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 DHK *

CA strain for 2610090027463442181

--- normal mode 7 ---

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 0.0003

PRO 2 VAL 3 0.0084

VAL 3 VAL 4 -0.0003

VAL 4 VAL 5 -0.0108

VAL 5 THR 6 -0.0001

THR 6 GLY 7 -0.0526

GLY 7 ALA 8 0.0002

ALA 8 SER 9 0.0299

SER 9 GLY 10 -0.0004

GLY 10 PHE 11 -0.2719

PHE 11 VAL 12 0.0000

VAL 12 GLY 13 -0.0550

GLY 13 SER 14 -0.0003

SER 14 TRP 15 -0.1771

TRP 15 LEU 16 -0.0001

LEU 16 VAL 17 -0.0036

VAL 17 MET 18 0.0003

MET 18 LYS 19 -0.0885

LYS 19 LEU 20 -0.0003

LEU 20 LEU 21 -0.0617

LEU 21 GLN 22 -0.0000

GLN 22 ALA 23 -0.0283

ALA 23 GLY 24 -0.0001

GLY 24 TYR 25 0.0314

TYR 25 THR 26 -0.0000

THR 26 VAL 27 0.0067

VAL 27 ARG 28 0.0000

ARG 28 ALA 29 -0.0391

ALA 29 THR 30 0.0002

THR 30 VAL 31 -0.0190

VAL 31 ARG 32 -0.0002

ARG 32 ASP 33 0.0621

ASP 33 PRO 34 -0.0001

PRO 34 GLU 35 -0.0477

GLU 35 ASN 36 -0.0001

ASN 36 VAL 37 -0.0055

VAL 37 GLY 38 -0.0001

GLY 38 LYS 39 -0.0491

LYS 39 THR 40 -0.0001

THR 40 LYS 41 0.0347

LYS 41 PRO 42 -0.0001

PRO 42 LEU 43 -0.0115

LEU 43 LEU 44 0.0005

LEU 44 ASP 45 0.0081

ASP 45 LEU 46 -0.0003

LEU 46 PRO 47 0.0134

PRO 47 GLY 48 -0.0003

GLY 48 ALA 49 0.0144

ALA 49 THR 50 -0.0001

THR 50 GLU 51 -0.0046

GLU 51 ARG 52 0.0001

ARG 52 LEU 53 0.0192

LEU 53 SER 54 -0.0004

SER 54 ILE 55 0.0140

ILE 55 TRP 56 0.0001

TRP 56 LYS 57 0.0845

LYS 57 ALA 58 -0.0004

ALA 58 ASP 59 0.1392

ASP 59 MET 60 0.0001

MET 60 ALA 61 -0.0396

ALA 61 ASP 62 -0.0001

ASP 62 GLU 63 0.0208

GLU 63 ASP 64 -0.0001

ASP 64 SER 65 -0.0535

SER 65 PHE 66 0.0000

PHE 66 ASP 67 -0.0042

ASP 67 GLU 68 0.0001

GLU 68 ALA 69 -0.0362

ALA 69 ILE 70 -0.0004

ILE 70 ARG 71 -0.0113

ARG 71 GLY 72 -0.0000

GLY 72 CYS 73 0.0216

CYS 73 THR 74 -0.0002

THR 74 GLY 75 0.0081

GLY 75 VAL 76 -0.0000

VAL 76 PHE 77 0.0251

PHE 77 HIS 78 0.0001

HIS 78 VAL 79 -0.1082

VAL 79 ALA 80 -0.0003

ALA 80 THR 81 0.1694

THR 81 PRO 82 0.0002

PRO 82 THR 83 0.1487

THR 83 ASP 84 0.0002

ASP 84 PHE 85 -0.0052

PHE 85 GLU 86 -0.0001

GLU 86 SER 87 -0.0207

SER 87 LYS 88 0.0002

LYS 88 ASP 89 0.0063

ASP 89 PRO 90 0.0001

PRO 90 GLU 91 0.0337

GLU 91 ASN 92 0.0004

ASN 92 GLU 93 -0.0152

GLU 93 VAL 94 -0.0000

VAL 94 ILE 95 0.0395

ILE 95 LYS 96 0.0002

LYS 96 PRO 97 0.0363

PRO 97 THR 98 -0.0002

THR 98 VAL 99 0.0197

VAL 99 GLU 100 -0.0004

GLU 100 GLY 101 0.0050

GLY 101 MET 102 0.0000

MET 102 ILE 103 -0.0035

ILE 103 ARG 104 0.0001

ARG 104 ILE 105 -0.0187

ILE 105 LEU 106 -0.0004

LEU 106 ARG 107 0.0136

ARG 107 ALA 108 0.0001

ALA 108 CYS 109 0.0224

CYS 109 LYS 110 0.0001

LYS 110 GLU 111 -0.0392

GLU 111 ALA 112 -0.0002

