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

* *

CA strain for 2401161745071321422

--- 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 0.0000

GLU 2 LEU 3 0.0073

LEU 3 ARG 4 -0.0001

ARG 4 HIS 5 0.0141

HIS 5 THR 6 0.0003

THR 6 PRO 7 -0.0024

PRO 7 ALA 8 0.0002

ALA 8 ARG 9 0.0114

ARG 9 ASP 10 0.0004

ASP 10 LEU 11 -0.0022

LEU 11 ASP 12 0.0001

ASP 12 LYS 13 -0.0184

LYS 13 PHE 14 -0.0001

PHE 14 ILE 15 -0.0196

ILE 15 GLU 16 0.0000

GLU 16 ASP 17 -0.0281

ASP 17 HIS 18 0.0001

HIS 18 LEU 19 0.0023

LEU 19 LEU 20 -0.0002

LEU 20 PRO 21 0.0824

PRO 21 ASN 22 -0.0002

ASN 22 THR 23 -0.0418

THR 23 CYS 24 0.0004

CYS 24 PHE 25 -0.0147

PHE 25 ARG 26 -0.0001

ARG 26 THR 27 0.0083

THR 27 GLN 28 0.0000

GLN 28 VAL 29 -0.0015

VAL 29 LYS 30 0.0001

LYS 30 GLU 31 0.0446

GLU 31 ALA 32 -0.0001

ALA 32 ILE 33 0.0318

ILE 33 ASP 34 -0.0000

ASP 34 ILE 35 0.0411

ILE 35 VAL 36 -0.0000

VAL 36 CYS 37 0.0392

CYS 37 ARG 38 0.0001

ARG 38 PHE 39 0.0029

PHE 39 LEU 40 0.0002

LEU 40 LYS 41 0.0053

LYS 41 GLU 42 -0.0002

GLU 42 ARG 43 0.0371

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 -0.0084

PHE 45 GLN 46 0.0001

GLN 46 GLY 47 -0.0059

GLY 47 THR 48 -0.0000

THR 48 ALA 49 0.0214

ALA 49 ASP 50 -0.0002

ASP 50 PRO 51 -0.0144

PRO 51 VAL 52 -0.0003

VAL 52 ARG 53 -0.0199

ARG 53 VAL 54 -0.0001

VAL 54 SER 55 0.0965

SER 55 LYS 56 0.0004

LYS 56 VAL 57 -0.0089

VAL 57 VAL 58 0.0002

VAL 58 LYS 59 -0.0581

LYS 59 GLY 60 0.0003

GLY 60 GLY 61 0.0322

GLY 61 SER 62 -0.0000

SER 62 SER 63 -0.0448

SER 63 GLY 64 -0.0002

GLY 64 LYS 65 0.0291

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 -0.0110

THR 67 THR 68 -0.0001

THR 68 LEU 69 0.0120

LEU 69 ARG 70 -0.0002

ARG 70 GLY 71 -0.0497

GLY 71 ARG 72 0.0002

ARG 72 SER 73 0.0930

SER 73 ASP 74 0.0000

ASP 74 ALA 75 0.0155

ALA 75 ASP 76 0.0001

ASP 76 LEU 77 0.0148

LEU 77 VAL 78 -0.0002

VAL 78 VAL 79 -0.0120

VAL 79 PHE 80 -0.0004

PHE 80 LEU 81 -0.0061

LEU 81 THR 82 -0.0004

THR 82 LYS 83 -0.0189

LYS 83 LEU 84 -0.0004

LEU 84 THR 85 0.0169

THR 85 SER 86 -0.0002

SER 86 PHE 87 0.0321

PHE 87 GLU 88 0.0001

GLU 88 ASP 89 -0.0268

ASP 89 GLN 90 0.0002

GLN 90 LEU 91 0.0059

LEU 91 ARG 92 -0.0001

ARG 92 ARG 93 -0.0835

ARG 93 ARG 94 -0.0002

ARG 94 GLY 95 -0.0403

GLY 95 GLU 96 -0.0001

GLU 96 PHE 97 0.0268

PHE 97 ILE 98 0.0001

ILE 98 GLN 99 -0.0175

GLN 99 GLU 100 -0.0000

GLU 100 ILE 101 0.0191

ILE 101 ARG 102 0.0004

ARG 102 ARG 103 0.0484

ARG 103 GLN 104 -0.0004

GLN 104 LEU 105 0.0169

LEU 105 GLU 106 -0.0003

GLU 106 ALA 107 -0.0013

ALA 107 CYS 108 0.0001

CYS 108 GLN 109 0.0223

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 0.0156

GLU 111 GLN 112 0.0000

GLN 112 LYS 113 -0.0021

LYS 113 PHE 114 -0.0001

PHE 114 LYS 115 -0.0167

LYS 115 VAL 116 -0.0003

VAL 116 THR 117 -0.0048

