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

* *

CA strain for 22122720241827122

--- 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 0.0054

LEU 3 ARG 4 -0.0004

ARG 4 HIS 5 -0.0171

HIS 5 THR 6 0.0001

THR 6 PRO 7 -0.0097

PRO 7 ALA 8 -0.0002

ALA 8 ARG 9 -0.0024

ARG 9 ASP 10 0.0004

ASP 10 LEU 11 0.0041

LEU 11 ASP 12 -0.0002

ASP 12 LYS 13 -0.0081

LYS 13 PHE 14 0.0001

PHE 14 ILE 15 0.0259

ILE 15 GLU 16 0.0002

GLU 16 ASP 17 0.0242

ASP 17 HIS 18 0.0001

HIS 18 LEU 19 -0.0009

LEU 19 LEU 20 -0.0002

LEU 20 PRO 21 -0.0321

PRO 21 ASN 22 -0.0002

ASN 22 THR 23 0.0258

THR 23 CYS 24 0.0001

CYS 24 PHE 25 0.0266

PHE 25 ARG 26 0.0001

ARG 26 THR 27 0.0025

THR 27 GLN 28 -0.0003

GLN 28 VAL 29 0.0002

VAL 29 LYS 30 0.0002

LYS 30 GLU 31 -0.0148

GLU 31 ALA 32 0.0003

ALA 32 ILE 33 -0.0150

ILE 33 ASP 34 0.0001

ASP 34 ILE 35 -0.0059

ILE 35 VAL 36 0.0004

VAL 36 CYS 37 -0.0044

CYS 37 ARG 38 -0.0003

ARG 38 PHE 39 -0.0037

PHE 39 LEU 40 -0.0001

LEU 40 LYS 41 0.0056

LYS 41 GLU 42 0.0001

GLU 42 ARG 43 -0.0245

ARG 43 CYS 44 -0.0003

CYS 44 PHE 45 0.0086

PHE 45 GLN 46 -0.0003

GLN 46 GLY 47 -0.0097

GLY 47 THR 48 -0.0003

THR 48 ALA 49 -0.0667

ALA 49 ASP 50 -0.0002

ASP 50 PRO 51 0.0260

PRO 51 VAL 52 -0.0000

VAL 52 ARG 53 0.0110

ARG 53 VAL 54 0.0001

VAL 54 SER 55 -0.0328

SER 55 LYS 56 0.0001

LYS 56 VAL 57 -0.0236

VAL 57 VAL 58 -0.0002

VAL 58 LYS 59 -0.0130

LYS 59 GLY 60 -0.0001

GLY 60 GLY 61 -0.0621

GLY 61 SER 62 -0.0002

SER 62 SER 63 -0.0210

SER 63 GLY 64 -0.0002

GLY 64 LYS 65 0.0129

LYS 65 GLY 66 -0.0000

GLY 66 THR 67 -0.0062

THR 67 THR 68 -0.0003

THR 68 LEU 69 0.0005

LEU 69 ARG 70 0.0002

ARG 70 GLY 71 -0.0833

GLY 71 ARG 72 0.0005

ARG 72 SER 73 -0.0862

SER 73 ASP 74 -0.0006

ASP 74 ALA 75 -0.0829

ALA 75 ASP 76 -0.0000

ASP 76 LEU 77 -0.0564

LEU 77 VAL 78 0.0004

VAL 78 VAL 79 0.0042

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 0.0166

LEU 81 THR 82 0.0003

THR 82 LYS 83 -0.0007

LYS 83 LEU 84 0.0002

LEU 84 THR 85 -0.0075

THR 85 SER 86 0.0000

SER 86 PHE 87 -0.0173

PHE 87 GLU 88 -0.0001

GLU 88 ASP 89 0.0082

ASP 89 GLN 90 -0.0004

GLN 90 LEU 91 -0.0223

LEU 91 ARG 92 -0.0004

ARG 92 ARG 93 0.0453

ARG 93 ARG 94 -0.0001

ARG 94 GLY 95 -0.0381

GLY 95 GLU 96 0.0003

GLU 96 PHE 97 -0.0394

PHE 97 ILE 98 0.0000

ILE 98 GLN 99 0.0438

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 0.0055

ILE 101 ARG 102 0.0003

ARG 102 ARG 103 -0.0828

ARG 103 GLN 104 0.0002

GLN 104 LEU 105 0.0114

LEU 105 GLU 106 -0.0000

GLU 106 ALA 107 -0.0255

ALA 107 CYS 108 0.0004

CYS 108 GLN 109 0.0099

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 0.0039

GLU 111 GLN 112 -0.0001

GLN 112 LYS 113 -0.0107

LYS 113 PHE 114 -0.0002

PHE 114 LYS 115 0.0325

LYS 115 VAL 116 0.0003

VAL 116 THR 117 0.0646

THR 117 PHE 118 0.0004

PHE 118 GLY 119 0.3304

GLY 119 VAL 120 -0.0002

VAL 120 GLN 121 -0.0972

GLN 121 SER 122 0.0000

