Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* Zm A1b DHQ *

CA strain for 2610090028133442294

--- normal mode 10 ---

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
GLY 1 PRO 2 -0.0008

PRO 2 VAL 3 -0.0411

VAL 3 VAL 4 0.0002

VAL 4 VAL 5 -0.0989

VAL 5 THR 6 -0.0001

THR 6 GLY 7 -0.0442

GLY 7 ALA 8 -0.0002

ALA 8 SER 9 -0.0424

SER 9 GLY 10 0.0001

GLY 10 PHE 11 -0.2549

PHE 11 VAL 12 -0.0002

VAL 12 GLY 13 -0.0454

GLY 13 SER 14 -0.0000

SER 14 TRP 15 0.0689

TRP 15 LEU 16 -0.0001

LEU 16 VAL 17 0.0326

VAL 17 MET 18 0.0000

MET 18 LYS 19 0.0595

LYS 19 LEU 20 -0.0001

LEU 20 LEU 21 0.0695

LEU 21 GLN 22 0.0000

GLN 22 ALA 23 0.0417

ALA 23 GLY 24 -0.0002

GLY 24 TYR 25 0.0040

TYR 25 THR 26 0.0002

THR 26 VAL 27 -0.0313

VAL 27 ARG 28 0.0004

ARG 28 ALA 29 0.0031

ALA 29 THR 30 -0.0002

THR 30 VAL 31 0.0539

VAL 31 ARG 32 -0.0001

ARG 32 ASP 33 -0.1662

ASP 33 PRO 34 0.0001

PRO 34 GLU 35 0.0935

GLU 35 ASN 36 0.0002

ASN 36 VAL 37 -0.0162

VAL 37 GLY 38 -0.0002

GLY 38 LYS 39 -0.0466

LYS 39 THR 40 -0.0002

THR 40 LYS 41 -0.0516

LYS 41 PRO 42 0.0002

PRO 42 LEU 43 -0.0636

LEU 43 LEU 44 0.0001

LEU 44 ASP 45 0.0168

ASP 45 LEU 46 -0.0001

LEU 46 PRO 47 -0.0357

PRO 47 GLY 48 0.0001

GLY 48 ALA 49 -0.0120

ALA 49 THR 50 0.0001

THR 50 GLU 51 0.0165

GLU 51 ARG 52 -0.0003

ARG 52 LEU 53 -0.0523

LEU 53 SER 54 0.0003

SER 54 ILE 55 -0.0386

ILE 55 TRP 56 0.0001

TRP 56 LYS 57 -0.1026

LYS 57 ALA 58 -0.0000

ALA 58 ASP 59 -0.1739

ASP 59 MET 60 -0.0002

MET 60 ALA 61 0.0626

ALA 61 ASP 62 -0.0000

ASP 62 GLU 63 -0.0396

GLU 63 ASP 64 -0.0001

ASP 64 SER 65 0.0594

SER 65 PHE 66 0.0001

PHE 66 ASP 67 -0.0448

ASP 67 GLU 68 -0.0002

GLU 68 ALA 69 0.0378

ALA 69 ILE 70 0.0003

ILE 70 ARG 71 -0.0117

ARG 71 GLY 72 0.0000

GLY 72 CYS 73 0.0036

CYS 73 THR 74 -0.0001

THR 74 GLY 75 -0.0519

GLY 75 VAL 76 0.0003

VAL 76 PHE 77 -0.0594

PHE 77 HIS 78 0.0001

HIS 78 VAL 79 -0.0827

VAL 79 ALA 80 0.0004

ALA 80 THR 81 -0.3978

THR 81 PRO 82 -0.0002

PRO 82 THR 83 -0.1371

THR 83 ASP 84 -0.0000

ASP 84 PHE 85 -0.0539

PHE 85 GLU 86 -0.0002

GLU 86 SER 87 -0.1200

SER 87 LYS 88 0.0001

LYS 88 ASP 89 0.0176

ASP 89 PRO 90 -0.0002

PRO 90 GLU 91 0.0204

GLU 91 ASN 92 -0.0004

ASN 92 GLU 93 -0.0162

GLU 93 VAL 94 -0.0002

VAL 94 ILE 95 0.0162

ILE 95 LYS 96 -0.0001

LYS 96 PRO 97 -0.0681

PRO 97 THR 98 -0.0002

THR 98 VAL 99 -0.0595

VAL 99 GLU 100 0.0002

GLU 100 GLY 101 -0.0090

GLY 101 MET 102 -0.0000

MET 102 ILE 103 -0.0370

ILE 103 ARG 104 0.0001

ARG 104 ILE 105 0.0434

ILE 105 LEU 106 -0.0000

LEU 106 ARG 107 0.0090

ARG 107 ALA 108 0.0003

ALA 108 CYS 109 0.0228

CYS 109 LYS 110 -0.0001

LYS 110 GLU 111 0.0456

