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

* *

CA strain for 230101190352136506

--- normal mode 26 ---

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 -0.2026

MET 3 ILE 4 -0.0002

ILE 4 ARG 5 0.1035

ARG 5 LEU 6 -0.0003

LEU 6 ALA 7 0.1424

ALA 7 THR 8 -0.0002

THR 8 ASN 9 0.1331

ASN 9 LYS 10 -0.0002

LYS 10 PHE 11 -0.0487

PHE 11 SER 12 0.0004

SER 12 GLU 13 0.0011

GLU 13 ASP 14 -0.0001

ASP 14 ASN 15 -0.0144

ASN 15 LYS 16 -0.0000

LYS 16 ILE 17 -0.0336

ILE 17 GLY 18 -0.0000

GLY 18 GLU 19 -0.0317

GLU 19 GLY 20 -0.0003

GLY 20 GLY 21 0.1014

GLY 21 PHE 22 -0.0001

PHE 22 GLY 23 -0.0009

GLY 23 ASP 24 0.0004

ASP 24 VAL 25 0.0344

VAL 25 TYR 26 -0.0001

TYR 26 LYS 27 0.0014

LYS 27 GLY 28 0.0002

GLY 28 MET 29 -0.1380

MET 29 PHE 30 0.0002

PHE 30 PRO 31 0.1484

PRO 31 ASN 32 -0.0002

ASN 32 GLY 33 -0.0438

GLY 33 TYR 34 -0.0000

TYR 34 GLU 35 0.0798

GLU 35 ILE 36 0.0001

ILE 36 ALA 37 -0.1020

ALA 37 VAL 38 -0.0003

VAL 38 LYS 39 0.0295

LYS 39 ARG 40 -0.0000

ARG 40 LEU 41 -0.1266

LEU 41 ILE 42 0.0000

ILE 42 ARG 43 0.1523

ARG 43 ASN 44 0.0004

ASN 44 SER 45 -0.0597

SER 45 SER 46 0.0002

SER 46 GLN 47 -0.0349

GLN 47 GLY 48 -0.0004

GLY 48 ALA 49 0.0126

ALA 49 VAL 50 0.0002

VAL 50 GLU 51 0.0547

GLU 51 PHE 52 -0.0002

PHE 52 LYS 53 0.0211

LYS 53 ASN 54 0.0003

ASN 54 GLU 55 -0.0619

GLU 55 VAL 56 0.0003

VAL 56 LEU 57 0.1611

LEU 57 LEU 58 -0.0000

LEU 58 ILE 59 -0.0031

ILE 59 ALA 60 0.0001

ALA 60 LYS 61 0.1266

LYS 61 LEU 62 0.0001

LEU 62 GLN 63 -0.0228

GLN 63 HIS 64 -0.0002

HIS 64 ARG 65 -0.0619

ARG 65 ASN 66 -0.0002

ASN 66 LEU 67 0.1337

LEU 67 VAL 68 0.0003

VAL 68 ARG 69 0.2428

ARG 69 LEU 70 0.0000

LEU 70 LEU 71 0.1773

LEU 71 GLY 72 -0.0001

GLY 72 PHE 73 0.0578

PHE 73 CYS 74 -0.0003

CYS 74 ILE 75 0.0027

ILE 75 GLN 76 0.0004

GLN 76 ARG 77 0.1438

ARG 77 ASN 78 0.0002

ASN 78 GLU 79 0.0622

GLU 79 LYS 80 0.0000

LYS 80 ILE 81 -0.0241

ILE 81 LEU 82 -0.0001

LEU 82 ILE 83 -0.0979

ILE 83 TYR 84 0.0001

TYR 84 GLU 85 0.0202

GLU 85 TYR 86 0.0001

TYR 86 MET 87 0.3414

MET 87 HIS 88 0.0001

HIS 88 ASN 89 0.2339

ASN 89 LYS 90 -0.0000

LYS 90 SER 91 0.1471

SER 91 LEU 92 0.0003

LEU 92 ASP 93 0.0575

ASP 93 TYR 94 -0.0000

TYR 94 TYR 95 -0.0251

TYR 95 LEU 96 0.0002

LEU 96 PHE 97 0.0155

PHE 97 SER 98 -0.0003

SER 98 PRO 99 -0.0436

PRO 99 GLU 100 0.0002

GLU 100 ASN 101 -0.0039

ASN 101 HIS 102 0.0003

HIS 102 ARG 103 -0.0353

ARG 103 LYS 104 0.0001

LYS 104 LEU 105 -0.0625

LEU 105 THR 106 -0.0001

THR 106 TRP 107 -0.0664

TRP 107 HIS 108 -0.0001

HIS 108 ALA 109 0.0966

ALA 109 ARG 110 -0.0000

ARG 110 TYR 111 -0.0938

TYR 111 LYS 112 0.0005

LYS 112 ILE 113 0.0038

