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

* *

CA strain for 22122720105119216

--- normal mode 10 ---

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
MET 1 GLU 2 -0.0002

GLU 2 LEU 3 -0.0234

LEU 3 ARG 4 0.0004

ARG 4 HIS 5 0.0274

HIS 5 THR 6 -0.0002

THR 6 PRO 7 0.0350

PRO 7 ALA 8 0.0003

ALA 8 ARG 9 -0.0490

ARG 9 ASP 10 -0.0001

ASP 10 LEU 11 0.0130

LEU 11 ASP 12 0.0001

ASP 12 LYS 13 -0.0961

LYS 13 PHE 14 -0.0001

PHE 14 ILE 15 -0.0023

ILE 15 GLU 16 -0.0001

GLU 16 ASP 17 -0.0951

ASP 17 HIS 18 -0.0003

HIS 18 LEU 19 -0.0162

LEU 19 LEU 20 0.0002

LEU 20 PRO 21 0.3191

PRO 21 ASN 22 0.0000

ASN 22 THR 23 0.0582

THR 23 CYS 24 -0.0001

CYS 24 PHE 25 -0.1149

PHE 25 ARG 26 -0.0000

ARG 26 THR 27 0.0161

THR 27 GLN 28 0.0002

GLN 28 VAL 29 -0.0840

VAL 29 LYS 30 -0.0002

LYS 30 GLU 31 -0.0895

GLU 31 ALA 32 0.0002

ALA 32 ILE 33 -0.0994

ILE 33 ASP 34 0.0003

ASP 34 ILE 35 -0.0831

ILE 35 VAL 36 0.0003

VAL 36 CYS 37 -0.0853

CYS 37 ARG 38 0.0002

ARG 38 PHE 39 -0.0136

PHE 39 LEU 40 0.0000

LEU 40 LYS 41 0.0021

LYS 41 GLU 42 -0.0002

GLU 42 ARG 43 -0.1188

ARG 43 CYS 44 -0.0001

CYS 44 PHE 45 -0.0275

PHE 45 GLN 46 -0.0002

GLN 46 GLY 47 0.0452

GLY 47 THR 48 -0.0002

THR 48 ALA 49 -0.0694

ALA 49 ASP 50 0.0002

ASP 50 PRO 51 0.0741

PRO 51 VAL 52 -0.0001

VAL 52 ARG 53 0.0629

ARG 53 VAL 54 -0.0005

VAL 54 SER 55 -0.1925

SER 55 LYS 56 -0.0002

LYS 56 VAL 57 -0.0293

VAL 57 VAL 58 0.0001

VAL 58 LYS 59 0.1152

LYS 59 GLY 60 0.0001

GLY 60 GLY 61 -0.0059

GLY 61 SER 62 0.0002

SER 62 SER 63 -0.0582

SER 63 GLY 64 0.0001

GLY 64 LYS 65 0.0185

LYS 65 GLY 66 0.0003

GLY 66 THR 67 -0.0948

THR 67 THR 68 -0.0003

THR 68 LEU 69 -0.0849

LEU 69 ARG 70 -0.0000

ARG 70 GLY 71 0.1788

GLY 71 ARG 72 -0.0001

ARG 72 SER 73 0.0698

SER 73 ASP 74 0.0004

ASP 74 ALA 75 0.1158

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 0.0925

LEU 77 VAL 78 0.0002

VAL 78 VAL 79 0.0803

VAL 79 PHE 80 0.0002

PHE 80 LEU 81 0.0502

LEU 81 THR 82 -0.0001

THR 82 LYS 83 0.0440

LYS 83 LEU 84 -0.0000

LEU 84 THR 85 -0.0232

THR 85 SER 86 -0.0003

SER 86 PHE 87 -0.0975

PHE 87 GLU 88 -0.0003

GLU 88 ASP 89 -0.0846

ASP 89 GLN 90 0.0001

GLN 90 LEU 91 -0.0081

LEU 91 ARG 92 0.0000

ARG 92 ARG 93 -0.0177

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 0.0137

GLY 95 GLU 96 0.0001

GLU 96 PHE 97 0.0094

PHE 97 ILE 98 -0.0001

ILE 98 GLN 99 0.0308

GLN 99 GLU 100 -0.0000

GLU 100 ILE 101 0.0266

ILE 101 ARG 102 -0.0001

ARG 102 ARG 103 -0.0653

ARG 103 GLN 104 0.0001

GLN 104 LEU 105 0.0257

LEU 105 GLU 106 -0.0003

GLU 106 ALA 107 -0.0051

ALA 107 CYS 108 -0.0000

CYS 108 GLN 109 -0.0439

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 0.0249

GLU 111 GLN 112 0.0002

GLN 112 LYS 113 -0.0244

LYS 113 PHE 114 -0.0002

PHE 114 LYS 115 -0.0234

LYS 115 VAL 116 0.0001

VAL 116 THR 117 -0.0461

THR 117 PHE 118 -0.0003

PHE 118 GLU 119 -0.1426

GLU 119 VAL 120 -0.0001