GLU 111 ALA 112 0.0000

ALA 112 GLY 113 -0.0087

GLY 113 THR 114 -0.0001

THR 114 VAL 115 0.0069

VAL 115 ARG 116 -0.0003

ARG 116 ARG 117 0.0424

ARG 117 ILE 118 0.0000

ILE 118 VAL 119 0.0027

VAL 119 PHE 120 -0.0001

PHE 120 THR 121 -0.0324

THR 121 SER 122 -0.0005

SER 122 SER 123 -0.0397

SER 123 ALA 124 0.0001

ALA 124 GLY 125 -0.0184

GLY 125 THR 126 0.0003

THR 126 VAL 127 -0.0009

VAL 127 CYS 128 -0.0001

CYS 128 VAL 129 0.0404

VAL 129 GLU 130 -0.0002

GLU 130 GLU 131 -0.0091

GLU 131 ARG 132 0.0001

ARG 132 ARG 133 -0.0844

ARG 133 ARG 134 -0.0003

ARG 134 PRO 135 0.0392

PRO 135 VAL 136 -0.0002

VAL 136 TYR 137 0.0029

TYR 137 ASP 138 0.0002

ASP 138 HIS 139 0.0387

HIS 139 ASP 140 0.0001

ASP 140 ASN 141 0.1179

ASN 141 TRP 142 0.0002

TRP 142 SER 143 0.1955

SER 143 ASP 144 -0.0001

ASP 144 VAL 145 -0.0122

VAL 145 ASP 146 -0.0003

ASP 146 PHE 147 -0.0466

PHE 147 CYS 148 0.0005

CYS 148 ARG 149 0.0424

ARG 149 ARG 150 -0.0003

ARG 150 VAL 151 -0.0921

VAL 151 LYS 152 -0.0001

LYS 152 MET 153 -0.3195

MET 153 THR 154 0.0003

THR 154 GLY 155 -0.1495

GLY 155 TRP 156 -0.0001

TRP 156 MET 157 -0.0625

MET 157 TYR 158 -0.0001

TYR 158 PHE 159 0.0744

PHE 159 VAL 160 0.0000

VAL 160 SER 161 -0.1367

SER 161 LYS 162 -0.0001

LYS 162 SER 163 -0.0598

SER 163 LEU 164 -0.0002

LEU 164 ALA 165 -0.0317

ALA 165 GLU 166 -0.0005

GLU 166 LYS 167 -0.0230

LYS 167 ALA 168 0.0001

ALA 168 ALA 169 0.0261

ALA 169 MET 170 -0.0001

MET 170 ALA 171 -0.0407

ALA 171 TYR 172 -0.0001

TYR 172 ALA 173 0.0143

ALA 173 ALA 174 0.0000

ALA 174 GLU 175 -0.0000

GLU 175 HIS 176 -0.0003

HIS 176 GLY 177 -0.0180

GLY 177 LEU 178 0.0000

LEU 178 ASP 179 -0.0014

ASP 179 LEU 180 0.0002

LEU 180 VAL 181 0.0318

VAL 181 SER 182 -0.0004

SER 182 VAL 183 0.0582

VAL 183 ILE 184 -0.0001

ILE 184 PRO 185 0.0018

PRO 185 THR 186 0.0001

THR 186 LEU 187 -0.0412

LEU 187 VAL 188 -0.0001

VAL 188 VAL 189 -0.0175

VAL 189 GLY 190 -0.0001

GLY 190 PRO 191 -0.0106

PRO 191 PHE 192 0.0001

PHE 192 LEU 193 -0.1107

LEU 193 SER 194 -0.0001

SER 194 ALA 195 -0.1689

ALA 195 ALA 196 -0.0004

ALA 196 MET 197 -0.0041

MET 197 PRO 198 0.0001

PRO 198 PRO 199 -0.2095

PRO 199 SER 200 0.0000

SER 200 LEU 201 -0.0659

LEU 201 VAL 202 0.0002

VAL 202 THR 203 -0.0056

THR 203 ALA 204 -0.0001

ALA 204 LEU 205 0.0701

LEU 205 ALA 206 0.0002

ALA 206 LEU 207 -0.2276

LEU 207 VAL 208 -0.0000

VAL 208 THR 209 -0.1261

THR 209 GLY 210 -0.0002

GLY 210 ASN 211 -0.1732

ASN 211 GLU 212 0.0001

GLU 212 ALA 213 -0.3043

ALA 213 HIS 214 -0.0003

HIS 214 TYR 215 -0.2339

TYR 215 SER 216 0.0002

SER 216 ILE 217 -0.0024

ILE 217 LEU 218 -0.0004

LEU 218 LYS 219 -0.0060

LYS 219 GLN 220 0.0004