ILE 113 ILE 114 0.0002

ILE 114 ARG 115 -0.0398

ARG 115 GLY 116 -0.0002

GLY 116 ILE 117 0.0223

ILE 117 ALA 118 0.0001

ALA 118 ARG 119 -0.0037

ARG 119 GLY 120 0.0001

GLY 120 ILE 121 0.0108

ILE 121 LEU 122 -0.0001

LEU 122 TYR 123 0.0967

TYR 123 LEU 124 0.0001

LEU 124 HIS 125 0.0933

HIS 125 GLU 126 -0.0002

GLU 126 ASP 127 -0.0372

ASP 127 SER 128 0.0001

SER 128 HIS 129 0.0348

HIS 129 LEU 130 0.0002

LEU 130 LYS 131 -0.0229

LYS 131 ILE 132 0.0003

ILE 132 ILE 133 -0.0466

ILE 133 HIS 134 0.0001

HIS 134 CYS 135 -0.0573

CYS 135 ASP 136 0.0003

ASP 136 LEU 137 0.0177

LEU 137 LYS 138 -0.0000

LYS 138 PRO 139 -0.1289

PRO 139 SER 140 0.0001

SER 140 ASN 141 -0.0114

ASN 141 ILE 142 -0.0001

ILE 142 LEU 143 0.1242

LEU 143 LEU 144 0.0000

LEU 144 ASP 145 -0.0322

ASP 145 ASP 146 0.0003

ASP 146 LYS 147 0.1075

LYS 147 MET 148 0.0002

MET 148 ASN 149 -0.0580

ASN 149 ALA 150 -0.0000

ALA 150 LYS 151 0.1160

LYS 151 ILE 152 0.0002

ILE 152 SER 153 0.1104

SER 153 ASP 154 0.0000

ASP 154 PHE 155 -0.0369

PHE 155 GLY 156 0.0001

GLY 156 LEU 157 0.1894

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 -0.1084

ARG 159 ILE 160 -0.0000

ILE 160 VAL 161 -0.0065

VAL 161 ALA 162 -0.0000

ALA 162 ILE 163 0.0176

ILE 163 ASP 164 -0.0001

ASP 164 GLN 165 -0.0784

GLN 165 MET 166 -0.0001

MET 166 GLN 167 -0.1946

GLN 167 GLY 168 0.0000

GLY 168 ASN 169 -0.1937

ASN 169 THR 170 0.0002

THR 170 SER 171 -0.1798

SER 171 ILE 172 -0.0002

ILE 172 ILE 173 -0.0906

ILE 173 ALA 174 -0.0004

ALA 174 GLY 175 -0.2251

GLY 175 THR 176 -0.0000

THR 176 TYR 177 0.1932

TYR 177 GLY 178 -0.0003

GLY 178 TYR 179 0.0840

TYR 179 MET 180 0.0001

MET 180 SER 181 0.0937

SER 181 PRO 182 0.0000

PRO 182 GLU 183 -0.0533

GLU 183 TYR 184 -0.0000

TYR 184 ALA 185 -0.0509

ALA 185 MET 186 -0.0002

MET 186 LEU 187 -0.1999

LEU 187 GLY 188 -0.0004

GLY 188 GLN 189 -0.0138

GLN 189 PHE 190 -0.0002

PHE 190 SER 191 -0.0194

SER 191 VAL 192 0.0001

VAL 192 LYS 193 0.0323

LYS 193 SER 194 -0.0001

SER 194 ASP 195 0.0016

ASP 195 VAL 196 -0.0000

VAL 196 PHE 197 -0.0214

PHE 197 SER 198 0.0002

SER 198 PHE 199 0.0204

PHE 199 GLY 200 0.0004

GLY 200 VAL 201 -0.0081

VAL 201 ILE 202 -0.0003

ILE 202 MET 203 0.0771

MET 203 LEU 204 -0.0005

LEU 204 GLU 205 0.0138

GLU 205 ILE 206 -0.0003

ILE 206 VAL 207 0.0882

VAL 207 SER 208 0.0002

SER 208 GLY 209 0.0732

GLY 209 LYS 210 -0.0001

LYS 210 ARG 211 -0.0753

ARG 211 ASN 212 0.0000

ASN 212 VAL 213 0.0484

VAL 213 ASP 214 0.0002

ASP 214 TYR 215 0.0122

TYR 215 ASN 216 -0.0003

ASN 216 GLY 217 0.6630

GLY 217 VAL 218 0.0001

VAL 218 ASN 219 0.0096

ASN 219 SER 220 -0.0001

SER 220 ILE 221 -0.3383

ILE 221 ASP 222 0.0000

