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

* *

CA strain for 230101190352136506

--- normal mode 30 ---

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 -0.0001

ASP 2 MET 3 -0.0668

MET 3 ILE 4 -0.0001

ILE 4 ARG 5 -0.0176

ARG 5 LEU 6 0.0005

LEU 6 ALA 7 -0.0242

ALA 7 THR 8 -0.0001

THR 8 ASN 9 -0.0432

ASN 9 LYS 10 -0.0004

LYS 10 PHE 11 -0.0043

PHE 11 SER 12 -0.0001

SER 12 GLU 13 0.0201

GLU 13 ASP 14 0.0003

ASP 14 ASN 15 -0.0353

ASN 15 LYS 16 -0.0004

LYS 16 ILE 17 -0.0352

ILE 17 GLY 18 0.0005

GLY 18 GLU 19 0.1828

GLU 19 GLY 20 0.0002

GLY 20 GLY 21 0.0204

GLY 21 PHE 22 0.0001

PHE 22 GLY 23 0.0789

GLY 23 ASP 24 -0.0000

ASP 24 VAL 25 0.0390

VAL 25 TYR 26 -0.0001

TYR 26 LYS 27 0.1330

LYS 27 GLY 28 -0.0003

GLY 28 MET 29 0.1598

MET 29 PHE 30 0.0001

PHE 30 PRO 31 0.0036

PRO 31 ASN 32 -0.0002

ASN 32 GLY 33 0.1575

GLY 33 TYR 34 -0.0001

TYR 34 GLU 35 0.1028

GLU 35 ILE 36 -0.0001

ILE 36 ALA 37 0.0696

ALA 37 VAL 38 -0.0002

VAL 38 LYS 39 0.0324

LYS 39 ARG 40 -0.0001

ARG 40 LEU 41 0.0016

LEU 41 ILE 42 0.0000

ILE 42 ARG 43 0.0537

ARG 43 ASN 44 -0.0001

ASN 44 SER 45 0.0170

SER 45 SER 46 0.0004

SER 46 GLN 47 0.0082

GLN 47 GLY 48 -0.0000

GLY 48 ALA 49 0.0108

ALA 49 VAL 50 -0.0000

VAL 50 GLU 51 -0.0090

GLU 51 PHE 52 -0.0001

PHE 52 LYS 53 0.0082

LYS 53 ASN 54 0.0000

ASN 54 GLU 55 -0.0474

GLU 55 VAL 56 0.0001

VAL 56 LEU 57 -0.0750

LEU 57 LEU 58 0.0000

LEU 58 ILE 59 -0.1283

ILE 59 ALA 60 0.0001

ALA 60 LYS 61 -0.0931

LYS 61 LEU 62 -0.0001

LEU 62 GLN 63 -0.0580

GLN 63 HIS 64 0.0002

HIS 64 ARG 65 -0.0978

ARG 65 ASN 66 -0.0000

ASN 66 LEU 67 0.0128

LEU 67 VAL 68 0.0000

VAL 68 ARG 69 0.0271

ARG 69 LEU 70 0.0002

LEU 70 LEU 71 -0.1225

LEU 71 GLY 72 0.0003

GLY 72 PHE 73 -0.0429

PHE 73 CYS 74 0.0002

CYS 74 ILE 75 -0.0272

ILE 75 GLN 76 0.0002

GLN 76 ARG 77 -0.0040

ARG 77 ASN 78 0.0002

ASN 78 GLU 79 0.0499

GLU 79 LYS 80 -0.0001

LYS 80 ILE 81 -0.0208

ILE 81 LEU 82 0.0000

LEU 82 ILE 83 -0.0389

ILE 83 TYR 84 0.0001

TYR 84 GLU 85 0.0201

GLU 85 TYR 86 -0.0002

TYR 86 MET 87 -0.0416

MET 87 HIS 88 0.0001

HIS 88 ASN 89 -0.0082

ASN 89 LYS 90 0.0001

LYS 90 SER 91 0.0601

SER 91 LEU 92 -0.0004

LEU 92 ASP 93 -0.0764

ASP 93 TYR 94 -0.0003

TYR 94 TYR 95 0.0262

TYR 95 LEU 96 -0.0003

LEU 96 PHE 97 -0.0159

PHE 97 SER 98 -0.0002

SER 98 PRO 99 0.0638

PRO 99 GLU 100 0.0000

GLU 100 ASN 101 -0.0319

ASN 101 HIS 102 -0.0001

HIS 102 ARG 103 0.1066

ARG 103 LYS 104 -0.0002

LYS 104 LEU 105 -0.0656

LEU 105 THR 106 -0.0001

THR 106 TRP 107 -0.0579

TRP 107 HIS 108 -0.0001

HIS 108 ALA 109 -0.0156

ALA 109 ARG 110 -0.0000

ARG 110 TYR 111 -0.0001

TYR 111 LYS 112 -0.0002

