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

* *

CA strain for 230101190352136506

--- normal mode 22 ---

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 -0.0855

MET 3 ILE 4 -0.0001

ILE 4 ARG 5 0.0069

ARG 5 LEU 6 0.0002

LEU 6 ALA 7 0.0802

ALA 7 THR 8 -0.0001

THR 8 ASN 9 0.0841

ASN 9 LYS 10 0.0004

LYS 10 PHE 11 -0.0443

PHE 11 SER 12 0.0001

SER 12 GLU 13 -0.0159

GLU 13 ASP 14 -0.0002

ASP 14 ASN 15 0.0294

ASN 15 LYS 16 0.0002

LYS 16 ILE 17 0.0763

ILE 17 GLY 18 -0.0002

GLY 18 GLU 19 -0.0564

GLU 19 GLY 20 0.0002

GLY 20 GLY 21 0.0006

GLY 21 PHE 22 0.0002

PHE 22 GLY 23 -0.1427

GLY 23 ASP 24 0.0000

ASP 24 VAL 25 -0.0323

VAL 25 TYR 26 0.0000

TYR 26 LYS 27 -0.0865

LYS 27 GLY 28 0.0003

GLY 28 MET 29 -0.1690

MET 29 PHE 30 0.0001

PHE 30 PRO 31 0.0419

PRO 31 ASN 32 0.0000

ASN 32 GLY 33 -0.1134

GLY 33 TYR 34 -0.0003

TYR 34 GLU 35 -0.0516

GLU 35 ILE 36 -0.0003

ILE 36 ALA 37 -0.0553

ALA 37 VAL 38 0.0000

VAL 38 LYS 39 -0.0223

LYS 39 ARG 40 -0.0002

ARG 40 LEU 41 -0.1470

LEU 41 ILE 42 0.0001

ILE 42 ARG 43 0.0898

ARG 43 ASN 44 0.0002

ASN 44 SER 45 -0.1354

SER 45 SER 46 -0.0002

SER 46 GLN 47 0.0973

GLN 47 GLY 48 0.0003

GLY 48 ALA 49 0.0945

ALA 49 VAL 50 -0.0001

VAL 50 GLU 51 -0.0261

GLU 51 PHE 52 0.0001

PHE 52 LYS 53 -0.0144

LYS 53 ASN 54 0.0000

ASN 54 GLU 55 -0.0144

GLU 55 VAL 56 -0.0000

VAL 56 LEU 57 -0.0161

LEU 57 LEU 58 0.0002

LEU 58 ILE 59 0.0114

ILE 59 ALA 60 0.0001

ALA 60 LYS 61 0.0306

LYS 61 LEU 62 0.0000

LEU 62 GLN 63 -0.0030

GLN 63 HIS 64 0.0002

HIS 64 ARG 65 -0.0516

ARG 65 ASN 66 -0.0000

ASN 66 LEU 67 0.0726

LEU 67 VAL 68 -0.0000

VAL 68 ARG 69 0.0347

ARG 69 LEU 70 0.0001

LEU 70 LEU 71 0.1265

LEU 71 GLY 72 0.0001

GLY 72 PHE 73 -0.0138

PHE 73 CYS 74 0.0001

CYS 74 ILE 75 -0.0075

ILE 75 GLN 76 -0.0001

GLN 76 ARG 77 -0.0045

ARG 77 ASN 78 0.0003

ASN 78 GLU 79 0.0365

GLU 79 LYS 80 -0.0001

LYS 80 ILE 81 0.0191

ILE 81 LEU 82 -0.0002

LEU 82 ILE 83 0.0150

ILE 83 TYR 84 0.0001

TYR 84 GLU 85 -0.0191

GLU 85 TYR 86 0.0000

TYR 86 MET 87 0.0834

MET 87 HIS 88 -0.0001

HIS 88 ASN 89 0.0076

ASN 89 LYS 90 -0.0001

LYS 90 SER 91 0.0238

SER 91 LEU 92 0.0001

LEU 92 ASP 93 0.0731

ASP 93 TYR 94 -0.0002

TYR 94 TYR 95 -0.0073

TYR 95 LEU 96 -0.0004

LEU 96 PHE 97 0.0123

PHE 97 SER 98 -0.0003

SER 98 PRO 99 -0.0427

PRO 99 GLU 100 -0.0004

GLU 100 ASN 101 -0.0557

ASN 101 HIS 102 -0.0001

HIS 102 ARG 103 0.0212

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 -0.0545

LEU 105 THR 106 0.0003

THR 106 TRP 107 -0.0423

TRP 107 HIS 108 -0.0000

HIS 108 ALA 109 0.0390

ALA 109 ARG 110 0.0000

ARG 110 TYR 111 -0.0137

TYR 111 LYS 112 0.0002

LYS 112 ILE 113 -0.0064

