61 0.0505

LYS 61 LEU 62 -0.0003

LEU 62 GLN 63 -0.0316

GLN 63 HIS 64 -0.0002

HIS 64 ARG 65 -0.0799

ARG 65 ASN 66 0.0002

ASN 66 LEU 67 0.0563

LEU 67 VAL 68 0.0001

VAL 68 ARG 69 -0.0681

ARG 69 LEU 70 0.0000

LEU 70 LEU 71 0.0757

LEU 71 GLY 72 0.0001

GLY 72 PHE 73 0.0538

PHE 73 CYS 74 0.0002

CYS 74 ILE 75 0.0463

ILE 75 GLN 76 0.0000

GLN 76 ARG 77 0.0085

ARG 77 ASN 78 -0.0001

ASN 78 GLU 79 -0.0066

GLU 79 LYS 80 0.0001

LYS 80 ILE 81 -0.0620

ILE 81 LEU 82 0.0002

LEU 82 ILE 83 -0.1204

ILE 83 TYR 84 -0.0000

TYR 84 GLU 85 -0.1440

GLU 85 TYR 86 0.0000

TYR 86 MET 87 0.0886

MET 87 HIS 88 0.0001

HIS 88 ASN 89 -0.0098

ASN 89 LYS 90 0.0002

LYS 90 SER 91 0.1752

SER 91 LEU 92 -0.0001

LEU 92 ASP 93 0.0319

ASP 93 TYR 94 0.0002

TYR 94 TYR 95 0.0023

TYR 95 LEU 96 0.0002

LEU 96 PHE 97 0.0273

PHE 97 SER 98 0.0000

SER 98 PRO 99 -0.0931

PRO 99 GLU 100 -0.0000

GLU 100 ASN 101 0.0338

ASN 101 HIS 102 0.0002

HIS 102 ARG 103 -0.1036

ARG 103 LYS 104 0.0001

LYS 104 LEU 105 0.1716

LEU 105 THR 106 0.0000

THR 106 TRP 107 0.1714

TRP 107 HIS 108 -0.0001

HIS 108 ALA 109 -0.0786

ALA 109 ARG 110 -0.0000

ARG 110 TYR 111 0.1290

TYR 111 LYS 112 0.0000

LYS 112 ILE 113 -0.0191

ILE 113 ILE 114 0.0002

ILE 114 ARG 115 -0.0213

ARG 115 GLY 116 -0.0002

GLY 116 ILE 117 0.0527

ILE 117 ALA 118 -0.0001

ALA 118 ARG 119 0.0773

ARG 119 GLY 120 0.0000

GLY 120 ILE 121 0.0765

ILE 121 LEU 122 -0.0004

LEU 122 TYR 123 0.1849

TYR 123 LEU 124 0.0000

LEU 124 HIS 125 0.1486

HIS 125 GLU 126 -0.0001

GLU 126 ASP 127 0.0536

ASP 127 SER 128 0.0003

SER 128 HIS 129 -0.0425

HIS 129 LEU 130 -0.0002

LEU 130 LYS 131 0.0172

LYS 131 ILE 132 -0.0001

ILE 132 ILE 133 0.0347

ILE 133 HIS 134 -0.0003

HIS 134 CYS 135 0.0486

CYS 135 ASP 136 0.0002

ASP 136 LEU 137 -0.0847

LEU 137 LYS 138 0.0001

LYS 138 PRO 139 -0.1722

PRO 139 SER 140 -0.0001

SER 140 ASN 141 -0.1564

ASN 141 ILE 142 0.0002

ILE 142 LEU 143 0.1639

LEU 143 LEU 144 0.0001

LEU 144 ASP 145 -0.0427

ASP 145 ASP 146 0.0000

ASP 146 LYS 147 0.0501

LYS 147 MET 148 -0.0000

MET 148 ASN 149 -0.0899

ASN 149 ALA 150 0.0001

ALA 150 LYS 151 -0.0999

LYS 151 ILE 152 0.0004

ILE 152 SER 153 -0.0256

SER 153 ASP 154 -0.0000

ASP 154 PHE 155 -0.2434

PHE 155 GLY 156 -0.0002

GLY 156 LEU 157 0.0960

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 -0.0540

ARG 159 ILE 160 0.0001

ILE 160 VAL 161 -0.0154

VAL 161 ALA 162 0.0003

ALA 162 ILE 163 -0.0279

ILE 163 ASP 164 0.0000

ASP 164 GLN 165 0.0471

GLN 165 MET 166 -0.0004

MET 166 GLN 167 0.0522

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 0.0510

ASN 169 THR 170 0.0001

THR 170 SER 171 0.1569

SER 171 ILE 172 0.0003

ILE 172 ILE 173 -0.0455

ILE 173 ALA 174 -0.0002

ALA 174 GLY 175 -0.1355

GLY 175 THR 176 -0.0000

THR 176 TYR 177 -0.0262

TYR 177 GLY 178 0.0002

GLY 178 TYR 179 -0.0951

TYR 179 MET 180 -0.0001

MET 180 SER 181 0.0289

SER 181 PRO 182 0.0004

PRO 182 GLU 183 0.0442

GLU 183 TYR 184 0.0001

TYR 184 ALA 185 0.0974

ALA 185 MET 186 -0.0000

MET 186 LEU 187 0.1491

LEU 187 GLY 188 -0.0000

GLY 188 GLN 189 0.0371

GLN 189 PHE 190 0.0001

PHE 190 SER 191 0.0661

SER 191 VAL 192 -0.0001

VAL 192 LYS 193 0.1902

LYS 193 SER 194 -0.0001

SER 194 ASP 195 0.0476

ASP 195 VAL 196 0.0005

VAL 196 PHE 197 0.0219