ALA 112 GLY 113 0.0152

GLY 113 THR 114 -0.0001

THR 114 VAL 115 -0.0033

VAL 115 ARG 116 0.0000

ARG 116 ARG 117 -0.0408

ARG 117 ILE 118 -0.0001

ILE 118 VAL 119 -0.0112

VAL 119 PHE 120 -0.0002

PHE 120 THR 121 -0.0378

THR 121 SER 122 0.0004

SER 122 SER 123 0.0383

SER 123 ALA 124 0.0003

ALA 124 GLY 125 0.0015

GLY 125 THR 126 -0.0002

THR 126 VAL 127 0.0292

VAL 127 CYS 128 0.0001

CYS 128 VAL 129 0.0035

VAL 129 GLU 130 0.0004

GLU 130 GLU 131 -0.0107

GLU 131 ARG 132 -0.0003

ARG 132 ARG 133 0.0393

ARG 133 ARG 134 -0.0004

ARG 134 PRO 135 0.0795

PRO 135 VAL 136 -0.0000

VAL 136 TYR 137 0.0157

TYR 137 ASP 138 0.0001

ASP 138 HIS 139 0.0039

HIS 139 ASP 140 -0.0002

ASP 140 ASN 141 -0.0679

ASN 141 TRP 142 -0.0002

TRP 142 SER 143 -0.0744

SER 143 ASP 144 -0.0002

ASP 144 VAL 145 0.0917

VAL 145 ASP 146 0.0001

ASP 146 PHE 147 0.0136

PHE 147 CYS 148 0.0004

CYS 148 ARG 149 0.0194

ARG 149 ARG 150 -0.0004

ARG 150 VAL 151 -0.0250

VAL 151 LYS 152 0.0001

LYS 152 MET 153 -0.1004

MET 153 THR 154 -0.0002

THR 154 GLY 155 -0.0994

GLY 155 TRP 156 0.0002

TRP 156 MET 157 -0.0348

MET 157 TYR 158 -0.0000

TYR 158 PHE 159 -0.0289

PHE 159 VAL 160 -0.0001

VAL 160 SER 161 0.0503

SER 161 LYS 162 -0.0000

LYS 162 SER 163 0.0392

SER 163 LEU 164 0.0001

LEU 164 ALA 165 -0.0135

ALA 165 GLU 166 0.0001

GLU 166 LYS 167 0.0000

LYS 167 ALA 168 -0.0000

ALA 168 ALA 169 0.0051

ALA 169 MET 170 0.0002

MET 170 ALA 171 0.0518

ALA 171 TYR 172 -0.0000

TYR 172 ALA 173 0.0230

ALA 173 ALA 174 -0.0000

ALA 174 GLU 175 0.0006

GLU 175 HIS 176 0.0001

HIS 176 GLY 177 0.0583

GLY 177 LEU 178 -0.0001

LEU 178 ASP 179 0.1565

ASP 179 LEU 180 0.0002

LEU 180 VAL 181 0.0467

VAL 181 SER 182 0.0003

SER 182 VAL 183 -0.0130

VAL 183 ILE 184 -0.0002

ILE 184 PRO 185 -0.0460

PRO 185 THR 186 0.0004

THR 186 LEU 187 -0.0759

LEU 187 VAL 188 -0.0002

VAL 188 VAL 189 -0.0910

VAL 189 GLY 190 0.0005

GLY 190 PRO 191 0.0147

PRO 191 PHE 192 -0.0000

PHE 192 LEU 193 -0.0846

LEU 193 SER 194 -0.0001

SER 194 ALA 195 -0.0018

ALA 195 ALA 196 -0.0003

ALA 196 MET 197 -0.0190

MET 197 PRO 198 -0.0000

PRO 198 PRO 199 -0.0042

PRO 199 SER 200 -0.0001

SER 200 LEU 201 -0.0671

LEU 201 VAL 202 0.0002

VAL 202 THR 203 0.0131

THR 203 ALA 204 -0.0001

ALA 204 LEU 205 0.0110

LEU 205 ALA 206 0.0000

ALA 206 LEU 207 -0.0270

LEU 207 VAL 208 0.0001

VAL 208 THR 209 -0.0566

THR 209 GLY 210 0.0002

GLY 210 ASN 211 -0.0803

ASN 211 GLU 212 -0.0003

GLU 212 ALA 213 -0.1232

ALA 213 HIS 214 -0.0002

HIS 214 TYR 215 -0.0472

TYR 215 SER 216 -0.0000

SER 216 ILE 217 -0.0808

ILE 217 LEU 218 -0.0004

LEU 218 LYS 219 0.0105

LYS 219 GLN 220 -0.0002

GLN 220 VAL 221 0.0368

