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

* *

CA strain for 22122720180123252

--- 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 0.0003

GLU 2 LEU 3 -0.0217

LEU 3 ARG 4 -0.0002

ARG 4 HIS 5 0.0277

HIS 5 THR 6 -0.0002

THR 6 PRO 7 0.0322

PRO 7 ALA 8 0.0002

ALA 8 ARG 9 -0.0434

ARG 9 ASP 10 0.0001

ASP 10 LEU 11 0.0096

LEU 11 ASP 12 -0.0000

ASP 12 LYS 13 -0.0855

LYS 13 PHE 14 0.0002

PHE 14 ILE 15 -0.0081

ILE 15 GLU 16 -0.0001

GLU 16 ASP 17 -0.0891

ASP 17 HIS 18 -0.0000

HIS 18 LEU 19 -0.0165

LEU 19 LEU 20 -0.0001

LEU 20 PRO 21 0.3035

PRO 21 ASN 22 -0.0006

ASN 22 THR 23 0.0538

THR 23 CYS 24 -0.0003

CYS 24 PHE 25 -0.1095

PHE 25 ARG 26 -0.0000

ARG 26 THR 27 0.0197

THR 27 GLN 28 0.0001

GLN 28 VAL 29 -0.0798

VAL 29 LYS 30 -0.0002

LYS 30 GLU 31 -0.0844

GLU 31 ALA 32 0.0001

ALA 32 ILE 33 -0.0940

ILE 33 ASP 34 0.0002

ASP 34 ILE 35 -0.0780

ILE 35 VAL 36 0.0002

VAL 36 CYS 37 -0.0815

CYS 37 ARG 38 -0.0000

ARG 38 PHE 39 -0.0096

PHE 39 LEU 40 -0.0000

LEU 40 LYS 41 0.0044

LYS 41 GLU 42 -0.0003

GLU 42 ARG 43 -0.1138

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 -0.0340

PHE 45 GLN 46 -0.0003

GLN 46 GLY 47 0.0487

GLY 47 THR 48 0.0002

THR 48 ALA 49 -0.0534

ALA 49 ASP 50 -0.0005

ASP 50 PRO 51 0.0679

PRO 51 VAL 52 0.0002

VAL 52 ARG 53 0.0638

ARG 53 VAL 54 0.0000

VAL 54 SER 55 -0.1770

SER 55 LYS 56 0.0000

LYS 56 VAL 57 -0.0343

VAL 57 VAL 58 0.0002

VAL 58 LYS 59 0.0989

LYS 59 GLY 60 -0.0000

GLY 60 GLY 61 -0.0038

GLY 61 SER 62 -0.0003

SER 62 SER 63 -0.0458

SER 63 GLY 64 0.0002

GLY 64 LYS 65 0.0157

LYS 65 GLY 66 -0.0004

GLY 66 THR 67 -0.0903

THR 67 THR 68 -0.0001

THR 68 LEU 69 -0.0826

LEU 69 ARG 70 0.0000

ARG 70 GLY 71 0.1667

GLY 71 ARG 72 -0.0002

ARG 72 SER 73 0.0729

SER 73 ASP 74 -0.0000

ASP 74 ALA 75 0.1129

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 0.0852

LEU 77 VAL 78 0.0001

VAL 78 VAL 79 0.0676

VAL 79 PHE 80 -0.0004

PHE 80 LEU 81 0.0445

LEU 81 THR 82 -0.0002

THR 82 LYS 83 0.0429

LYS 83 LEU 84 0.0001

LEU 84 THR 85 -0.0173

THR 85 SER 86 0.0001

SER 86 PHE 87 -0.0976

PHE 87 GLU 88 -0.0001

GLU 88 ASP 89 -0.0879

ASP 89 GLN 90 0.0000

GLN 90 LEU 91 -0.0107

LEU 91 ARG 92 -0.0003

ARG 92 ARG 93 -0.0280

ARG 93 ARG 94 -0.0000

ARG 94 GLY 95 0.0317

GLY 95 GLU 96 0.0003

GLU 96 PHE 97 0.0248

PHE 97 ILE 98 0.0000

ILE 98 GLN 99 0.0236

GLN 99 GLU 100 0.0001

GLU 100 ILE 101 0.0258

ILE 101 ARG 102 0.0002

ARG 102 ARG 103 -0.0687

ARG 103 GLN 104 -0.0001

GLN 104 LEU 105 0.0228

LEU 105 GLU 106 0.0002

GLU 106 ALA 107 -0.0072

ALA 107 CYS 108 -0.0000

CYS 108 GLN 109 -0.0475

GLN 109 ARG 110 0.0003

ARG 110 GLU 111 0.0206

GLU 111 GLN 112 -0.0001

GLN 112 LYS 113 -0.0214

LYS 113 PHE 114 0.0003

PHE 114 LYS 115 -0.0332

LYS 115 VAL 116 -0.0000

VAL 116 THR 117 -0.0729

THR 117 PHE 118 0.0001

PHE 118 GLY 119 0.0265

GLY 119 VAL 120 0.0001

VAL 120 GLN 121 -0.0011

GLN 121 SER 122 0.0000