VAL 120 GLN 121 -0.0369

GLN 121 SER 122 0.0000

SER 122 PRO 123 0.1008

PRO 123 ARG 124 -0.0001

ARG 124 ARG 125 0.0730

ARG 125 GLU 126 -0.0002

GLU 126 ASN 127 -0.1230

ASN 127 PRO 128 -0.0000

PRO 128 ARG 129 0.0179

ARG 129 ALA 130 -0.0002

ALA 130 LEU 131 0.1997

LEU 131 SER 132 0.0001

SER 132 PHE 133 -0.0120

PHE 133 VAL 134 0.0005

VAL 134 LEU 135 0.0147

LEU 135 SER 136 -0.0003

SER 136 SER 137 -0.0193

SER 137 PRO 138 -0.0005

PRO 138 GLN 139 -0.0131

GLN 139 LEU 140 0.0001

LEU 140 GLN 141 -0.0072

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 -0.0623

GLU 143 VAL 144 -0.0001

VAL 144 GLU 145 -0.0716

GLU 145 PHE 146 0.0003

PHE 146 ASP 147 -0.0388

ASP 147 VAL 148 0.0003

VAL 148 LEU 149 0.0198

LEU 149 PRO 150 -0.0001

PRO 150 ALA 151 0.0226

ALA 151 PHE 152 -0.0002

PHE 152 ASP 153 0.0505

ASP 153 ALA 154 0.0002

ALA 154 LEU 155 0.0800

LEU 155 GLY 156 0.0002

GLY 156 GLN 157 0.0494

GLN 157 TRP 158 0.0001

TRP 158 THR 159 0.0126

THR 159 PRO 160 -0.0004

PRO 160 GLY 161 0.0067

GLY 161 TYR 162 0.0000

TYR 162 LYS 163 0.0467

LYS 163 PRO 164 0.0000

PRO 164 ASN 165 -0.0288

ASN 165 PRO 166 0.0005

PRO 166 GLU 167 0.0099

GLU 167 ILE 168 -0.0004

ILE 168 TYR 169 -0.0592

TYR 169 VAL 170 -0.0002

VAL 170 GLN 171 -0.0479

GLN 171 LEU 172 0.0004

LEU 172 ILE 173 -0.0414

ILE 173 LYS 174 0.0001

LYS 174 GLU 175 -0.0150

GLU 175 CYS 176 -0.0000

CYS 176 LYS 177 0.0040

LYS 177 SER 178 0.0003

SER 178 ARG 179 -0.0013

ARG 179 GLY 180 0.0002

GLY 180 LYS 181 0.0518

LYS 181 GLU 182 -0.0001

GLU 182 GLY 183 0.0069

GLY 183 GLU 184 0.0000

GLU 184 PHE 185 0.0020

PHE 185 SER 186 -0.0001

SER 186 THR 187 -0.0451

THR 187 CYS 188 -0.0002

CYS 188 PHE 189 -0.0076

PHE 189 THR 190 -0.0004

THR 190 GLU 191 0.0056

GLU 191 LEU 192 -0.0002

LEU 192 GLN 193 -0.0081

GLN 193 ARG 194 -0.0003

ARG 194 ARG 194 -0.1147

ARG 194 ASP 195 -0.0193

ASP 195 PHE 196 -0.0002

PHE 196 LEU 197 -0.0610

LEU 197 ARG 198 -0.0001

ARG 198 ASN 199 0.0782

ASN 199 ARG 200 0.0004

ARG 200 PRO 201 -0.0194

PRO 201 THR 202 0.0003

THR 202 LYS 203 0.0251

LYS 203 LEU 204 0.0002

LEU 204 LYS 205 0.1596

LYS 205 SER 206 0.0000

SER 206 LEU 207 0.0574

LEU 207 ILE 208 -0.0000

ILE 208 ARG 209 0.0386

ARG 209 LEU 210 0.0000

LEU 210 VAL 211 -0.0395

VAL 211 LYS 212 0.0000

LYS 212 HIS 213 0.0296

HIS 213 TRP 214 -0.0000

TRP 214 TYR 215 0.0185

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 0.0691

THR 217 CYS 218 0.0000

CYS 218 LYS 219 0.0382

LYS 219 LYS 220 -0.0003

LYS 220 THR 221 -0.0311

THR 221 HIS 222 -0.0002

HIS 222 GLY 223 0.0019

GLY 223 ASN 224 0.0000

ASN 224 LYS 225 0.0422

LYS 225 LEU 226 0.0001

LEU 226 PRO 227 0.0529

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 -0.0142

GLN 229 TYR 230 0.0000

TYR 230 ALA 231 -0.0445

ALA 231 LEU 232 -0.0005

LEU 232 GLU 233 -0.0380

GLU 233 LEU 234 0.0000

LEU 234 LEU 235 -0.0489

LEU 235 THR 236 0.0005

THR 236 VAL 237 -0.0257

