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

* *

CA strain for 230101190352136506

--- normal mode 19 ---

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
PHE 1 ASP 2 -0.0003

ASP 2 MET 3 -0.0623

MET 3 ILE 4 0.0001

ILE 4 ARG 5 0.0135

ARG 5 LEU 6 -0.0001

LEU 6 ALA 7 0.0394

ALA 7 THR 8 -0.0002

THR 8 ASN 9 0.0009

ASN 9 LYS 10 0.0003

LYS 10 PHE 11 -0.0565

PHE 11 SER 12 0.0000

SER 12 GLU 13 0.0353

GLU 13 ASP 14 -0.0003

ASP 14 ASN 15 -0.0547

ASN 15 LYS 16 0.0001

LYS 16 ILE 17 -0.1433

ILE 17 GLY 18 0.0004

GLY 18 GLU 19 0.1021

GLU 19 GLY 20 0.0001

GLY 20 GLY 21 0.1089

GLY 21 PHE 22 -0.0002

PHE 22 GLY 23 -0.1504

GLY 23 ASP 24 -0.0004

ASP 24 VAL 25 0.1004

VAL 25 TYR 26 0.0000

TYR 26 LYS 27 0.1427

LYS 27 GLY 28 0.0000

GLY 28 MET 29 0.0685

MET 29 PHE 30 0.0001

PHE 30 PRO 31 0.0388

PRO 31 ASN 32 -0.0001

ASN 32 GLY 33 0.0773

GLY 33 TYR 34 -0.0000

TYR 34 GLU 35 0.0953

GLU 35 ILE 36 -0.0003

ILE 36 ALA 37 0.0355

ALA 37 VAL 38 -0.0002

VAL 38 LYS 39 0.0677

LYS 39 ARG 40 -0.0002

ARG 40 LEU 41 -0.0069

LEU 41 ILE 42 -0.0001

ILE 42 ARG 43 0.0658

ARG 43 ASN 44 -0.0004

ASN 44 SER 45 0.0383

SER 45 SER 46 -0.0002

SER 46 GLN 47 -0.0094

GLN 47 GLY 48 -0.0003

GLY 48 ALA 49 0.0341

ALA 49 VAL 50 0.0003

VAL 50 GLU 51 0.0237

GLU 51 PHE 52 0.0002

PHE 52 LYS 53 0.0315

LYS 53 ASN 54 -0.0003

ASN 54 GLU 55 -0.0421

GLU 55 VAL 56 0.0000

VAL 56 LEU 57 0.0076

LEU 57 LEU 58 -0.0002

LEU 58 ILE 59 -0.0744

ILE 59 ALA 60 -0.0001

ALA 60 LYS 61 0.0255

LYS 61 LEU 62 -0.0003

LEU 62 GLN 63 0.0134

GLN 63 HIS 64 0.0002

HIS 64 ARG 65 0.1030

ARG 65 ASN 66 -0.0006

ASN 66 LEU 67 0.0336

LEU 67 VAL 68 0.0001

VAL 68 ARG 69 0.1668

ARG 69 LEU 70 0.0000

LEU 70 LEU 71 -0.0600

LEU 71 GLY 72 0.0002

GLY 72 PHE 73 0.1058

PHE 73 CYS 74 0.0000

CYS 74 ILE 75 0.0454

ILE 75 GLN 76 0.0002

GLN 76 ARG 77 0.0518

ARG 77 ASN 78 0.0002

ASN 78 GLU 79 0.0763

GLU 79 LYS 80 0.0000

LYS 80 ILE 81 -0.0067

ILE 81 LEU 82 0.0002

LEU 82 ILE 83 0.0069

ILE 83 TYR 84 -0.0001

TYR 84 GLU 85 0.1971

GLU 85 TYR 86 -0.0001

TYR 86 MET 87 0.1906

MET 87 HIS 88 -0.0003

HIS 88 ASN 89 0.2621

ASN 89 LYS 90 -0.0001

LYS 90 SER 91 0.0424

SER 91 LEU 92 0.0004

LEU 92 ASP 93 0.0703

ASP 93 TYR 94 0.0002

TYR 94 TYR 95 -0.0487

TYR 95 LEU 96 0.0004

LEU 96 PHE 97 0.0422

PHE 97 SER 98 0.0002

SER 98 PRO 99 -0.0294

PRO 99 GLU 100 -0.0002

GLU 100 ASN 101 0.0093

ASN 101 HIS 102 0.0002

HIS 102 ARG 103 -0.0436

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 -0.0665

LEU 105 THR 106 -0.0001

THR 106 TRP 107 -0.0718

TRP 107 HIS 108 -0.0004

HIS 108 ALA 109 0.0637

ALA 109 ARG 110 0.0002

ARG 110 TYR 111 -0.0487

TYR 111 LYS 112 0.0003

LYS 112 ILE 113 -0.0162