SER 122 PRO 123 -0.0571

PRO 123 ARG 124 0.0001

ARG 124 ARG 125 0.0160

ARG 125 GLU 126 0.0000

GLU 126 GLY 127 0.0458

GLY 127 PRO 128 0.0002

PRO 128 ARG 129 0.0123

ARG 129 ALA 130 -0.0000

ALA 130 LEU 131 0.2185

LEU 131 SER 132 -0.0000

SER 132 PHE 133 0.0018

PHE 133 VAL 134 -0.0002

VAL 134 LEU 135 0.0061

LEU 135 SER 136 -0.0002

SER 136 SER 137 -0.0248

SER 137 PRO 138 0.0005

PRO 138 GLN 139 -0.0116

GLN 139 LEU 140 0.0002

LEU 140 GLN 141 -0.0069

GLN 141 GLN 142 -0.0002

GLN 142 GLU 143 -0.0652

GLU 143 VAL 144 0.0002

VAL 144 GLU 145 -0.0983

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 -0.0201

ASP 147 VAL 148 0.0003

VAL 148 LEU 149 0.0282

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 0.0348

ALA 151 PHE 152 0.0003

PHE 152 ASP 153 0.0575

ASP 153 ALA 154 0.0001

ALA 154 LEU 155 0.0730

LEU 155 GLY 156 0.0003

GLY 156 GLN 157 0.0480

GLN 157 TRP 158 0.0001

TRP 158 THR 159 0.0160

THR 159 PRO 160 -0.0003

PRO 160 GLY 161 0.0062

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 0.0460

LYS 163 PRO 164 0.0004

PRO 164 ASN 165 -0.0343

ASN 165 PRO 166 0.0000

PRO 166 GLU 167 0.0055

GLU 167 ILE 168 0.0002

ILE 168 TYR 169 -0.0528

TYR 169 VAL 170 0.0000

VAL 170 GLN 171 -0.0347

GLN 171 LEU 172 -0.0002

LEU 172 ILE 173 -0.0395

ILE 173 LYS 174 -0.0001

LYS 174 GLU 175 -0.0147

GLU 175 CYS 176 0.0000

CYS 176 LYS 177 0.0127

LYS 177 SER 178 0.0000

SER 178 ARG 179 -0.0011

ARG 179 GLY 180 -0.0004

GLY 180 LYS 181 0.0579

LYS 181 GLU 182 -0.0003

GLU 182 GLY 183 0.0040

GLY 183 GLU 184 -0.0002

GLU 184 PHE 185 -0.0008

PHE 185 SER 186 0.0002

SER 186 THR 187 -0.0445

THR 187 CYS 188 0.0005

CYS 188 PHE 189 -0.0086

PHE 189 THR 190 0.0001

THR 190 GLU 191 0.0029

GLU 191 LEU 192 -0.0002

LEU 192 GLN 193 -0.0041

GLN 193 ARG 194 -0.0002

ARG 194 ARG 194 0.0381

ARG 194 ASP 195 -0.0196

ASP 195 PHE 196 -0.0004

PHE 196 LEU 197 -0.0719

LEU 197 ARG 198 -0.0000

ARG 198 ASN 199 0.0772

ASN 199 ARG 200 -0.0004

ARG 200 PRO 201 -0.0375

PRO 201 THR 202 0.0002

THR 202 LYS 203 0.0101

LYS 203 LEU 204 -0.0000

LEU 204 LYS 205 0.1548

LYS 205 SER 206 0.0001

SER 206 LEU 207 0.0521

LEU 207 ILE 208 0.0001

ILE 208 ARG 209 0.0373

ARG 209 LEU 210 0.0002

LEU 210 VAL 211 -0.0346

VAL 211 LYS 212 0.0001

LYS 212 HIS 213 0.0280

HIS 213 TRP 214 0.0000

TRP 214 TYR 215 0.0160

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 0.0713

THR 217 CYS 218 0.0001

CYS 218 LYS 219 0.0207

LYS 219 LYS 220 0.0003

LYS 220 THR 221 -0.0233

THR 221 HIS 222 -0.0002

HIS 222 GLY 223 -0.0168

GLY 223 ASN 224 -0.0001

ASN 224 LYS 225 0.0457

LYS 225 LEU 226 0.0002

LEU 226 PRO 227 0.0723

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 -0.0204

GLN 229 TYR 230 0.0000

TYR 230 ALA 231 -0.0424

ALA 231 LEU 232 0.0003

LEU 232 GLU 233 -0.0355

GLU 233 LEU 234 -0.0001

LEU 234 LEU 235 -0.0438

LEU 235 THR 236 -0.0001

THR 236 VAL 237 -0.0274

VAL 237 TYR 238 0.0003