VAL 221 GLN 222 0.0001

GLN 222 PHE 223 0.0181

PHE 223 VAL 224 0.0002

VAL 224 HIS 225 0.0064

HIS 225 LEU 226 -0.0003

LEU 226 ASP 227 0.0431

ASP 227 ASP 228 0.0000

ASP 228 LEU 229 -0.0261

LEU 229 CYS 230 -0.0004

CYS 230 ASP 231 -0.0392

ASP 231 ALA 232 0.0001

ALA 232 GLU 233 -0.0020

GLU 233 ILE 234 -0.0000

ILE 234 PHE 235 -0.1225

PHE 235 LEU 236 0.0001

LEU 236 PHE 237 -0.0090

PHE 237 GLU 238 -0.0002

GLU 238 HIS 239 -0.0907

HIS 239 PRO 240 0.0002

PRO 240 ALA 241 -0.0563

ALA 241 ALA 242 0.0003

ALA 242 ALA 243 -0.0538

ALA 243 GLY 244 0.0000

GLY 244 ARG 245 -0.0822

ARG 245 TYR 246 0.0000

TYR 246 VAL 247 0.0131

VAL 247 CYS 248 -0.0000

CYS 248 SER 249 0.0571

SER 249 SER 250 -0.0001

SER 250 HIS 251 -0.0012

HIS 251 ASP 252 0.0003

ASP 252 ALA 253 -0.0273

ALA 253 THR 254 -0.0001

THR 254 ILE 255 0.0234

ILE 255 HIS 256 0.0001

HIS 256 GLY 257 -0.0257

GLY 257 LEU 258 -0.0000

LEU 258 ALA 259 0.0414

ALA 259 ALA 260 0.0000

ALA 260 MET 261 -0.0496

MET 261 LEU 262 -0.0000

LEU 262 ARG 263 0.0125

ARG 263 ASP 264 -0.0001

ASP 264 ARG 265 -0.0621

ARG 265 TYR 266 -0.0003

TYR 266 PRO 267 0.0278

PRO 267 GLU 268 0.0002

GLU 268 TYR 269 -0.0318

TYR 269 ASP 270 0.0002

ASP 270 ILE 271 -0.0133

ILE 271 PRO 272 0.0002

PRO 272 GLN 273 0.0380

GLN 273 LYS 274 -0.0001

LYS 274 LEU 275 -0.0607

LEU 275 ARG 276 0.0002

ARG 276 GLY 277 -0.0216

GLY 277 ILE 278 -0.0001

ILE 278 GLU 279 0.0277

GLU 279 ASP 280 0.0005

ASP 280 ASP 281 0.0093

ASP 281 LEU 282 0.0003

LEU 282 GLN 283 -0.0191

GLN 283 PRO 284 0.0000

PRO 284 VAL 285 0.0205

VAL 285 HIS 286 -0.0000

HIS 286 PHE 287 -0.0385

PHE 287 SER 288 0.0004

SER 288 SER 289 -0.0507

SER 289 LYS 290 0.0002

LYS 290 LYS 291 0.0280

LYS 291 LEU 292 -0.0002

LEU 292 LEU 293 0.0073

LEU 293 ASP 294 0.0001

ASP 294 HIS 295 -0.0080

HIS 295 GLY 296 -0.0001

GLY 296 PHE 297 0.0677

PHE 297 THR 298 0.0001

THR 298 PHE 299 0.1239

PHE 299 ARG 300 -0.0000

ARG 300 TYR 301 0.1687

TYR 301 THR 302 -0.0000

THR 302 VAL 303 0.0152

VAL 303 GLU 304 -0.0002

GLU 304 ASP 305 -0.0359

ASP 305 MET 306 -0.0001

MET 306 PHE 307 0.0878

PHE 307 ASP 308 0.0001

ASP 308 ALA 309 -0.0729

ALA 309 GLY 310 -0.0002

GLY 310 ILE 311 -0.0328

ILE 311 ARG 312 -0.0003

ARG 312 THR 313 -0.0725

THR 313 CYS 314 -0.0003

CYS 314 ARG 315 -0.0426

ARG 315 GLU 316 -0.0002

GLU 316 LYS 317 -0.0587

LYS 317 GLY 318 0.0002

GLY 318 LEU 319 -0.0438

LEU 319 ILE 320 -0.0002

ILE 320 PRO 321 0.0131

PRO 321 LEU 322 -0.0001

LEU 322 ALA 323 -0.0175

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 DHK ***

CA strain for 2610090027463442181

--- normal mode 7 ---

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 DHK *