VAL 237 TYR 238 0.0001

TYR 238 ALA 239 -0.1173

ALA 239 TRP 240 0.0003

TRP 240 GLU 241 -0.0481

GLU 241 GLN 242 0.0003

GLN 242 GLY 243 -0.0712

GLY 243 SER 244 -0.0003

SER 244 ARG 245 0.0329

ARG 245 LYS 246 -0.0001

LYS 246 THR 247 0.0184

THR 247 ASP 248 -0.0000

ASP 248 PHE 249 0.0017

PHE 249 SER 250 -0.0002

SER 250 THR 251 0.0307

THR 251 ALA 252 0.0004

ALA 252 GLN 253 -0.0323

GLN 253 GLY 254 0.0003

GLY 254 PHE 255 -0.0084

PHE 255 GLN 256 0.0001

GLN 256 THR 257 -0.0615

THR 257 VAL 258 0.0000

VAL 258 LEU 259 0.0335

LEU 259 GLU 260 0.0001

GLU 260 LEU 261 -0.0909

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 0.0265

LEU 263 LYS 264 0.0000

LYS 264 HIS 265 -0.0482

HIS 265 GLN 266 -0.0001

GLN 266 LYS 267 0.0737

LYS 267 LEU 268 -0.0003

LEU 268 CYS 269 -0.0452

CYS 269 ILE 270 0.0000

ILE 270 PHE 271 0.0830

PHE 271 TRP 272 -0.0001

TRP 272 GLU 273 -0.0100

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 -0.0008

TYR 275 TYR 276 0.0001

TYR 276 ASP 277 -0.0056

ASP 277 PHE 278 -0.0004

PHE 278 THR 279 0.0297

THR 279 ASN 280 -0.0003

ASN 280 PRO 281 -0.0110

PRO 281 VAL 282 -0.0002

VAL 282 VAL 283 -0.0192

VAL 283 GLY 284 -0.0003

GLY 284 ARG 285 -0.0120

ARG 285 CYS 286 0.0001

CYS 286 MET 287 -0.0951

MET 287 LEU 288 0.0001

LEU 288 GLN 289 0.0144

GLN 289 GLN 290 0.0004

GLN 290 LEU 291 -0.1398

LEU 291 LYS 292 0.0002

LYS 292 LYS 293 0.1378

LYS 293 PRO 294 0.0000

PRO 294 ARG 295 -0.0382

ARG 295 PRO 296 0.0003

PRO 296 VAL 297 -0.0021

VAL 297 ILE 298 -0.0003

ILE 298 LEU 299 -0.0490

LEU 299 ASP 300 -0.0004

ASP 300 PRO 301 0.0155

PRO 301 ALA 302 0.0002

ALA 302 ASP 303 -0.0072

ASP 303 PRO 304 0.0002

PRO 304 THR 305 0.0183

THR 305 GLY 306 0.0002

GLY 306 ASN 307 -0.2027

ASN 307 VAL 308 0.0003

VAL 308 GLY 309 -0.1000

GLY 309 GLY 310 0.0001

GLY 310 GLY 311 0.0550

GLY 311 ASP 312 0.0001

ASP 312 THR 313 -0.0337

THR 313 HIS 314 0.0001

HIS 314 SER 315 -0.0458

SER 315 TRP 316 0.0002

TRP 316 GLN 317 -0.0248

GLN 317 ARG 318 -0.0003

ARG 318 LEU 319 0.0076

LEU 319 ALA 320 0.0000

ALA 320 GLN 321 -0.0203

GLN 321 GLU 322 -0.0003

GLU 322 ALA 323 0.0189

ALA 323 ARG 324 -0.0003

ARG 324 VAL 325 -0.0456

VAL 325 TRP 326 0.0000

TRP 326 LEU 327 0.0252

LEU 327 GLY 328 -0.0003

GLY 328 TYR 329 -0.0091

TYR 329 PRO 330 0.0003

PRO 330 CYS 331 -0.0255

CYS 331 CYS 332 0.0001

CYS 332 LYS 333 -0.0248

LYS 333 ASN 334 -0.0004

ASN 334 LEU 335 -0.1407

LEU 335 ASP 336 0.0002

ASP 336 GLY 337 0.0507

GLY 337 SER 338 0.0001

SER 338 LEU 339 -0.0503

LEU 339 VAL 340 0.0003

VAL 340 GLY 341 -0.1586

GLY 341 ALA 342 -0.0002

ALA 342 TRP 343 -0.0584

TRP 343 THR 344 0.0002

THR 344 MET 345 -0.1040

MET 345 LEU 346 -0.0005

LEU 346 GLN 347 -0.0152

GLN 347 LYS 348 0.0002

LYS 348 ILE 349 -0.0295

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 22122720105119216

--- normal mode 10 ---

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

* *