LYS 112 ILE 113 0.0305

ILE 113 ILE 114 -0.0001

ILE 114 ARG 115 -0.0426

ARG 115 GLY 116 -0.0001

GLY 116 ILE 117 0.0347

ILE 117 ALA 118 -0.0001

ALA 118 ARG 119 0.0246

ARG 119 GLY 120 0.0003

GLY 120 ILE 121 0.0485

ILE 121 LEU 122 -0.0000

LEU 122 TYR 123 0.0179

TYR 123 LEU 124 0.0001

LEU 124 HIS 125 -0.0175

HIS 125 GLU 126 -0.0005

GLU 126 ASP 127 0.0576

ASP 127 SER 128 0.0002

SER 128 HIS 129 -0.1910

HIS 129 LEU 130 0.0001

LEU 130 LYS 131 0.0529

LYS 131 ILE 132 -0.0003

ILE 132 ILE 133 0.0787

ILE 133 HIS 134 -0.0004

HIS 134 CYS 135 0.1113

CYS 135 ASP 136 0.0000

ASP 136 LEU 137 0.0137

LEU 137 LYS 138 0.0000

LYS 138 PRO 139 0.0755

PRO 139 SER 140 -0.0001

SER 140 ASN 141 -0.0504

ASN 141 ILE 142 0.0002

ILE 142 LEU 143 0.0908

LEU 143 LEU 144 0.0001

LEU 144 ASP 145 0.0276

ASP 145 ASP 146 0.0002

ASP 146 LYS 147 -0.0055

LYS 147 MET 148 0.0004

MET 148 ASN 149 -0.1242

ASN 149 ALA 150 -0.0000

ALA 150 LYS 151 0.0089

LYS 151 ILE 152 0.0001

ILE 152 SER 153 0.0618

SER 153 ASP 154 0.0002

ASP 154 PHE 155 -0.0462

PHE 155 GLY 156 -0.0002

GLY 156 LEU 157 0.0228

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 -0.0050

ARG 159 ILE 160 -0.0002

ILE 160 VAL 161 -0.0805

VAL 161 ALA 162 0.0003

ALA 162 ILE 163 0.0140

ILE 163 ASP 164 -0.0001

ASP 164 GLN 165 0.1143

GLN 165 MET 166 -0.0001

MET 166 GLN 167 0.2370

GLN 167 GLY 168 0.0002

GLY 168 ASN 169 0.3128

ASN 169 THR 170 -0.0001

THR 170 SER 171 0.4086

SER 171 ILE 172 0.0001

ILE 172 ILE 173 -0.0804

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 -0.1484

GLY 175 THR 176 0.0000

THR 176 TYR 177 0.3294

TYR 177 GLY 178 0.0003

GLY 178 TYR 179 0.2289

TYR 179 MET 180 -0.0001

MET 180 SER 181 0.0027

SER 181 PRO 182 -0.0002

PRO 182 GLU 183 0.1106

GLU 183 TYR 184 0.0000

TYR 184 ALA 185 0.2562

ALA 185 MET 186 0.0002

MET 186 LEU 187 -0.0144

LEU 187 GLY 188 0.0002

GLY 188 GLN 189 0.1452

GLN 189 PHE 190 0.0002

PHE 190 SER 191 0.1014

SER 191 VAL 192 0.0002

VAL 192 LYS 193 0.1029

LYS 193 SER 194 -0.0000

SER 194 ASP 195 0.1055

ASP 195 VAL 196 -0.0006

VAL 196 PHE 197 -0.0008

PHE 197 SER 198 -0.0002

SER 198 PHE 199 0.1451

PHE 199 GLY 200 0.0000

GLY 200 VAL 201 -0.0445

VAL 201 ILE 202 0.0001

ILE 202 MET 203 0.0437

MET 203 LEU 204 0.0000

LEU 204 GLU 205 -0.0411

GLU 205 ILE 206 0.0002

ILE 206 VAL 207 -0.0753

VAL 207 SER 208 -0.0002

SER 208 GLY 209 -0.0735

GLY 209 LYS 210 0.0002

LYS 210 ARG 211 0.1301

ARG 211 ASN 212 -0.0004

ASN 212 VAL 213 0.1077

VAL 213 ASP 214 -0.0002

ASP 214 TYR 215 -0.1827

TYR 215 ASN 216 0.0000

ASN 216 GLY 217 -0.2923

GLY 217 VAL 218 0.0003

VAL 218 ASN 219 -0.0155

ASN 219 SER 220 0.0001

SER 220 ILE 221 0.4964