ILE 113 ILE 114 0.0001

ILE 114 ARG 115 0.0274

ARG 115 GLY 116 -0.0002

GLY 116 ILE 117 0.0459

ILE 117 ALA 118 -0.0002

ALA 118 ARG 119 0.0429

ARG 119 GLY 120 -0.0003

GLY 120 ILE 121 -0.0004

ILE 121 LEU 122 0.0002

LEU 122 TYR 123 0.1004

TYR 123 LEU 124 -0.0000

LEU 124 HIS 125 0.0359

HIS 125 GLU 126 0.0003

GLU 126 ASP 127 0.0007

ASP 127 SER 128 0.0000

SER 128 HIS 129 -0.0048

HIS 129 LEU 130 -0.0000

LEU 130 LYS 131 -0.0023

LYS 131 ILE 132 -0.0003

ILE 132 ILE 133 -0.0004

ILE 133 HIS 134 -0.0005

HIS 134 CYS 135 0.0204

CYS 135 ASP 136 -0.0000

ASP 136 LEU 137 -0.0102

LEU 137 LYS 138 0.0000

LYS 138 PRO 139 -0.0368

PRO 139 SER 140 -0.0000

SER 140 ASN 141 -0.0104

ASN 141 ILE 142 0.0001

ILE 142 LEU 143 0.0326

LEU 143 LEU 144 0.0002

LEU 144 ASP 145 -0.0092

ASP 145 ASP 146 -0.0000

ASP 146 LYS 147 0.1102

LYS 147 MET 148 0.0001

MET 148 ASN 149 -0.0912

ASN 149 ALA 150 -0.0001

ALA 150 LYS 151 0.0370

LYS 151 ILE 152 0.0004

ILE 152 SER 153 0.0628

SER 153 ASP 154 0.0001

ASP 154 PHE 155 -0.0336

PHE 155 GLY 156 0.0001

GLY 156 LEU 157 0.0440

LEU 157 ALA 158 -0.0000

ALA 158 ARG 159 -0.0334

ARG 159 ILE 160 0.0001

ILE 160 VAL 161 -0.0571

VAL 161 ALA 162 -0.0002

ALA 162 ILE 163 0.0003

ILE 163 ASP 164 -0.0001

ASP 164 GLN 165 -0.0053

GLN 165 MET 166 0.0001

MET 166 GLN 167 -0.0298

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 0.0150

ASN 169 THR 170 -0.0005

THR 170 SER 171 0.0269

SER 171 ILE 172 0.0001

ILE 172 ILE 173 -0.0646

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 -0.0839

GLY 175 THR 176 -0.0002

THR 176 TYR 177 0.1889

TYR 177 GLY 178 -0.0002

GLY 178 TYR 179 0.0123

TYR 179 MET 180 0.0005

MET 180 SER 181 0.0359

SER 181 PRO 182 0.0000

PRO 182 GLU 183 -0.0369

GLU 183 TYR 184 -0.0000

TYR 184 ALA 185 0.0252

ALA 185 MET 186 -0.0001

MET 186 LEU 187 0.0184

LEU 187 GLY 188 0.0002

GLY 188 GLN 189 0.0020

GLN 189 PHE 190 0.0003

PHE 190 SER 191 0.0162

SER 191 VAL 192 -0.0000

VAL 192 LYS 193 0.0033

LYS 193 SER 194 0.0001

SER 194 ASP 195 -0.0117

ASP 195 VAL 196 0.0001

VAL 196 PHE 197 -0.0250

PHE 197 SER 198 0.0001

SER 198 PHE 199 -0.0186

PHE 199 GLY 200 0.0000

GLY 200 VAL 201 0.0083

VAL 201 ILE 202 -0.0002

ILE 202 MET 203 -0.0259

MET 203 LEU 204 0.0001

LEU 204 GLU 205 0.0307

GLU 205 ILE 206 -0.0000

ILE 206 VAL 207 -0.0203

VAL 207 SER 208 -0.0000

SER 208 GLY 209 -0.0689

GLY 209 LYS 210 0.0001

LYS 210 ARG 211 -0.2507

ARG 211 ASN 212 0.0002

ASN 212 VAL 213 -0.0460

VAL 213 ASP 214 -0.0003

ASP 214 TYR 215 0.1603

TYR 215 ASN 216 -0.0001

ASN 216 GLY 217 -0.8109

GLY 217 VAL 218 0.0001

VAL 218 ASN 219 -0.0134

ASN 219 SER 220 0.0000

SER 220 ILE 221 0.1388