THR 117 PHE 118 -0.0001

PHE 118 GLY 119 -0.0300

GLY 119 GLY 120 0.0005

GLY 120 GLY 121 0.0204

GLY 121 PHE 122 0.0002

PHE 122 VAL 123 0.0697

VAL 123 LEU 124 0.0005

LEU 124 SER 125 0.0074

SER 125 SER 126 0.0000

SER 126 PRO 127 0.0189

PRO 127 GLN 128 -0.0003

GLN 128 LEU 129 0.0239

LEU 129 GLN 130 0.0004

GLN 130 GLN 131 -0.0021

GLN 131 GLU 132 0.0002

GLU 132 VAL 133 0.0204

VAL 133 GLU 134 0.0001

GLU 134 PHE 135 0.0316

PHE 135 ASP 136 -0.0002

ASP 136 VAL 137 0.0893

VAL 137 LEU 138 0.0002

LEU 138 PRO 139 0.0679

PRO 139 ALA 140 0.0000

ALA 140 PHE 141 0.0008

PHE 141 ASP 142 -0.0004

ASP 142 ALA 143 0.0771

ALA 143 LEU 144 -0.0004

LEU 144 GLY 145 0.0438

GLY 145 GLN 146 0.0004

GLN 146 TRP 147 0.0042

TRP 147 THR 148 -0.0005

THR 148 PRO 149 -0.0305

PRO 149 GLY 150 0.0003

GLY 150 TYR 151 -0.0405

TYR 151 LYS 152 -0.0001

LYS 152 PRO 153 -0.0415

PRO 153 ASN 154 -0.0001

ASN 154 PRO 155 0.0286

PRO 155 GLU 156 -0.0002

GLU 156 ILE 157 0.0439

ILE 157 TYR 158 0.0001

TYR 158 VAL 159 -0.0037

VAL 159 GLN 160 -0.0001

GLN 160 LEU 161 0.0026

LEU 161 ILE 162 0.0003

ILE 162 LYS 163 0.0189

LYS 163 GLU 164 -0.0000

GLU 164 CYS 165 0.0154

CYS 165 LYS 166 0.0003

LYS 166 SER 167 -0.0259

SER 167 ARG 168 -0.0001

ARG 168 GLY 169 0.0416

GLY 169 LYS 170 -0.0002

LYS 170 GLU 171 0.0032

GLU 171 GLY 172 -0.0002

GLY 172 GLU 173 -0.0878

GLU 173 PHE 174 0.0003

PHE 174 SER 175 0.0881

SER 175 THR 176 0.0001

THR 176 CYS 177 -0.0017

CYS 177 PHE 178 0.0002

PHE 178 THR 179 0.0114

THR 179 GLU 180 0.0001

GLU 180 LEU 181 0.0311

LEU 181 GLN 182 0.0001

GLN 182 ARG 183 0.0087

ARG 183 ASP 184 -0.0001

ASP 184 PHE 185 0.0411

PHE 185 LEU 186 -0.0000

LEU 186 ARG 187 -0.0034

ARG 187 ASN 188 0.0003

ASN 188 ARG 189 -0.0286

ARG 189 PRO 190 0.0002

PRO 190 THR 191 -0.0019

THR 191 LYS 192 0.0000

LYS 192 LEU 193 -0.0103

LEU 193 LYS 194 0.0000

LYS 194 SER 195 -0.0570

SER 195 LEU 196 0.0000

LEU 196 ILE 197 -0.0178

ILE 197 ARG 198 0.0001

ARG 198 LEU 199 0.0021

LEU 199 VAL 200 0.0002

VAL 200 LYS 201 -0.0437

LYS 201 HIS 202 0.0002

HIS 202 TRP 203 -0.0403

TRP 203 TYR 204 -0.0002

TYR 204 GLN 205 -0.0717

GLN 205 THR 206 -0.0002

THR 206 CYS 207 -0.0227

CYS 207 LYS 208 -0.0003

LYS 208 LYS 209 0.0173

LYS 209 THR 210 0.0004

THR 210 HIS 211 -0.0200

HIS 211 GLY 212 -0.0003

GLY 212 ASN 213 0.0068

ASN 213 LYS 214 0.0000

LYS 214 LEU 215 0.0228

LEU 215 PRO 216 -0.0004

PRO 216 PRO 217 -0.0386

PRO 217 GLN 218 0.0004

GLN 218 TYR 219 0.0697

TYR 219 ALA 220 0.0000

ALA 220 LEU 221 0.0465

LEU 221 GLU 222 0.0001

GLU 222 LEU 223 -0.0134

LEU 223 LEU 224 -0.0000

LEU 224 THR 225 0.0149

THR 225 VAL 226 0.0002

VAL 226 TYR 227 0.0205

TYR 227 ALA 228 0.0001

ALA 228 TRP 229 0.0129

TRP 229 GLU 230 -0.0002

GLU 230 GLN 231 0.0383

GLN 231 GLY 232 -0.0002

GLY 232 SER 233 0.0095