PHE 197 SER 198 -0.0000

SER 198 PHE 199 -0.0134

PHE 199 GLY 200 0.0002

GLY 200 VAL 201 -0.0115

VAL 201 ILE 202 -0.0001

ILE 202 MET 203 -0.0626

MET 203 LEU 204 -0.0001

LEU 204 GLU 205 0.0079

GLU 205 ILE 206 0.0001

ILE 206 VAL 207 -0.0198

VAL 207 SER 208 -0.0003

SER 208 GLY 209 0.0193

GLY 209 LYS 210 -0.0002

LYS 210 ARG 211 -0.0181

ARG 211 ASN 212 0.0001

ASN 212 VAL 213 -0.0549

VAL 213 ASP 214 0.0000

ASP 214 TYR 215 -0.0673

TYR 215 ASN 216 -0.0003

ASN 216 GLY 217 -0.0357

GLY 217 VAL 218 0.0000

VAL 218 ASN 219 -0.0026

ASN 219 SER 220 -0.0000

SER 220 ILE 221 0.0759

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 0.0242

ASP 223 LEU 224 -0.0005

LEU 224 VAL 225 0.0100

VAL 225 SER 226 -0.0001

SER 226 HIS 227 0.0148

HIS 227 ALA 228 0.0000

ALA 228 TRP 229 0.0034

TRP 229 LYS 230 -0.0000

LYS 230 LYS 231 0.0386

LYS 231 TRP 232 0.0003

TRP 232 THR 233 -0.0034

THR 233 GLU 234 -0.0004

GLU 234 ASN 235 -0.0040

ASN 235 LYS 236 0.0001

LYS 236 GLN 237 -0.0082

GLN 237 MET 238 0.0000

MET 238 GLU 239 -0.0285

GLU 239 LEU 240 0.0002

LEU 240 LEU 241 0.0215

LEU 241 ASP 242 0.0002

ASP 242 PRO 243 -0.0049

PRO 243 ALA 244 0.0002

ALA 244 LEU 245 0.0692

LEU 245 THR 246 0.0001

THR 246 TYR 247 0.0766

TYR 247 SER 248 0.0000

SER 248 PHE 249 0.1210

PHE 249 SER 250 0.0003

SER 250 GLU 251 -0.0362

GLU 251 THR 252 -0.0001

THR 252 GLU 253 -0.0014

GLU 253 VAL 254 0.0001

VAL 254 SER 255 0.0162

SER 255 ARG 256 0.0001

ARG 256 CYS 257 -0.0291

CYS 257 ILE 258 0.0001

ILE 258 GLN 259 0.0030

GLN 259 LEU 260 -0.0001

LEU 260 GLY 261 -0.0539

GLY 261 LEU 262 -0.0001

LEU 262 LEU 263 0.0287

LEU 263 CYS 264 0.0000

CYS 264 VAL 265 0.0198

VAL 265 GLN 266 0.0002

GLN 266 GLU 267 -0.0261

GLU 267 ASN 268 0.0002

ASN 268 PRO 269 0.1074

PRO 269 ASP 270 -0.0001

ASP 270 GLN 271 0.0436

GLN 271 ARG 272 0.0001

ARG 272 PRO 273 0.0233

PRO 273 THR 274 0.0002

THR 274 MET 275 0.0706

MET 275 ALA 276 0.0001

ALA 276 THR 277 0.1471

THR 277 ILE 278 -0.0001

ILE 278 ALA 279 -0.0158

ALA 279 LEU 280 0.0001

LEU 280 TYR 281 0.0109

TYR 281 PHE 282 0.0003

PHE 282 ASN 283 0.0048

ASN 283 ILE 284 0.0003

ILE 284 ASP 285 0.0138

ASP 285 SER 286 -0.0003

SER 286 ILE 287 0.0273

ILE 287 ASP 288 0.0000

ASP 288 LEU 289 -0.0676

LEU 289 PRO 290 0.0002

PRO 290 LEU 291 -0.0137

LEU 291 PRO 292 -0.0002

PRO 292 GLN 293 -0.0461

GLN 293 GLN 294 -0.0002

GLN 294 PRO 295 -0.0166

PRO 295 PRO 296 -0.0002

PRO 296 PHE 297 0.0808

PHE 297 TYR 298 -0.0002

TYR 298 MET 299 0.0170

MET 299 ARG 300 0.0001

ARG 300 GLY 301 -0.1217

GLY 301 LYS 302 0.0000

LYS 302 ILE 303 0.0567

ILE 303 GLU 304 0.0003

GLU 304 SER 305 -0.0130

SER 305 LYS 306 -0.0001

LYS 306 VAL 307 0.0411

VAL 307 ALA 308 0.0002

ALA 308 SER 309 0.1618

SER 309 LYS 310 0.0004

LYS 310 LYS 311 -0.0507

LYS 311 THR 312 0.0001

THR 312 MET 313 0.0980

MET 313 SER 314 -0.0004

SER 314 GLY 315 0.0499

GLY 315 ARG 316 0.0001

ARG 316 PRO 317 0.3253

PRO 317 ARG 318 0.0000

ARG 318 SER 319 -0.1941

SER 319 TYR 320 0.0000

TYR 320 SER 321 -0.0292

SER 321 VAL 322 -0.0001

VAL 322 THR 323 0.1470

THR 323 ARG 324 -0.0000

ARG 324 PHE 325 -0.4672

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 23 ---

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

* *