SER 122 PRO 123 0.2542

PRO 123 ARG 124 -0.0000

ARG 124 ARG 125 0.0666

ARG 125 GLU 126 -0.0001

GLU 126 GLY 127 -0.1505

GLY 127 PRO 128 -0.0001

PRO 128 ARG 129 0.1265

ARG 129 ALA 130 -0.0000

ALA 130 LEU 131 0.1057

LEU 131 SER 132 -0.0001

SER 132 PHE 133 0.0222

PHE 133 VAL 134 -0.0000

VAL 134 LEU 135 0.0574

LEU 135 SER 136 0.0002

SER 136 SER 137 0.0392

SER 137 PRO 138 -0.0000

PRO 138 GLN 139 -0.0021

GLN 139 LEU 140 0.0000

LEU 140 GLN 141 -0.0091

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 0.0457

GLU 143 VAL 144 -0.0000

VAL 144 GLU 145 0.0588

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 0.0029

ASP 147 VAL 148 0.0003

VAL 148 LEU 149 -0.0153

LEU 149 PRO 150 0.0001

PRO 150 ALA 151 0.0108

ALA 151 PHE 152 0.0001

PHE 152 ASP 153 0.0129

ASP 153 ALA 154 0.0000

ALA 154 LEU 155 0.0430

LEU 155 GLY 156 -0.0000

GLY 156 GLN 157 0.0028

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 0.0028

THR 159 PRO 160 -0.0001

PRO 160 GLY 161 -0.0087

GLY 161 TYR 162 -0.0005

TYR 162 LYS 163 -0.0169

LYS 163 PRO 164 -0.0000

PRO 164 ASN 165 -0.0123

ASN 165 PRO 166 -0.0003

PRO 166 GLU 167 0.0234

GLU 167 ILE 168 -0.0002

ILE 168 TYR 169 -0.0191

TYR 169 VAL 170 -0.0001

VAL 170 GLN 171 0.0228

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 0.0157

ILE 173 LYS 174 0.0004

LYS 174 GLU 175 0.0325

GLU 175 CYS 176 0.0000

CYS 176 LYS 177 -0.0004

LYS 177 SER 178 -0.0001

SER 178 ARG 179 0.0215

ARG 179 GLY 180 -0.0000

GLY 180 ALA 181 0.0223

ALA 181 GLU 182 0.0003

GLU 182 GLY 183 -0.0119

GLY 183 GLU 184 0.0001

GLU 184 PHE 185 0.0225

PHE 185 SER 186 0.0000

SER 186 THR 187 0.0227

THR 187 CYS 188 0.0000

CYS 188 PHE 189 0.0251

PHE 189 THR 190 0.0002

THR 190 GLU 191 0.0030

GLU 191 LEU 192 -0.0001

LEU 192 GLN 193 -0.0266

GLN 193 ARG 194 -0.0003

ARG 194 ARG 194 0.0749

ARG 194 ASP 195 -0.0074

ASP 195 PHE 196 -0.0000

PHE 196 LEU 197 0.0300

LEU 197 ARG 198 -0.0003

ARG 198 ASN 199 0.0002

ASN 199 ARG 200 -0.0002

ARG 200 PRO 201 0.0837

PRO 201 THR 202 -0.0001

THR 202 LYS 203 0.0576

LYS 203 LEU 204 0.0000

LEU 204 LYS 205 -0.0306

LYS 205 SER 206 0.0002

SER 206 LEU 207 -0.0091

LEU 207 ILE 208 0.0002

ILE 208 ARG 209 -0.0098

ARG 209 LEU 210 0.0003

LEU 210 VAL 211 0.0072

VAL 211 LYS 212 0.0000

LYS 212 HIS 213 -0.0262

HIS 213 TRP 214 0.0003

TRP 214 TYR 215 -0.0010

TYR 215 GLN 216 -0.0001

GLN 216 THR 217 -0.0415

THR 217 CYS 218 0.0001

CYS 218 GLU 219 0.0050

GLU 219 LYS 220 -0.0000

LYS 220 THR 221 -0.0059

THR 221 HIS 222 -0.0001

HIS 222 GLY 223 0.0017

GLY 223 GLY 224 -0.0002

GLY 224 LYS 225 0.0197

LYS 225 LEU 226 -0.0000

LEU 226 PRO 227 -0.0842

PRO 227 PRO 228 0.0003

PRO 228 GLN 229 0.0676

GLN 229 TYR 230 0.0002

TYR 230 ALA 231 0.0064

ALA 231 LEU 232 -0.0001

LEU 232 GLU 233 -0.0078

GLU 233 LEU 234 -0.0000

LEU 234 LEU 235 -0.0089

LEU 235 THR 236 -0.0001

THR 236 VAL 237 0.0354

VAL 237 TYR 238 0.0000

