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 8 ---

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 -0.0001

PRO 2 VAL 3 -0.0231

VAL 3 VAL 4 0.0000

VAL 4 VAL 5 0.0582

VAL 5 THR 6 0.0000

THR 6 GLY 7 0.0121

GLY 7 ALA 8 0.0001

ALA 8 SER 9 0.0221

SER 9 GLY 10 -0.0002

GLY 10 PHE 11 0.4105

PHE 11 VAL 12 0.0000

VAL 12 GLY 13 0.1414

GLY 13 SER 14 0.0000

SER 14 TRP 15 -0.0407

TRP 15 LEU 16 -0.0002

LEU 16 VAL 17 -0.0003

VAL 17 MET 18 -0.0004

MET 18 LYS 19 -0.0102

LYS 19 LEU 20 -0.0002

LEU 20 LEU 21 -0.0395

LEU 21 GLN 22 -0.0001

GLN 22 ALA 23 0.0048

ALA 23 GLY 24 -0.0000

GLY 24 TYR 25 0.0177

TYR 25 THR 26 -0.0000

THR 26 VAL 27 -0.0208

VAL 27 ARG 28 -0.0001

ARG 28 ALA 29 0.0358

ALA 29 THR 30 0.0000

THR 30 VAL 31 -0.0204

VAL 31 ARG 32 0.0001

ARG 32 ASP 33 -0.0686

ASP 33 PRO 34 0.0004

PRO 34 GLU 35 -0.0300

GLU 35 ASN 36 -0.0002

ASN 36 VAL 37 -0.0371

VAL 37 GLY 38 -0.0001

GLY 38 LYS 39 0.0398

LYS 39 THR 40 0.0002

THR 40 LYS 41 -0.0391

LYS 41 PRO 42 -0.0002

PRO 42 LEU 43 0.0815

LEU 43 LEU 44 0.0001

LEU 44 ASP 45 -0.0315

ASP 45 LEU 46 -0.0000

LEU 46 PRO 47 0.0111

PRO 47 GLY 48 -0.0001

GLY 48 ALA 49 -0.0105

ALA 49 THR 50 0.0001

THR 50 GLU 51 0.0111

GLU 51 ARG 52 0.0004

ARG 52 LEU 53 -0.0242

LEU 53 SER 54 -0.0001

SER 54 ILE 55 -0.0731

ILE 55 TRP 56 0.0000

TRP 56 LYS 57 -0.0677

LYS 57 ALA 58 0.0002

ALA 58 ASP 59 -0.0509

ASP 59 MET 60 0.0002

MET 60 ALA 61 0.0323

ALA 61 ASP 62 -0.0002

ASP 62 GLU 63 0.0073

GLU 63 ASP 64 0.0000

ASP 64 SER 65 -0.0127

SER 65 PHE 66 -0.0003

PHE 66 ASP 67 -0.0018

ASP 67 GLU 68 0.0000

GLU 68 ALA 69 0.0195

ALA 69 ILE 70 0.0000

ILE 70 ARG 71 0.0011

ARG 71 GLY 72 0.0003

GLY 72 CYS 73 -0.0476

CYS 73 THR 74 0.0001

THR 74 GLY 75 -0.0063

GLY 75 VAL 76 -0.0001

VAL 76 PHE 77 0.0171

PHE 77 HIS 78 -0.0003

HIS 78 VAL 79 -0.0322

VAL 79 ALA 80 0.0002

ALA 80 THR 81 -0.1384

THR 81 PRO 82 -0.0000

PRO 82 THR 83 0.1807

THR 83 ASP 84 0.0003

ASP 84 PHE 85 0.0674

PHE 85 GLU 86 0.0001

GLU 86 SER 87 0.1290

SER 87 LYS 88 0.0000

LYS 88 ASP 89 0.0385

ASP 89 PRO 90 -0.0002

PRO 90 GLU 91 0.0266

GLU 91 ASN 92 -0.0003

ASN 92 GLU 93 -0.0070

GLU 93 VAL 94 0.0000

VAL 94 ILE 95 0.0375

ILE 95 LYS 96 -0.0002

LYS 96 PRO 97 -0.0295

PRO 97 THR 98 0.0001

THR 98 VAL 99 -0.0398

VAL 99 GLU 100 0.0001

GLU 100 GLY 101 -0.0682

GLY 101 MET 102 0.0004

MET 102 ILE 103 0.0107

ILE 103 ARG 104 -0.0004

ARG 104 ILE 105 0.0245

ILE 105 LEU 106 0.0003

LEU 106 ARG 107 -0.0522

ARG 107 ALA 108 -0.0004

ALA 108 CYS 109 -0.0070