ILE 221 ASP 222 -0.0001

ASP 222 ASP 223 -0.0476

ASP 223 LEU 224 -0.0001

LEU 224 VAL 225 -0.0092

VAL 225 SER 226 -0.0001

SER 226 HIS 227 0.0417

HIS 227 ALA 228 -0.0000

ALA 228 TRP 229 -0.0435

TRP 229 LYS 230 0.0002

LYS 230 LYS 231 0.0052

LYS 231 TRP 232 0.0002

TRP 232 THR 233 -0.0292

THR 233 GLU 234 0.0000

GLU 234 ASN 235 -0.0343

ASN 235 LYS 236 -0.0004

LYS 236 GLN 237 -0.0350

GLN 237 MET 238 -0.0000

MET 238 GLU 239 0.1089

GLU 239 LEU 240 -0.0005

LEU 240 LEU 241 -0.1939

LEU 241 ASP 242 0.0003

ASP 242 PRO 243 -0.0067

PRO 243 ALA 244 0.0002

ALA 244 LEU 245 -0.0731

LEU 245 THR 246 -0.0000

THR 246 TYR 247 -0.1056

TYR 247 SER 248 -0.0001

SER 248 PHE 249 -0.1021

PHE 249 SER 250 -0.0002

SER 250 GLU 251 0.0328

GLU 251 THR 252 -0.0001

THR 252 GLU 253 -0.0224

GLU 253 VAL 254 0.0001

VAL 254 SER 255 -0.0649

SER 255 ARG 256 -0.0001

ARG 256 CYS 257 0.0238

CYS 257 ILE 258 -0.0001

ILE 258 GLN 259 -0.0252

GLN 259 LEU 260 0.0002

LEU 260 GLY 261 -0.0071

GLY 261 LEU 262 -0.0004

LEU 262 LEU 263 0.0148

LEU 263 CYS 264 -0.0001

CYS 264 VAL 265 -0.0118

VAL 265 GLN 266 -0.0002

GLN 266 GLU 267 0.0000

GLU 267 ASN 268 -0.0003

ASN 268 PRO 269 0.1036

PRO 269 ASP 270 -0.0002

ASP 270 GLN 271 0.0708

GLN 271 ARG 272 0.0000

ARG 272 PRO 273 -0.0170

PRO 273 THR 274 0.0001

THR 274 MET 275 0.0238

MET 275 ALA 276 -0.0000

ALA 276 THR 277 0.0318

THR 277 ILE 278 -0.0002

ILE 278 ALA 279 0.0123

ALA 279 LEU 280 0.0004

LEU 280 TYR 281 -0.0152

TYR 281 PHE 282 -0.0003

PHE 282 ASN 283 0.0296

ASN 283 ILE 284 0.0001

ILE 284 ASP 285 -0.0208

ASP 285 SER 286 -0.0001

SER 286 ILE 287 -0.0167

ILE 287 ASP 288 -0.0000

ASP 288 LEU 289 -0.0170

LEU 289 PRO 290 -0.0001

PRO 290 LEU 291 -0.0016

LEU 291 PRO 292 0.0004

PRO 292 GLN 293 -0.1146

GLN 293 GLN 294 0.0000

GLN 294 PRO 295 -0.0034

PRO 295 PRO 296 0.0000

PRO 296 PHE 297 -0.0182

PHE 297 TYR 298 -0.0003

TYR 298 MET 299 -0.1059

MET 299 ARG 300 -0.0000

ARG 300 GLY 301 0.2617

GLY 301 LYS 302 -0.0001

LYS 302 ILE 303 -0.1411

ILE 303 GLU 304 0.0002

GLU 304 SER 305 0.0148

SER 305 LYS 306 -0.0000

LYS 306 VAL 307 0.0717

VAL 307 ALA 308 0.0001

ALA 308 SER 309 0.1632

SER 309 LYS 310 -0.0000

LYS 310 LYS 311 0.0984

LYS 311 THR 312 -0.0001

THR 312 MET 313 0.3329

MET 313 SER 314 -0.0001

SER 314 GLY 315 0.3405

GLY 315 ARG 316 0.0000

ARG 316 PRO 317 -0.2510

PRO 317 ARG 318 -0.0000

ARG 318 SER 319 -0.2710

SER 319 TYR 320 0.0001

TYR 320 SER 321 0.5030

SER 321 VAL 322 0.0001

VAL 322 THR 323 0.1074

THR 323 ARG 324 -0.0001

ARG 324 PHE 325 -0.0404

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 30 ---

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

* *