TYR 238 ALA 239 -0.1184

ALA 239 TRP 240 -0.0001

TRP 240 GLU 241 -0.0447

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 -0.0733

GLY 243 SER 244 -0.0000

SER 244 ARG 245 0.0261

ARG 245 LYS 246 0.0002

LYS 246 THR 247 0.0215

THR 247 ASP 248 0.0001

ASP 248 PHE 249 -0.0058

PHE 249 SER 250 -0.0004

SER 250 THR 251 0.0335

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 -0.0282

GLN 253 GLY 254 -0.0003

GLY 254 PHE 255 -0.0114

PHE 255 GLN 256 -0.0000

GLN 256 THR 257 -0.0619

THR 257 VAL 258 -0.0002

VAL 258 LEU 259 0.0243

LEU 259 GLU 260 -0.0000

GLU 260 LEU 261 -0.0821

LEU 261 VAL 262 -0.0003

VAL 262 LEU 263 0.0223

LEU 263 LYS 264 0.0001

LYS 264 HIS 265 -0.0406

HIS 265 GLN 266 0.0003

GLN 266 LYS 267 0.0581

LYS 267 LEU 268 -0.0003

LEU 268 CYS 269 -0.0463

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0765

PHE 271 TRP 272 0.0001

TRP 272 GLU 273 -0.0206

GLU 273 ALA 274 0.0000

ALA 274 TYR 275 -0.0019

TYR 275 TYR 276 0.0000

TYR 276 ASP 277 -0.0023

ASP 277 PHE 278 -0.0002

PHE 278 THR 279 0.0279

THR 279 ASN 280 0.0001

ASN 280 PRO 281 -0.0061

PRO 281 VAL 282 0.0003

VAL 282 VAL 283 -0.0222

VAL 283 GLY 284 0.0001

GLY 284 ARG 285 -0.0133

ARG 285 CYS 286 -0.0004

CYS 286 MET 287 -0.0942

MET 287 LEU 288 0.0006

LEU 288 GLN 289 0.0072

GLN 289 GLN 290 0.0000

GLN 290 LEU 291 -0.1455

LEU 291 LYS 292 -0.0001

LYS 292 LYS 293 0.1328

LYS 293 PRO 294 0.0001

PRO 294 ARG 295 -0.0272

ARG 295 PRO 296 -0.0002

PRO 296 VAL 297 0.0095

VAL 297 ILE 298 -0.0004

ILE 298 LEU 299 -0.0384

LEU 299 ASP 300 0.0003

ASP 300 PRO 301 0.0209

PRO 301 ALA 302 -0.0002

ALA 302 ASP 303 -0.0154

ASP 303 PRO 304 0.0001

PRO 304 THR 305 0.0030

THR 305 GLY 306 0.0000

GLY 306 ASN 307 -0.1649

ASN 307 VAL 308 -0.0000

VAL 308 GLY 309 -0.0816

GLY 309 GLY 310 0.0001

GLY 310 GLY 311 0.0409

GLY 311 ASP 312 -0.0004

ASP 312 THR 313 -0.0320

THR 313 HIS 314 -0.0001

HIS 314 SER 315 -0.0444

SER 315 TRP 316 0.0001

TRP 316 GLN 317 -0.0217

GLN 317 ARG 318 0.0002

ARG 318 LEU 319 0.0048

LEU 319 ALA 320 0.0000

ALA 320 GLN 321 -0.0249

GLN 321 GLU 322 -0.0001

GLU 322 ALA 323 0.0089

ALA 323 ARG 324 0.0000

ARG 324 VAL 325 -0.0408

VAL 325 TRP 326 0.0004

TRP 326 LEU 327 0.0215

LEU 327 GLY 328 -0.0001

GLY 328 TYR 329 -0.0069

TYR 329 PRO 330 0.0002

PRO 330 CYS 331 -0.0258

CYS 331 CYS 332 0.0004

CYS 332 LYS 333 -0.0246

LYS 333 ASN 334 0.0003

ASN 334 LEU 335 -0.1337

LEU 335 ASP 336 0.0000

ASP 336 GLY 337 0.0574

GLY 337 SER 338 0.0000

SER 338 LEU 339 -0.0442

LEU 339 VAL 340 -0.0004

VAL 340 GLY 341 -0.1493

GLY 341 ALA 342 -0.0001

ALA 342 TRP 343 -0.0637

TRP 343 THR 344 -0.0000

THR 344 MET 345 -0.1010

MET 345 LEU 346 -0.0000

LEU 346 GLN 347 -0.0129

GLN 347 LYS 348 0.0002

LYS 348 ILE 349 -0.0209

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 22122720180123252

--- normal mode 10 ---

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

* *