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

* *

CA strain for 22122720105119216

--- normal mode 9 ---

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 0.0001

GLU 2 LEU 3 0.0191

LEU 3 ARG 4 -0.0005

ARG 4 HIS 5 -0.0166

HIS 5 THR 6 -0.0001

THR 6 PRO 7 -0.0231

PRO 7 ALA 8 0.0004

ALA 8 ARG 9 0.0063

ARG 9 ASP 10 0.0000

ASP 10 LEU 11 0.0002

LEU 11 ASP 12 -0.0002

ASP 12 LYS 13 -0.0048

LYS 13 PHE 14 -0.0002

PHE 14 ILE 15 0.0078

ILE 15 GLU 16 0.0000

GLU 16 ASP 17 0.0198

ASP 17 HIS 18 -0.0001

HIS 18 LEU 19 0.0051

LEU 19 LEU 20 -0.0004

LEU 20 PRO 21 -0.0788

PRO 21 ASN 22 0.0000

ASN 22 THR 23 -0.0071

THR 23 CYS 24 0.0000

CYS 24 PHE 25 0.0166

PHE 25 ARG 26 -0.0003

ARG 26 THR 27 -0.0545

THR 27 GLN 28 -0.0003

GLN 28 VAL 29 0.0372

VAL 29 LYS 30 0.0003

LYS 30 GLU 31 0.0104

GLU 31 ALA 32 -0.0003

ALA 32 ILE 33 0.0360

ILE 33 ASP 34 -0.0001

ASP 34 ILE 35 0.0076

ILE 35 VAL 36 0.0000

VAL 36 CYS 37 0.0434

CYS 37 ARG 38 -0.0004

ARG 38 PHE 39 -0.0420

PHE 39 LEU 40 0.0003

LEU 40 LYS 41 0.0135

LYS 41 GLU 42 -0.0000

GLU 42 ARG 43 0.0004

ARG 43 CYS 44 -0.0002

CYS 44 PHE 45 0.0292

PHE 45 GLN 46 -0.0002

GLN 46 GLY 47 -0.0397

GLY 47 THR 48 0.0001

THR 48 ALA 49 -0.0340

ALA 49 ASP 50 -0.0001

ASP 50 PRO 51 -0.0179

PRO 51 VAL 52 -0.0003

VAL 52 ARG 53 -0.0277

ARG 53 VAL 54 0.0003

VAL 54 SER 55 -0.0175

SER 55 LYS 56 0.0003

LYS 56 VAL 57 0.0053

VAL 57 VAL 58 0.0003

VAL 58 LYS 59 -0.0920

LYS 59 GLY 60 0.0001

GLY 60 GLY 61 -0.0667

GLY 61 SER 62 0.0005

SER 62 SER 63 -0.0619

SER 63 GLY 64 0.0002

GLY 64 LYS 65 0.0124

LYS 65 GLY 66 0.0002

GLY 66 THR 67 -0.0313

THR 67 THR 68 -0.0002

THR 68 LEU 69 -0.0090

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 -0.0184

GLY 71 ARG 72 -0.0000

ARG 72 SER 73 -0.0652

SER 73 ASP 74 -0.0004

ASP 74 ALA 75 -0.1086

ALA 75 ASP 76 -0.0002

ASP 76 LEU 77 -0.0633

LEU 77 VAL 78 -0.0002

VAL 78 VAL 79 -0.0088

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 -0.0256

LEU 81 THR 82 0.0000

THR 82 LYS 83 -0.0246

LYS 83 LEU 84 -0.0003

LEU 84 THR 85 0.0047

THR 85 SER 86 -0.0001

SER 86 PHE 87 0.0238

PHE 87 GLU 88 0.0003

GLU 88 ASP 89 0.0524

ASP 89 GLN 90 0.0000

GLN 90 LEU 91 -0.0287

LEU 91 ARG 92 0.0001

ARG 92 ARG 93 0.0472

ARG 93 ARG 94 -0.0004

ARG 94 GLY 95 -0.0226

GLY 95 GLU 96 0.0002

GLU 96 PHE 97 -0.0420

PHE 97 ILE 98 0.0000

ILE 98 GLN 99 0.0500

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 0.0062

ILE 101 ARG 102 0.0002

ARG 102 ARG 103 -0.0715

ARG 103 GLN 104 -0.0004

GLN 104 LEU 105 0.0279

LEU 105 GLU 106 0.0002

GLU 106 ALA 107 -0.0296

ALA 107 CYS 108 -0.0001

CYS 108 GLN 109 0.0361

GLN 109 ARG 110 -0.0001

ARG 110 GLU 111 -0.0049

GLU 111 GLN 112 -0.0002

GLN 112 LYS 113 0.0007

LYS 113 PHE 114 0.0005

PHE 114 LYS 115 -0.0034

LYS 115 VAL 116 0.0000

VAL 116 THR 117 -0.0284

THR 117 PHE 118 0.0003

PHE 118 GLU 119 -0.1558

GLU 119 VAL 120 -0.0003