CYS 109 LYS 110 -0.0003

LYS 110 GLU 111 -0.0212

GLU 111 ALA 112 -0.0000

ALA 112 GLY 113 -0.0352

GLY 113 THR 114 0.0000

THR 114 VAL 115 -0.0289

VAL 115 ARG 116 0.0001

ARG 116 ARG 117 -0.0646

ARG 117 ILE 118 0.0000

ILE 118 VAL 119 -0.0145

VAL 119 PHE 120 0.0001

PHE 120 THR 121 -0.0106

THR 121 SER 122 0.0002

SER 122 SER 123 0.0209

SER 123 ALA 124 0.0001

ALA 124 GLY 125 -0.0205

GLY 125 THR 126 -0.0002

THR 126 VAL 127 0.0136

VAL 127 CYS 128 0.0004

CYS 128 VAL 129 0.0378

VAL 129 GLU 130 0.0000

GLU 130 GLU 131 -0.0269

GLU 131 ARG 132 0.0001

ARG 132 ARG 133 0.0307

ARG 133 ARG 134 -0.0002

ARG 134 PRO 135 0.0086

PRO 135 VAL 136 -0.0003

VAL 136 TYR 137 -0.1301

TYR 137 ASP 138 -0.0003

ASP 138 HIS 139 -0.1141

HIS 139 ASP 140 0.0001

ASP 140 ASN 141 0.0975

ASN 141 TRP 142 -0.0002

TRP 142 SER 143 0.0967

SER 143 ASP 144 0.0001

ASP 144 VAL 145 0.0307

VAL 145 ASP 146 0.0002

ASP 146 PHE 147 0.0295

PHE 147 CYS 148 0.0001

CYS 148 ARG 149 0.0472

ARG 149 ARG 150 -0.0001

ARG 150 VAL 151 -0.0518

VAL 151 LYS 152 -0.0003

LYS 152 MET 153 -0.0599

MET 153 THR 154 -0.0000

THR 154 GLY 155 0.1717

GLY 155 TRP 156 -0.0001

TRP 156 MET 157 0.0190

MET 157 TYR 158 -0.0002

TYR 158 PHE 159 0.0231

PHE 159 VAL 160 0.0001

VAL 160 SER 161 -0.0392

SER 161 LYS 162 -0.0002

LYS 162 SER 163 -0.0124

SER 163 LEU 164 0.0000

LEU 164 ALA 165 -0.0255

ALA 165 GLU 166 -0.0001

GLU 166 LYS 167 -0.0040

LYS 167 ALA 168 -0.0002

ALA 168 ALA 169 0.0068

ALA 169 MET 170 0.0002

MET 170 ALA 171 -0.0415

ALA 171 TYR 172 0.0001

TYR 172 ALA 173 0.0281

ALA 173 ALA 174 -0.0001

ALA 174 GLU 175 -0.0110

GLU 175 HIS 176 0.0004

HIS 176 GLY 177 -0.0208

GLY 177 LEU 178 0.0001

LEU 178 ASP 179 -0.0984

ASP 179 LEU 180 -0.0000

LEU 180 VAL 181 -0.0682

VAL 181 SER 182 -0.0001

SER 182 VAL 183 -0.0264

VAL 183 ILE 184 0.0001

ILE 184 PRO 185 -0.0140

PRO 185 THR 186 -0.0000

THR 186 LEU 187 -0.0839

LEU 187 VAL 188 -0.0004

VAL 188 VAL 189 -0.0503

VAL 189 GLY 190 -0.0002

GLY 190 PRO 191 -0.0006

PRO 191 PHE 192 0.0001

PHE 192 LEU 193 0.1294

LEU 193 SER 194 -0.0001

SER 194 ALA 195 0.1630

ALA 195 ALA 196 -0.0002

ALA 196 MET 197 -0.0016

MET 197 PRO 198 -0.0002

PRO 198 PRO 199 -0.1479

PRO 199 SER 200 -0.0002

SER 200 LEU 201 -0.0674

LEU 201 VAL 202 0.0000

VAL 202 THR 203 -0.0152

THR 203 ALA 204 0.0001

ALA 204 LEU 205 -0.0513

LEU 205 ALA 206 -0.0000

ALA 206 LEU 207 0.0456

LEU 207 VAL 208 -0.0002

VAL 208 THR 209 -0.0462

THR 209 GLY 210 -0.0001

GLY 210 ASN 211 0.0057

ASN 211 GLU 212 0.0002

