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

* *

CA strain for 22122720180123252

--- normal mode 8 ---

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 0.0080

LEU 3 ARG 4 -0.0003

ARG 4 HIS 5 0.0177

HIS 5 THR 6 0.0000

THR 6 PRO 7 -0.0036

PRO 7 ALA 8 -0.0002

ALA 8 ARG 9 0.0035

ARG 9 ASP 10 0.0002

ASP 10 LEU 11 -0.0051

LEU 11 ASP 12 -0.0001

ASP 12 LYS 13 -0.0106

LYS 13 PHE 14 0.0002

PHE 14 ILE 15 -0.0302

ILE 15 GLU 16 0.0000

GLU 16 ASP 17 -0.0367

ASP 17 HIS 18 -0.0002

HIS 18 LEU 19 0.0044

LEU 19 LEU 20 0.0000

LEU 20 PRO 21 0.0708

PRO 21 ASN 22 -0.0003

ASN 22 THR 23 -0.0078

THR 23 CYS 24 -0.0001

CYS 24 PHE 25 -0.0588

PHE 25 ARG 26 -0.0003

ARG 26 THR 27 -0.0388

THR 27 GLN 28 0.0001

GLN 28 VAL 29 0.0163

VAL 29 LYS 30 0.0003

LYS 30 GLU 31 0.0438

GLU 31 ALA 32 -0.0002

ALA 32 ILE 33 0.0475

ILE 33 ASP 34 0.0003

ASP 34 ILE 35 0.0335

ILE 35 VAL 36 -0.0001

VAL 36 CYS 37 0.0482

CYS 37 ARG 38 -0.0003

ARG 38 PHE 39 -0.0320

PHE 39 LEU 40 0.0003

LEU 40 LYS 41 0.0040

LYS 41 GLU 42 -0.0002

GLU 42 ARG 43 0.0519

ARG 43 CYS 44 0.0002

CYS 44 PHE 45 0.0219

PHE 45 GLN 46 -0.0003

GLN 46 GLY 47 -0.0247

GLY 47 THR 48 -0.0000

THR 48 ALA 49 0.0412

ALA 49 ASP 50 0.0004

ASP 50 PRO 51 -0.0220

PRO 51 VAL 52 0.0002

VAL 52 ARG 53 -0.0336

ARG 53 VAL 54 -0.0001

VAL 54 SER 55 0.0914

SER 55 LYS 56 0.0001

LYS 56 VAL 57 0.0298

VAL 57 VAL 58 0.0006

VAL 58 LYS 59 -0.0684

LYS 59 GLY 60 0.0002

GLY 60 GLY 61 0.0471

GLY 61 SER 62 0.0000

SER 62 SER 63 -0.0424

SER 63 GLY 64 -0.0000

GLY 64 LYS 65 0.0062

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 -0.0465

THR 67 THR 68 0.0001

THR 68 LEU 69 -0.0151

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 0.1433

GLY 71 ARG 72 0.0001

ARG 72 SER 73 0.1128

SER 73 ASP 74 -0.0002

ASP 74 ALA 75 0.0328

ALA 75 ASP 76 -0.0000

ASP 76 LEU 77 0.0428

LEU 77 VAL 78 -0.0000

VAL 78 VAL 79 -0.0142

VAL 79 PHE 80 -0.0004

PHE 80 LEU 81 -0.0292

LEU 81 THR 82 0.0000

THR 82 LYS 83 -0.0269

LYS 83 LEU 84 0.0001

LEU 84 THR 85 0.0183

THR 85 SER 86 -0.0000

SER 86 PHE 87 0.0429

PHE 87 GLU 88 0.0002

GLU 88 ASP 89 0.0173

ASP 89 GLN 90 0.0000

GLN 90 LEU 91 0.0041

LEU 91 ARG 92 0.0000

ARG 92 ARG 93 -0.0248

ARG 93 ARG 94 0.0002

ARG 94 GLY 95 -0.0414

GLY 95 GLU 96 -0.0001

GLU 96 PHE 97 -0.0047

PHE 97 ILE 98 -0.0003

ILE 98 GLN 99 0.0030

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 0.0217

ILE 101 ARG 102 0.0002

ARG 102 ARG 103 0.0404

ARG 103 GLN 104 -0.0004

GLN 104 LEU 105 0.0263

LEU 105 GLU 106 0.0002

GLU 106 ALA 107 0.0107

ALA 107 CYS 108 -0.0000

CYS 108 GLN 109 0.0310

GLN 109 ARG 110 0.0004

ARG 110 GLU 111 -0.0062

GLU 111 GLN 112 0.0004

GLN 112 LYS 113 0.0194

LYS 113 PHE 114 -0.0002

PHE 114 LYS 115 -0.0137

LYS 115 VAL 116 -0.0001

VAL 116 THR 117 0.0044

THR 117 PHE 118 -0.0003

PHE 118 GLY 119 0.1070

GLY 119 VAL 120 0.0002

VAL 120 GLN 121 -0.0772