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 0.1859

ASP 223 LEU 224 -0.0000

LEU 224 VAL 225 0.0193

VAL 225 SER 226 0.0001

SER 226 HIS 227 0.0456

HIS 227 ALA 228 -0.0003

ALA 228 TRP 229 0.0765

TRP 229 LYS 230 -0.0002

LYS 230 LYS 231 -0.0002

LYS 231 TRP 232 -0.0001

TRP 232 THR 233 0.0018

THR 233 GLU 234 0.0002

GLU 234 ASN 235 -0.0217

ASN 235 LYS 236 -0.0001

LYS 236 GLN 237 0.0112

GLN 237 MET 238 0.0002

MET 238 GLU 239 0.0106

GLU 239 LEU 240 0.0004

LEU 240 LEU 241 0.0689

LEU 241 ASP 242 0.0003

ASP 242 PRO 243 -0.0142

PRO 243 ALA 244 -0.0001

ALA 244 LEU 245 -0.0227

LEU 245 THR 246 0.0002

THR 246 TYR 247 0.0301

TYR 247 SER 248 0.0000

SER 248 PHE 249 -0.0193

PHE 249 SER 250 0.0000

SER 250 GLU 251 -0.0159

GLU 251 THR 252 0.0001

THR 252 GLU 253 0.0407

GLU 253 VAL 254 0.0003

VAL 254 SER 255 -0.0209

SER 255 ARG 256 0.0004

ARG 256 CYS 257 0.0023

CYS 257 ILE 258 0.0002

ILE 258 GLN 259 0.0147

GLN 259 LEU 260 0.0001

LEU 260 GLY 261 -0.0155

GLY 261 LEU 262 0.0001

LEU 262 LEU 263 -0.0056

LEU 263 CYS 264 -0.0004

CYS 264 VAL 265 -0.0370

VAL 265 GLN 266 0.0002

GLN 266 GLU 267 -0.0025

GLU 267 ASN 268 0.0000

ASN 268 PRO 269 -0.0147

PRO 269 ASP 270 -0.0003

ASP 270 GLN 271 0.0435

GLN 271 ARG 272 0.0002

ARG 272 PRO 273 -0.1203

PRO 273 THR 274 -0.0000

THR 274 MET 275 -0.0359

MET 275 ALA 276 -0.0002

ALA 276 THR 277 0.0862

THR 277 ILE 278 -0.0000

ILE 278 ALA 279 -0.0197

ALA 279 LEU 280 0.0001

LEU 280 TYR 281 0.0046

TYR 281 PHE 282 0.0004

PHE 282 ASN 283 0.0074

ASN 283 ILE 284 0.0001

ILE 284 ASP 285 0.0043

ASP 285 SER 286 0.0002

SER 286 ILE 287 -0.0041

ILE 287 ASP 288 0.0002

ASP 288 LEU 289 -0.0798

LEU 289 PRO 290 0.0003

PRO 290 LEU 291 -0.0607

LEU 291 PRO 292 -0.0002

PRO 292 GLN 293 -0.1237

GLN 293 GLN 294 -0.0003

GLN 294 PRO 295 0.0137

PRO 295 PRO 296 -0.0003

PRO 296 PHE 297 -0.1279

PHE 297 TYR 298 -0.0000

TYR 298 MET 299 -0.0837

MET 299 ARG 300 0.0001

ARG 300 GLY 301 -0.0185

GLY 301 LYS 302 -0.0002

LYS 302 ILE 303 0.0789

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 0.0268

SER 305 LYS 306 0.0003

LYS 306 VAL 307 0.1070

VAL 307 ALA 308 -0.0002

ALA 308 SER 309 -0.0353

SER 309 LYS 310 0.0000

LYS 310 LYS 311 -0.2803

LYS 311 THR 312 0.0000

THR 312 MET 313 0.0898

MET 313 SER 314 0.0000

SER 314 GLY 315 0.2016

GLY 315 ARG 316 -0.0001

ARG 316 PRO 317 -0.3507

PRO 317 ARG 318 0.0000

ARG 318 SER 319 0.2059

SER 319 TYR 320 -0.0000

TYR 320 SER 321 0.0550

SER 321 VAL 322 -0.0001

VAL 322 THR 323 -0.1773

THR 323 ARG 324 -0.0002

ARG 324 PHE 325 0.4882

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 22 ---

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

* *