VAL 120 GLN 121 -0.0815

GLN 121 SER 122 -0.0001

SER 122 PRO 123 0.3336

PRO 123 ARG 124 -0.0003

ARG 124 ARG 125 0.0836

ARG 125 GLU 126 0.0000

GLU 126 ASN 127 -0.1453

ASN 127 PRO 128 -0.0002

PRO 128 ARG 129 0.1463

ARG 129 ALA 130 0.0000

ALA 130 LEU 131 -0.0444

LEU 131 SER 132 -0.0002

SER 132 PHE 133 -0.0840

PHE 133 VAL 134 0.0003

VAL 134 LEU 135 0.0981

LEU 135 SER 136 -0.0002

SER 136 SER 137 0.0184

SER 137 PRO 138 -0.0000

PRO 138 GLN 139 0.0005

GLN 139 LEU 140 -0.0002

LEU 140 GLN 141 0.0073

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 0.0645

GLU 143 VAL 144 0.0000

VAL 144 GLU 145 0.0863

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 -0.0549

ASP 147 VAL 148 -0.0001

VAL 148 LEU 149 -0.0341

LEU 149 PRO 150 0.0001

PRO 150 ALA 151 -0.0047

ALA 151 PHE 152 -0.0001

PHE 152 ASP 153 -0.0260

ASP 153 ALA 154 -0.0003

ALA 154 LEU 155 -0.0217

LEU 155 GLY 156 -0.0001

GLY 156 GLN 157 -0.0240

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 -0.0142

THR 159 PRO 160 -0.0004

PRO 160 GLY 161 -0.0025

GLY 161 TYR 162 -0.0001

TYR 162 LYS 163 -0.0140

LYS 163 PRO 164 0.0002

PRO 164 ASN 165 0.0120

ASN 165 PRO 166 0.0004

PRO 166 GLU 167 0.0073

GLU 167 ILE 168 -0.0002

ILE 168 TYR 169 -0.0008

TYR 169 VAL 170 -0.0002

VAL 170 GLN 171 0.0028

GLN 171 LEU 172 0.0003

LEU 172 ILE 173 0.0191

ILE 173 LYS 174 -0.0004

LYS 174 GLU 175 0.0199

GLU 175 CYS 176 0.0001

CYS 176 LYS 177 -0.0168

LYS 177 SER 178 0.0001

SER 178 ARG 179 0.0033

ARG 179 GLY 180 0.0004

GLY 180 LYS 181 -0.0214

LYS 181 GLU 182 -0.0003

GLU 182 GLY 183 -0.0077

GLY 183 GLU 184 0.0001

GLU 184 PHE 185 0.0088

PHE 185 SER 186 -0.0001

SER 186 THR 187 0.0091

THR 187 CYS 188 0.0003

CYS 188 PHE 189 0.0164

PHE 189 THR 190 -0.0001

THR 190 GLU 191 0.0239

GLU 191 LEU 192 -0.0001

LEU 192 GLN 193 -0.0398

GLN 193 ARG 194 0.0001

ARG 194 ARG 194 0.0000

ARG 194 ASP 195 0.0121

ASP 195 PHE 196 0.0002

PHE 196 LEU 197 0.0304

LEU 197 ARG 198 0.0001

ARG 198 ASN 199 0.0050

ASN 199 ARG 200 0.0000

ARG 200 PRO 201 0.0688

PRO 201 THR 202 0.0001

THR 202 LYS 203 0.0427

LYS 203 LEU 204 -0.0001

LEU 204 LYS 205 -0.0182

LYS 205 SER 206 -0.0000

SER 206 LEU 207 -0.0078

LEU 207 ILE 208 -0.0000

ILE 208 ARG 209 -0.0065

ARG 209 LEU 210 0.0003

LEU 210 VAL 211 0.0131

VAL 211 LYS 212 0.0001

LYS 212 HIS 213 -0.0133

HIS 213 TRP 214 0.0002

TRP 214 TYR 215 0.0179

TYR 215 GLN 216 -0.0000

GLN 216 THR 217 -0.0548

THR 217 CYS 218 0.0001

CYS 218 LYS 219 0.0560

LYS 219 LYS 220 -0.0001

LYS 220 THR 221 -0.0167

THR 221 HIS 222 0.0001

HIS 222 GLY 223 0.0656

GLY 223 ASN 224 0.0001

ASN 224 LYS 225 -0.0119

LYS 225 LEU 226 0.0001

LEU 226 PRO 227 -0.1074

PRO 227 PRO 228 0.0002

PRO 228 GLN 229 0.0504

GLN 229 TYR 230 -0.0002

TYR 230 ALA 231 0.0042

ALA 231 LEU 232 0.0004

LEU 232 GLU 233 -0.0240

GLU 233 LEU 234 -0.0003

LEU 234 LEU 235 -0.0029

LEU 235 THR 236 0.0001