ILE 113 ILE 114 -0.0001

ILE 114 ARG 115 -0.0095

ARG 115 GLY 116 0.0001

GLY 116 ILE 117 -0.0154

ILE 117 ALA 118 0.0004

ALA 118 ARG 119 -0.0619

ARG 119 GLY 120 -0.0000

GLY 120 ILE 121 0.0119

ILE 121 LEU 122 -0.0001

LEU 122 TYR 123 -0.1021

TYR 123 LEU 124 -0.0001

LEU 124 HIS 125 -0.0260

HIS 125 GLU 126 0.0003

GLU 126 ASP 127 -0.0356

ASP 127 SER 128 -0.0002

SER 128 HIS 129 0.0251

HIS 129 LEU 130 -0.0002

LEU 130 LYS 131 -0.0057

LYS 131 ILE 132 -0.0003

ILE 132 ILE 133 0.0102

ILE 133 HIS 134 -0.0000

HIS 134 CYS 135 0.0973

CYS 135 ASP 136 -0.0001

ASP 136 LEU 137 -0.0176

LEU 137 LYS 138 0.0001

LYS 138 PRO 139 -0.0532

PRO 139 SER 140 0.0002

SER 140 ASN 141 -0.0139

ASN 141 ILE 142 0.0001

ILE 142 LEU 143 0.0069

LEU 143 LEU 144 -0.0002

LEU 144 ASP 145 0.0396

ASP 145 ASP 146 -0.0002

ASP 146 LYS 147 0.0624

LYS 147 MET 148 -0.0002

MET 148 ASN 149 0.0950

ASN 149 ALA 150 -0.0000

ALA 150 LYS 151 0.0866

LYS 151 ILE 152 0.0005

ILE 152 SER 153 -0.0446

SER 153 ASP 154 0.0002

ASP 154 PHE 155 0.0480

PHE 155 GLY 156 -0.0004

GLY 156 LEU 157 -0.0190

LEU 157 ALA 158 -0.0003

ALA 158 ARG 159 -0.0357

ARG 159 ILE 160 0.0002

ILE 160 VAL 161 -0.1567

VAL 161 ALA 162 -0.0001

ALA 162 ILE 163 -0.0132

ILE 163 ASP 164 0.0003

ASP 164 GLN 165 -0.0024

GLN 165 MET 166 0.0002

MET 166 GLN 167 0.0512

GLN 167 GLY 168 0.0006

GLY 168 ASN 169 0.1868

ASN 169 THR 170 0.0000

THR 170 SER 171 0.2452

SER 171 ILE 172 -0.0000

ILE 172 ILE 173 -0.1159

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 -0.0970

GLY 175 THR 176 0.0004

THR 176 TYR 177 0.2627

TYR 177 GLY 178 -0.0001

GLY 178 TYR 179 0.0420

TYR 179 MET 180 -0.0000

MET 180 SER 181 -0.0063

SER 181 PRO 182 0.0000

PRO 182 GLU 183 -0.0975

GLU 183 TYR 184 -0.0001

TYR 184 ALA 185 0.1086

ALA 185 MET 186 0.0001

MET 186 LEU 187 0.0047

LEU 187 GLY 188 0.0001

GLY 188 GLN 189 0.0763

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 0.1473

SER 191 VAL 192 -0.0001

VAL 192 LYS 193 -0.1733

LYS 193 SER 194 -0.0002

SER 194 ASP 195 0.0350

ASP 195 VAL 196 -0.0002

VAL 196 PHE 197 0.0016

PHE 197 SER 198 -0.0002

SER 198 PHE 199 0.0200

PHE 199 GLY 200 -0.0000

GLY 200 VAL 201 0.0139

VAL 201 ILE 202 -0.0002

ILE 202 MET 203 -0.0421

MET 203 LEU 204 0.0000

LEU 204 GLU 205 0.0494

GLU 205 ILE 206 0.0003

ILE 206 VAL 207 0.0300

VAL 207 SER 208 -0.0001

SER 208 GLY 209 0.0950

GLY 209 LYS 210 -0.0002

LYS 210 ARG 211 -0.1976

ARG 211 ASN 212 0.0001

ASN 212 VAL 213 -0.0377

VAL 213 ASP 214 0.0001

ASP 214 TYR 215 0.0707

TYR 215 ASN 216 0.0001

ASN 216 GLY 217 -0.2680

GLY 217 VAL 218 0.0000

VAL 218 ASN 219 -0.0154

ASN 219 SER 220 -0.0001

SER 220 ILE 221 -0.0724