GLN 121 SER 122 0.0000

SER 122 PRO 123 0.0870

PRO 123 ARG 124 0.0001

ARG 124 ARG 125 0.0368

ARG 125 GLU 126 0.0001

GLU 126 GLY 127 -0.1079

GLY 127 PRO 128 -0.0001

PRO 128 ARG 129 0.0213

ARG 129 ALA 130 0.0001

ALA 130 LEU 131 -0.2474

LEU 131 SER 132 -0.0001

SER 132 PHE 133 -0.0768

PHE 133 VAL 134 0.0002

VAL 134 LEU 135 -0.0083

LEU 135 SER 136 -0.0000

SER 136 SER 137 -0.0307

SER 137 PRO 138 -0.0003

PRO 138 GLN 139 0.0094

GLN 139 LEU 140 0.0001

LEU 140 GLN 141 0.0064

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 0.0308

GLU 143 VAL 144 -0.0001

VAL 144 GLU 145 -0.0412

GLU 145 PHE 146 -0.0002

PHE 146 ASP 147 -0.0172

ASP 147 VAL 148 -0.0004

VAL 148 LEU 149 -0.0085

LEU 149 PRO 150 -0.0006

PRO 150 ALA 151 -0.0217

ALA 151 PHE 152 0.0002

PHE 152 ASP 153 -0.0324

ASP 153 ALA 154 0.0004

ALA 154 LEU 155 -0.0814

LEU 155 GLY 156 0.0001

GLY 156 GLN 157 -0.0185

GLN 157 TRP 158 0.0001

TRP 158 THR 159 -0.0050

THR 159 PRO 160 0.0002

PRO 160 GLY 161 0.0053

GLY 161 TYR 162 -0.0001

TYR 162 LYS 163 0.0234

LYS 163 PRO 164 -0.0004

PRO 164 ASN 165 0.0045

ASN 165 PRO 166 -0.0001

PRO 166 GLU 167 -0.0345

GLU 167 ILE 168 0.0001

ILE 168 TYR 169 0.0286

TYR 169 VAL 170 -0.0001

VAL 170 GLN 171 -0.0060

GLN 171 LEU 172 -0.0000

LEU 172 ILE 173 -0.0063

ILE 173 LYS 174 -0.0001

LYS 174 GLU 175 -0.0384

GLU 175 CYS 176 0.0004

CYS 176 LYS 177 0.0167

LYS 177 SER 178 -0.0001

SER 178 ARG 179 -0.0332

ARG 179 GLY 180 -0.0003

GLY 180 LYS 181 -0.0119

LYS 181 GLU 182 -0.0001

GLU 182 GLY 183 0.0030

GLY 183 GLU 184 -0.0000

GLU 184 PHE 185 0.0296

PHE 185 SER 186 -0.0003

SER 186 THR 187 -0.0911

THR 187 CYS 188 0.0000

CYS 188 PHE 189 -0.0169

PHE 189 THR 190 0.0003

THR 190 GLU 191 0.0080

GLU 191 LEU 192 -0.0002

LEU 192 GLN 193 -0.0042

GLN 193 ARG 194 0.0001

ARG 194 ARG 194 0.1147

ARG 194 ASP 195 0.0092

ASP 195 PHE 196 0.0001

PHE 196 LEU 197 -0.0605

LEU 197 ARG 198 -0.0002

ARG 198 ASN 199 0.0365

ASN 199 ARG 200 0.0005

ARG 200 PRO 201 -0.0745

PRO 201 THR 202 -0.0002

THR 202 LYS 203 -0.0456

LYS 203 LEU 204 0.0002

LEU 204 LYS 205 0.0618

LYS 205 SER 206 0.0004

SER 206 LEU 207 0.0196

LEU 207 ILE 208 0.0000

ILE 208 ARG 209 0.0112

ARG 209 LEU 210 -0.0001

LEU 210 VAL 211 0.0079

VAL 211 LYS 212 -0.0003

LYS 212 HIS 213 0.0480

HIS 213 TRP 214 0.0002

TRP 214 TYR 215 0.0359

TYR 215 GLN 216 0.0000

GLN 216 THR 217 0.0305

THR 217 CYS 218 -0.0000

CYS 218 LYS 219 0.0374

LYS 219 LYS 220 0.0004

LYS 220 THR 221 -0.0141

THR 221 HIS 222 0.0000

HIS 222 GLY 223 0.0373

GLY 223 ASN 224 -0.0001

ASN 224 LYS 225 -0.0213

LYS 225 LEU 226 -0.0000

LEU 226 PRO 227 0.0705

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 -0.0588

GLN 229 TYR 230 -0.0005

TYR 230 ALA 231 -0.0228

ALA 231 LEU 232 -0.0001

LEU 232 GLU 233 -0.0235

GLU 233 LEU 234 -0.0000

LEU 234 LEU 235 0.0036

LEU 235 THR 236 0.0000

THR 236 VAL 237 -0.0320

VAL 237 TYR 238 0.0001