GLN 220 VAL 221 -0.0052

VAL 221 GLN 222 0.0000

GLN 222 PHE 223 0.0135

PHE 223 VAL 224 -0.0002

VAL 224 HIS 225 0.0008

HIS 225 LEU 226 -0.0002

LEU 226 ASP 227 0.0144

ASP 227 ASP 228 0.0002

ASP 228 LEU 229 -0.0499

LEU 229 CYS 230 0.0003

CYS 230 ASP 231 -0.0498

ASP 231 ALA 232 -0.0000

ALA 232 GLU 233 0.0347

GLU 233 ILE 234 0.0001

ILE 234 PHE 235 0.0235

PHE 235 LEU 236 -0.0002

LEU 236 PHE 237 0.0971

PHE 237 GLU 238 -0.0000

GLU 238 HIS 239 0.0884

HIS 239 PRO 240 -0.0004

PRO 240 ALA 241 0.0102

ALA 241 ALA 242 0.0000

ALA 242 ALA 243 0.0377

ALA 243 GLY 244 -0.0001

GLY 244 ARG 245 0.0660

ARG 245 TYR 246 -0.0004

TYR 246 VAL 247 0.0898

VAL 247 CYS 248 0.0002

CYS 248 SER 249 0.1537

SER 249 SER 250 -0.0003

SER 250 HIS 251 0.1864

HIS 251 ASP 252 -0.0003

ASP 252 ALA 253 0.2106

ALA 253 THR 254 0.0005

THR 254 ILE 255 0.0533

ILE 255 HIS 256 0.0002

HIS 256 GLY 257 -0.0290

GLY 257 LEU 258 0.0001

LEU 258 ALA 259 0.0979

ALA 259 ALA 260 0.0003

ALA 260 MET 261 0.0705

MET 261 LEU 262 -0.0000

LEU 262 ARG 263 0.0487

ARG 263 ASP 264 -0.0000

ASP 264 ARG 265 0.0216

ARG 265 TYR 266 -0.0000

TYR 266 PRO 267 0.0437

PRO 267 GLU 268 0.0001

GLU 268 TYR 269 -0.0714

TYR 269 ASP 270 -0.0002

ASP 270 ILE 271 0.0529

ILE 271 PRO 272 -0.0002

PRO 272 GLN 273 -0.1390

GLN 273 LYS 274 -0.0000

LYS 274 LEU 275 -0.0925

LEU 275 ARG 276 -0.0002

ARG 276 GLY 277 -0.0722

GLY 277 ILE 278 0.0000

ILE 278 GLU 279 -0.0650

GLU 279 ASP 280 -0.0001

ASP 280 ASP 281 -0.1242

ASP 281 LEU 282 -0.0001

LEU 282 GLN 283 0.0376

GLN 283 PRO 284 0.0007

PRO 284 VAL 285 0.0354

VAL 285 HIS 286 0.0001

HIS 286 PHE 287 0.1210

PHE 287 SER 288 -0.0001

SER 288 SER 289 0.1351

SER 289 LYS 290 -0.0002

LYS 290 LYS 291 -0.0068

LYS 291 LEU 292 -0.0001

LEU 292 LEU 293 -0.0139

LEU 293 ASP 294 -0.0001

ASP 294 HIS 295 0.0112

HIS 295 GLY 296 -0.0000

GLY 296 PHE 297 0.0140

PHE 297 THR 298 -0.0002

THR 298 PHE 299 0.1423

PHE 299 ARG 300 -0.0002

ARG 300 TYR 301 0.2207

TYR 301 THR 302 0.0002

THR 302 VAL 303 0.1021

VAL 303 GLU 304 -0.0001

GLU 304 ASP 305 0.0551

ASP 305 MET 306 -0.0001

MET 306 PHE 307 0.0772

PHE 307 ASP 308 -0.0001

ASP 308 ALA 309 0.0063

ALA 309 GLY 310 -0.0000

GLY 310 ILE 311 0.0079

ILE 311 ARG 312 0.0006

ARG 312 THR 313 -0.0091

THR 313 CYS 314 -0.0001

CYS 314 ARG 315 -0.0639

ARG 315 GLU 316 0.0002

GLU 316 LYS 317 0.0101

LYS 317 GLY 318 -0.0002

GLY 318 LEU 319 0.0009

LEU 319 ILE 320 0.0001

ILE 320 PRO 321 -0.0680

PRO 321 LEU 322 -0.0001

LEU 322 ALA 323 -0.0431

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** Zm A1b DHQ ***

CA strain for 2610090028133442294

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* Zm A1b DHQ *