TYR 238 ALA 239 0.0518

ALA 239 TRP 240 -0.0003

TRP 240 GLU 241 0.0095

GLU 241 GLN 242 -0.0002

GLN 242 GLY 243 0.0319

GLY 243 SER 244 -0.0000

SER 244 ARG 245 0.0188

ARG 245 LYS 246 -0.0001

LYS 246 THR 247 -0.0175

THR 247 ASP 248 -0.0003

ASP 248 PHE 249 0.0392

PHE 249 SER 250 -0.0005

SER 250 THR 251 -0.0317

THR 251 ALA 252 0.0004

ALA 252 GLN 253 -0.0103

GLN 253 GLY 254 0.0002

GLY 254 PHE 255 0.0169

PHE 255 GLN 256 -0.0003

GLN 256 THR 257 0.0244

THR 257 VAL 258 0.0004

VAL 258 LEU 259 0.0204

LEU 259 GLU 260 0.0002

GLU 260 LEU 261 0.0014

LEU 261 VAL 262 -0.0001

VAL 262 LEU 263 0.0033

LEU 263 LYS 264 0.0002

LYS 264 HIS 265 -0.0193

HIS 265 GLN 266 -0.0004

GLN 266 LYS 267 0.0476

LYS 267 LEU 268 -0.0004

LEU 268 CYS 269 0.0758

CYS 269 ILE 270 0.0000

ILE 270 PHE 271 0.0711

PHE 271 TRP 272 0.0001

TRP 272 GLU 273 0.0741

GLU 273 ALA 274 -0.0001

ALA 274 TYR 275 0.0337

TYR 275 TYR 276 -0.0002

TYR 276 ASP 277 -0.0297

ASP 277 PHE 278 -0.0001

PHE 278 THR 279 0.0303

THR 279 ASN 280 0.0003

ASN 280 PRO 281 -0.0275

PRO 281 VAL 282 -0.0003

VAL 282 VAL 283 0.0029

VAL 283 GLY 284 0.0002

GLY 284 ARG 285 -0.0100

ARG 285 CYS 286 -0.0003

CYS 286 MET 287 0.0176

MET 287 LEU 288 -0.0004

LEU 288 GLN 289 0.0009

GLN 289 GLN 290 -0.0001

GLN 290 LEU 291 0.0149

LEU 291 LYS 292 0.0006

LYS 292 LYS 293 0.0160

LYS 293 PRO 294 0.0000

PRO 294 ARG 295 -0.0324

ARG 295 PRO 296 0.0002

PRO 296 VAL 297 -0.0303

VAL 297 ILE 298 -0.0003

ILE 298 LEU 299 -0.0229

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 -0.0243

PRO 301 ALA 302 0.0003

ALA 302 ASP 303 0.0328

ASP 303 PRO 304 0.0001

PRO 304 THR 305 0.0302

THR 305 GLY 306 0.0001

GLY 306 ASN 307 -0.1573

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 -0.0784

GLY 309 GLY 310 0.0002

GLY 310 GLY 311 0.0664

GLY 311 ASP 312 0.0001

ASP 312 THR 313 -0.0111

THR 313 HIS 314 0.0002

HIS 314 SER 315 0.0067

SER 315 TRP 316 0.0001

TRP 316 GLN 317 -0.0128

GLN 317 ARG 318 0.0000

ARG 318 LEU 319 0.0080

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 0.0160

GLN 321 GLU 322 0.0002

GLU 322 ALA 323 0.0190

ALA 323 ARG 324 -0.0000

ARG 324 VAL 325 0.0046

VAL 325 TRP 326 -0.0000

TRP 326 LEU 327 -0.0044

LEU 327 GLY 328 0.0000

GLY 328 TYR 329 0.0002

TYR 329 PRO 330 0.0000

PRO 330 CYS 331 0.0096

CYS 331 CYS 332 -0.0000

CYS 332 LYS 333 0.0076

LYS 333 ASN 334 0.0001

ASN 334 LEU 335 0.0359

LEU 335 ASP 336 0.0004

ASP 336 GLY 337 -0.0524

GLY 337 SER 338 0.0000

SER 338 LEU 339 -0.0011

LEU 339 VAL 340 -0.0000

VAL 340 GLY 341 0.0274

GLY 341 ALA 342 -0.0003

ALA 342 TRP 343 0.0496

TRP 343 THR 344 -0.0001

THR 344 MET 345 0.0209

MET 345 LEU 346 0.0001

LEU 346 GLN 347 0.0003

GLN 347 LYS 348 0.0001

LYS 348 ILE 349 -0.0024

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 22122720241827122

--- normal mode 9 ---

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

* *