THR 236 VAL 237 0.0272

VAL 237 TYR 238 -0.0000

TYR 238 ALA 239 0.0657

ALA 239 TRP 240 -0.0002

TRP 240 GLU 241 0.0129

GLU 241 GLN 242 -0.0002

GLN 242 GLY 243 0.0414

GLY 243 SER 244 -0.0000

SER 244 ARG 245 0.0169

ARG 245 LYS 246 0.0000

LYS 246 THR 247 -0.0135

THR 247 ASP 248 0.0001

ASP 248 PHE 249 0.0383

PHE 249 SER 250 -0.0006

SER 250 THR 251 -0.0306

THR 251 ALA 252 0.0001

ALA 252 GLN 253 -0.0051

GLN 253 GLY 254 -0.0002

GLY 254 PHE 255 0.0191

PHE 255 GLN 256 0.0001

GLN 256 THR 257 0.0334

THR 257 VAL 258 0.0003

VAL 258 LEU 259 0.0187

LEU 259 GLU 260 -0.0003

GLU 260 LEU 261 0.0208

LEU 261 VAL 262 -0.0000

VAL 262 LEU 263 -0.0100

LEU 263 LYS 264 -0.0006

LYS 264 HIS 265 -0.0058

HIS 265 GLN 266 -0.0002

GLN 266 LYS 267 0.0282

LYS 267 LEU 268 -0.0001

LEU 268 CYS 269 0.0730

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0352

PHE 271 TRP 272 -0.0002

TRP 272 GLU 273 0.0469

GLU 273 ALA 274 -0.0002

ALA 274 TYR 275 0.0202

TYR 275 TYR 276 -0.0000

TYR 276 ASP 277 -0.0112

ASP 277 PHE 278 0.0000

PHE 278 THR 279 0.0108

THR 279 ASN 280 0.0004

ASN 280 PRO 281 -0.0129

PRO 281 VAL 282 0.0001

VAL 282 VAL 283 0.0080

VAL 283 GLY 284 0.0000

GLY 284 ARG 285 -0.0021

ARG 285 CYS 286 -0.0000

CYS 286 MET 287 0.0351

MET 287 LEU 288 -0.0002

LEU 288 GLN 289 0.0049

GLN 289 GLN 290 0.0002

GLN 290 LEU 291 0.0603

LEU 291 LYS 292 0.0004

LYS 292 LYS 293 -0.0138

LYS 293 PRO 294 -0.0003

PRO 294 ARG 295 -0.0206

ARG 295 PRO 296 -0.0002

PRO 296 VAL 297 -0.0275

VAL 297 ILE 298 -0.0002

ILE 298 LEU 299 -0.0153

LEU 299 ASP 300 -0.0002

ASP 300 PRO 301 -0.0217

PRO 301 ALA 302 0.0004

ALA 302 ASP 303 0.0377

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 0.0447

THR 305 GLY 306 -0.0000

GLY 306 ASN 307 -0.0828

ASN 307 VAL 308 0.0002

VAL 308 GLY 309 -0.0519

GLY 309 GLY 310 -0.0002

GLY 310 GLY 311 0.0447

GLY 311 ASP 312 -0.0001

ASP 312 THR 313 0.0002

THR 313 HIS 314 0.0000

HIS 314 SER 315 0.0057

SER 315 TRP 316 -0.0002

TRP 316 GLN 317 -0.0051

GLN 317 ARG 318 0.0000

ARG 318 LEU 319 -0.0012

LEU 319 ALA 320 -0.0000

ALA 320 GLN 321 0.0241

GLN 321 GLU 322 -0.0004

GLU 322 ALA 323 0.0317

ALA 323 ARG 324 -0.0002

ARG 324 VAL 325 0.0060

VAL 325 TRP 326 -0.0000

TRP 326 LEU 327 -0.0040

LEU 327 GLY 328 -0.0002

GLY 328 TYR 329 -0.0013

TYR 329 PRO 330 0.0002

PRO 330 CYS 331 0.0070

CYS 331 CYS 332 0.0003

CYS 332 LYS 333 0.0092

LYS 333 ASN 334 -0.0002

ASN 334 LEU 335 0.0559

LEU 335 ASP 336 0.0002

ASP 336 GLY 337 -0.0585

GLY 337 SER 338 -0.0001

SER 338 LEU 339 0.0122

LEU 339 VAL 340 -0.0002

VAL 340 GLY 341 0.0547

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 0.0609

TRP 343 THR 344 -0.0001

THR 344 MET 345 0.0373

MET 345 LEU 346 -0.0001

LEU 346 GLN 347 0.0014

GLN 347 LYS 348 -0.0000

LYS 348 ILE 349 -0.0006

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 9 ---

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

* *