ASP 222 ASP 223 -0.0588

ASP 223 LEU 224 -0.0001

LEU 224 VAL 225 -0.0529

VAL 225 SER 226 0.0002

SER 226 HIS 227 -0.0132

HIS 227 ALA 228 0.0001

ALA 228 TRP 229 -0.0307

TRP 229 LYS 230 0.0002

LYS 230 LYS 231 0.0608

LYS 231 TRP 232 -0.0003

TRP 232 THR 233 0.0025

THR 233 GLU 234 0.0000

GLU 234 ASN 235 0.0122

ASN 235 LYS 236 0.0000

LYS 236 GLN 237 0.0231

GLN 237 MET 238 0.0000

MET 238 GLU 239 -0.0472

GLU 239 LEU 240 -0.0004

LEU 240 LEU 241 0.0348

LEU 241 ASP 242 -0.0001

ASP 242 PRO 243 -0.0066

PRO 243 ALA 244 -0.0001

ALA 244 LEU 245 -0.0092

LEU 245 THR 246 -0.0002

THR 246 TYR 247 -0.0690

TYR 247 SER 248 0.0000

SER 248 PHE 249 0.0264

PHE 249 SER 250 0.0005

SER 250 GLU 251 0.0195

GLU 251 THR 252 0.0003

THR 252 GLU 253 0.0357

GLU 253 VAL 254 -0.0002

VAL 254 SER 255 0.0104

SER 255 ARG 256 -0.0004

ARG 256 CYS 257 -0.0067

CYS 257 ILE 258 0.0004

ILE 258 GLN 259 -0.0361

GLN 259 LEU 260 0.0001

LEU 260 GLY 261 0.0064

GLY 261 LEU 262 0.0003

LEU 262 LEU 263 -0.0113

LEU 263 CYS 264 0.0004

CYS 264 VAL 265 -0.0079

VAL 265 GLN 266 0.0001

GLN 266 GLU 267 0.0490

GLU 267 ASN 268 0.0004

ASN 268 PRO 269 0.0087

PRO 269 ASP 270 -0.0002

ASP 270 GLN 271 0.0548

GLN 271 ARG 272 -0.0002

ARG 272 PRO 273 -0.0550

PRO 273 THR 274 0.0003

THR 274 MET 275 -0.0625

MET 275 ALA 276 -0.0000

ALA 276 THR 277 0.1034

THR 277 ILE 278 -0.0003

ILE 278 ALA 279 -0.0334

ALA 279 LEU 280 -0.0003

LEU 280 TYR 281 -0.0175

TYR 281 PHE 282 0.0002

PHE 282 ASN 283 -0.0047

ASN 283 ILE 284 -0.0002

ILE 284 ASP 285 0.0097

ASP 285 SER 286 -0.0000

SER 286 ILE 287 0.0526

ILE 287 ASP 288 -0.0003

ASP 288 LEU 289 0.0354

LEU 289 PRO 290 0.0002

PRO 290 LEU 291 -0.0454

LEU 291 PRO 292 0.0000

PRO 292 GLN 293 -0.0026

GLN 293 GLN 294 0.0002

GLN 294 PRO 295 0.0122

PRO 295 PRO 296 -0.0001

PRO 296 PHE 297 -0.0536

PHE 297 TYR 298 0.0002

TYR 298 MET 299 -0.0216

MET 299 ARG 300 -0.0000

ARG 300 GLY 301 0.0080

GLY 301 LYS 302 -0.0002

LYS 302 ILE 303 -0.0457

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 -0.0404

SER 305 LYS 306 0.0001

LYS 306 VAL 307 -0.0376

VAL 307 ALA 308 0.0003

ALA 308 SER 309 -0.1065

SER 309 LYS 310 0.0000

LYS 310 LYS 311 0.0244

LYS 311 THR 312 -0.0001

THR 312 MET 313 -0.2019

MET 313 SER 314 0.0001

SER 314 GLY 315 -0.1021

GLY 315 ARG 316 0.0000

ARG 316 PRO 317 -0.1733

PRO 317 ARG 318 -0.0001

ARG 318 SER 319 -0.1221

SER 319 TYR 320 -0.0001

TYR 320 SER 321 0.0700

SER 321 VAL 322 0.0002

VAL 322 THR 323 -0.0684

THR 323 ARG 324 0.0002

ARG 324 PHE 325 0.0658

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 26 ---

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

* *