ILE 221 ASP 222 -0.0001

ASP 222 ASP 223 0.1196

ASP 223 LEU 224 0.0004

LEU 224 VAL 225 0.0492

VAL 225 SER 226 -0.0002

SER 226 HIS 227 -0.0917

HIS 227 ALA 228 -0.0000

ALA 228 TRP 229 0.0490

TRP 229 LYS 230 0.0002

LYS 230 LYS 231 -0.0937

LYS 231 TRP 232 0.0000

TRP 232 THR 233 -0.0035

THR 233 GLU 234 -0.0000

GLU 234 ASN 235 0.0039

ASN 235 LYS 236 0.0003

LYS 236 GLN 237 0.0327

GLN 237 MET 238 -0.0001

MET 238 GLU 239 -0.0848

GLU 239 LEU 240 -0.0002

LEU 240 LEU 241 -0.0869

LEU 241 ASP 242 -0.0000

ASP 242 PRO 243 -0.0207

PRO 243 ALA 244 -0.0000

ALA 244 LEU 245 0.0365

LEU 245 THR 246 0.0000

THR 246 TYR 247 -0.1116

TYR 247 SER 248 -0.0004

SER 248 PHE 249 0.0214

PHE 249 SER 250 -0.0002

SER 250 GLU 251 0.0087

GLU 251 THR 252 0.0003

THR 252 GLU 253 -0.0181

GLU 253 VAL 254 0.0003

VAL 254 SER 255 -0.0004

SER 255 ARG 256 -0.0003

ARG 256 CYS 257 -0.0183

CYS 257 ILE 258 -0.0003

ILE 258 GLN 259 0.0226

GLN 259 LEU 260 0.0003

LEU 260 GLY 261 -0.0025

GLY 261 LEU 262 0.0002

LEU 262 LEU 263 -0.0110

LEU 263 CYS 264 0.0001

CYS 264 VAL 265 0.0020

VAL 265 GLN 266 0.0003

GLN 266 GLU 267 0.0166

GLU 267 ASN 268 -0.0004

ASN 268 PRO 269 -0.0863

PRO 269 ASP 270 0.0002

ASP 270 GLN 271 0.0339

GLN 271 ARG 272 0.0003

ARG 272 PRO 273 -0.0080

PRO 273 THR 274 -0.0001

THR 274 MET 275 -0.0626

MET 275 ALA 276 0.0000

ALA 276 THR 277 -0.0769

THR 277 ILE 278 -0.0002

ILE 278 ALA 279 -0.0032

ALA 279 LEU 280 0.0002

LEU 280 TYR 281 -0.0173

TYR 281 PHE 282 0.0003

PHE 282 ASN 283 -0.0405

ASN 283 ILE 284 0.0002

ILE 284 ASP 285 0.0302

ASP 285 SER 286 -0.0000

SER 286 ILE 287 0.0148

ILE 287 ASP 288 -0.0001

ASP 288 LEU 289 0.0165

LEU 289 PRO 290 0.0001

PRO 290 LEU 291 -0.0412

LEU 291 PRO 292 0.0002

PRO 292 GLN 293 0.0062

GLN 293 GLN 294 0.0003

GLN 294 PRO 295 0.0289

PRO 295 PRO 296 0.0004

PRO 296 PHE 297 -0.0004

PHE 297 TYR 298 -0.0002

TYR 298 MET 299 -0.0670

MET 299 ARG 300 -0.0002

ARG 300 GLY 301 -0.0072

GLY 301 LYS 302 -0.0001

LYS 302 ILE 303 0.0764

ILE 303 GLU 304 0.0004

GLU 304 SER 305 0.1367

SER 305 LYS 306 0.0001

LYS 306 VAL 307 0.0397

VAL 307 ALA 308 -0.0001

ALA 308 SER 309 0.0999

SER 309 LYS 310 -0.0001

LYS 310 LYS 311 -0.0718

LYS 311 THR 312 0.0003

THR 312 MET 313 0.3218

MET 313 SER 314 -0.0000

SER 314 GLY 315 -0.3305

GLY 315 ARG 316 0.0001

ARG 316 PRO 317 0.4474

PRO 317 ARG 318 0.0002

ARG 318 SER 319 -0.1248

SER 319 TYR 320 0.0001

TYR 320 SER 321 -0.1353

SER 321 VAL 322 -0.0001

VAL 322 THR 323 0.0553

THR 323 ARG 324 -0.0000

ARG 324 PHE 325 -0.2485

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 230101190352136506

--- normal mode 19 ---

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

* *