TYR 238 ALA 239 -0.0428

ALA 239 TRP 240 0.0000

TRP 240 GLU 241 -0.0174

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 -0.0305

GLY 243 SER 244 0.0002

SER 244 ARG 245 -0.0060

ARG 245 LYS 246 0.0002

LYS 246 THR 247 0.0187

THR 247 ASP 248 0.0001

ASP 248 PHE 249 -0.0236

PHE 249 SER 250 0.0002

SER 250 THR 251 0.0244

THR 251 ALA 252 -0.0000

ALA 252 GLN 253 0.0025

GLN 253 GLY 254 -0.0004

GLY 254 PHE 255 -0.0121

PHE 255 GLN 256 -0.0001

GLN 256 THR 257 -0.0217

THR 257 VAL 258 0.0001

VAL 258 LEU 259 -0.0100

LEU 259 GLU 260 0.0001

GLU 260 LEU 261 0.0052

LEU 261 VAL 262 0.0002

VAL 262 LEU 263 -0.0110

LEU 263 LYS 264 0.0000

LYS 264 HIS 265 0.0182

HIS 265 GLN 266 0.0001

GLN 266 LYS 267 -0.0378

LYS 267 LEU 268 -0.0001

LEU 268 CYS 269 -0.0494

CYS 269 ILE 270 -0.0001

ILE 270 PHE 271 -0.0415

PHE 271 TRP 272 -0.0003

TRP 272 GLU 273 -0.0744

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 -0.0278

TYR 275 TYR 276 0.0001

TYR 276 ASP 277 0.0366

ASP 277 PHE 278 -0.0001

PHE 278 THR 279 -0.0233

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 0.0356

PRO 281 VAL 282 -0.0000

VAL 282 VAL 283 -0.0091

VAL 283 GLY 284 -0.0000

GLY 284 ARG 285 0.0010

ARG 285 CYS 286 0.0001

CYS 286 MET 287 -0.0245

MET 287 LEU 288 -0.0001

LEU 288 GLN 289 -0.0092

GLN 289 GLN 290 0.0002

GLN 290 LEU 291 -0.0330

LEU 291 LYS 292 -0.0002

LYS 292 LYS 293 0.0112

LYS 293 PRO 294 0.0000

PRO 294 ARG 295 0.0278

ARG 295 PRO 296 0.0003

PRO 296 VAL 297 0.0399

VAL 297 ILE 298 -0.0000

ILE 298 LEU 299 0.0237

LEU 299 ASP 300 -0.0000

ASP 300 PRO 301 0.0332

PRO 301 ALA 302 0.0003

ALA 302 ASP 303 -0.0153

ASP 303 PRO 304 0.0000

PRO 304 THR 305 -0.0266

THR 305 GLY 306 -0.0001

GLY 306 ASN 307 0.1348

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 0.0557

GLY 309 GLY 310 0.0003

GLY 310 GLY 311 -0.0528

GLY 311 ASP 312 -0.0002

ASP 312 THR 313 0.0062

THR 313 HIS 314 -0.0005

HIS 314 SER 315 -0.0186

SER 315 TRP 316 0.0001

TRP 316 GLN 317 0.0122

GLN 317 ARG 318 0.0003

ARG 318 LEU 319 -0.0177

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 -0.0114

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 -0.0041

ALA 323 ARG 324 -0.0002

ARG 324 VAL 325 -0.0076

VAL 325 TRP 326 0.0002

TRP 326 LEU 327 0.0029

LEU 327 GLY 328 -0.0000

GLY 328 TYR 329 0.0001

TYR 329 PRO 330 0.0000

PRO 330 CYS 331 -0.0156

CYS 331 CYS 332 0.0003

CYS 332 LYS 333 -0.0085

LYS 333 ASN 334 0.0003

ASN 334 LEU 335 -0.0321

LEU 335 ASP 336 -0.0002

ASP 336 GLY 337 0.0426

GLY 337 SER 338 0.0000

SER 338 LEU 339 0.0063

LEU 339 VAL 340 0.0001

VAL 340 GLY 341 -0.0230

GLY 341 ALA 342 0.0004

ALA 342 TRP 343 -0.0349

TRP 343 THR 344 0.0004

THR 344 MET 345 -0.0244

MET 345 LEU 346 0.0003

LEU 346 GLN 347 -0.0005

GLN 347 LYS 348 0.0004

LYS 348 ILE 349 0.0007

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 8 ---

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

* *