SER 233 ARG 234 0.0001

ARG 234 LYS 235 0.0114

LYS 235 THR 236 0.0001

THR 236 ASP 237 -0.0173

ASP 237 PHE 238 0.0000

PHE 238 SER 239 -0.0309

SER 239 THR 240 0.0001

THR 240 ALA 241 -0.0071

ALA 241 GLN 242 0.0002

GLN 242 GLY 243 -0.0111

GLY 243 PHE 244 -0.0001

PHE 244 GLN 245 0.0004

GLN 245 THR 246 0.0001

THR 246 VAL 247 -0.0048

VAL 247 LEU 248 0.0000

LEU 248 GLU 249 -0.0147

GLU 249 LEU 250 -0.0000

LEU 250 VAL 251 -0.0054

VAL 251 LEU 252 0.0000

LEU 252 LYS 253 0.0009

LYS 253 HIS 254 0.0000

HIS 254 GLN 255 0.0013

GLN 255 LYS 256 0.0002

LYS 256 LEU 257 -0.0015

LEU 257 CYS 258 0.0000

CYS 258 ILE 259 0.0155

ILE 259 PHE 260 -0.0001

PHE 260 TRP 261 0.0371

TRP 261 GLU 262 0.0001

GLU 262 ALA 263 0.0684

ALA 263 TYR 264 -0.0000

TYR 264 TYR 265 -0.0020

TYR 265 ASP 266 0.0002

ASP 266 PHE 267 0.0348

PHE 267 THR 268 -0.0002

THR 268 ASN 269 -0.0234

ASN 269 PRO 270 0.0001

PRO 270 VAL 271 -0.0358

VAL 271 VAL 272 0.0000

VAL 272 GLY 273 0.0041

GLY 273 ARG 274 0.0002

ARG 274 CYS 275 0.0098

CYS 275 MET 276 -0.0001

MET 276 LEU 277 0.0008

LEU 277 GLN 278 0.0002

GLN 278 GLN 279 0.0117

GLN 279 LEU 280 0.0001

LEU 280 LYS 281 -0.0086

LYS 281 LYS 282 -0.0002

LYS 282 PRO 283 0.0759

PRO 283 ARG 284 0.0001

ARG 284 PRO 285 -0.0209

PRO 285 VAL 286 0.0001

VAL 286 ILE 287 -0.0151

ILE 287 LEU 288 0.0002

LEU 288 ASP 289 -0.0246

ASP 289 PRO 290 -0.0003

PRO 290 ALA 291 -0.0213

ALA 291 ASP 292 0.0001

ASP 292 PRO 293 -0.0276

PRO 293 THR 294 -0.0000

THR 294 GLY 295 0.1341

GLY 295 ASN 296 -0.0004

ASN 296 VAL 297 0.0972

VAL 297 GLY 298 -0.0002

GLY 298 GLY 299 -0.0377

GLY 299 GLY 300 0.0000

GLY 300 ASP 301 0.1138

ASP 301 THR 302 -0.0000

THR 302 HIS 303 0.0197

HIS 303 SER 304 0.0003

SER 304 TRP 305 -0.0008

TRP 305 GLN 306 0.0001

GLN 306 ARG 307 -0.0240

ARG 307 LEU 308 0.0004

LEU 308 ALA 309 -0.0158

ALA 309 GLN 310 0.0003

GLN 310 GLU 311 -0.0065

GLU 311 ALA 312 0.0004

ALA 312 ARG 313 -0.0155

ARG 313 VAL 314 -0.0000

VAL 314 TRP 315 -0.0142

TRP 315 LEU 316 0.0003

LEU 316 GLY 317 -0.0091

GLY 317 TYR 318 -0.0003

TYR 318 PRO 319 0.0367

PRO 319 CYS 320 -0.0003

CYS 320 CYS 321 -0.0059

CYS 321 LYS 322 0.0003

LYS 322 ASN 323 0.0239

ASN 323 LEU 324 0.0000

LEU 324 ASP 325 0.0011

ASP 325 GLY 326 -0.0002

GLY 326 SER 327 0.0019

SER 327 LEU 328 0.0002

LEU 328 VAL 329 -0.0095

VAL 329 GLY 330 -0.0004

GLY 330 ALA 331 -0.0345

ALA 331 TRP 332 -0.0002

TRP 332 THR 333 -0.0146

THR 333 MET 334 -0.0001

MET 334 LEU 335 -0.0476

LEU 335 GLN 336 -0.0003

GLN 336 LYS 337 -0.0431

LYS 337 ILE 338 -0.0000

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: April 25th, 2023.

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

*** ***

CA strain for 2401161745071321422

--- normal mode 8 ---

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

* *