GLU 212 ALA 213 0.1489

ALA 213 HIS 214 0.0002

HIS 214 TYR 215 0.1541

TYR 215 SER 216 -0.0005

SER 216 ILE 217 -0.0435

ILE 217 LEU 218 0.0003

LEU 218 LYS 219 0.0589

LYS 219 GLN 220 -0.0000

GLN 220 VAL 221 0.0863

VAL 221 GLN 222 -0.0001

GLN 222 PHE 223 0.0224

PHE 223 VAL 224 0.0000

VAL 224 HIS 225 0.0177

HIS 225 LEU 226 0.0002

LEU 226 ASP 227 -0.0112

ASP 227 ASP 228 -0.0003

ASP 228 LEU 229 -0.0189

LEU 229 CYS 230 -0.0002

CYS 230 ASP 231 0.0327

ASP 231 ALA 232 0.0001

ALA 232 GLU 233 -0.0317

GLU 233 ILE 234 -0.0002

ILE 234 PHE 235 0.0392

PHE 235 LEU 236 0.0000

LEU 236 PHE 237 -0.0532

PHE 237 GLU 238 0.0002

GLU 238 HIS 239 -0.0292

HIS 239 PRO 240 -0.0003

PRO 240 ALA 241 0.0311

ALA 241 ALA 242 0.0001

ALA 242 ALA 243 0.0518

ALA 243 GLY 244 -0.0002

GLY 244 ARG 245 0.0238

ARG 245 TYR 246 0.0001

TYR 246 VAL 247 -0.1062

VAL 247 CYS 248 -0.0000

CYS 248 SER 249 -0.0858

SER 249 SER 250 -0.0005

SER 250 HIS 251 -0.1456

HIS 251 ASP 252 -0.0001

ASP 252 ALA 253 -0.1251

ALA 253 THR 254 -0.0001

THR 254 ILE 255 -0.0552

ILE 255 HIS 256 0.0001

HIS 256 GLY 257 0.0122

GLY 257 LEU 258 -0.0000

LEU 258 ALA 259 -0.0327

ALA 259 ALA 260 -0.0002

ALA 260 MET 261 -0.0563

MET 261 LEU 262 0.0000

LEU 262 ARG 263 -0.0133

ARG 263 ASP 264 -0.0002

ASP 264 ARG 265 -0.0052

ARG 265 TYR 266 0.0001

TYR 266 PRO 267 -0.0259

PRO 267 GLU 268 0.0000

GLU 268 TYR 269 -0.0180

TYR 269 ASP 270 0.0003

ASP 270 ILE 271 -0.0044

ILE 271 PRO 272 0.0001

PRO 272 GLN 273 0.0979

GLN 273 LYS 274 0.0002

LYS 274 LEU 275 0.0402

LEU 275 ARG 276 0.0002

ARG 276 GLY 277 -0.0172

GLY 277 ILE 278 0.0002

ILE 278 GLU 279 -0.0839

GLU 279 ASP 280 -0.0003

ASP 280 ASP 281 0.0275

ASP 281 LEU 282 -0.0001

LEU 282 GLN 283 -0.1574

GLN 283 PRO 284 -0.0002

PRO 284 VAL 285 -0.0016

VAL 285 HIS 286 0.0000

HIS 286 PHE 287 -0.1080

PHE 287 SER 288 -0.0003

SER 288 SER 289 -0.1133

SER 289 LYS 290 -0.0005

LYS 290 LYS 291 -0.0776

LYS 291 LEU 292 0.0002

LEU 292 LEU 293 0.0403

LEU 293 ASP 294 -0.0001

ASP 294 HIS 295 -0.0351

HIS 295 GLY 296 -0.0001

GLY 296 PHE 297 0.0291

PHE 297 THR 298 -0.0000

THR 298 PHE 299 -0.0418

PHE 299 ARG 300 -0.0002

ARG 300 TYR 301 -0.0945

TYR 301 THR 302 0.0005

THR 302 VAL 303 -0.0974

VAL 303 GLU 304 -0.0001

GLU 304 ASP 305 -0.0287

ASP 305 MET 306 -0.0003

MET 306 PHE 307 -0.0086

PHE 307 ASP 308 0.0000

ASP 308 ALA 309 0.0192

ALA 309 GLY 310 0.0003

GLY 310 ILE 311 0.0506

ILE 311 ARG 312 0.0004

ARG 312 THR 313 0.0232

THR 313 CYS 314 0.0002

CYS 314 ARG 315 0.0057

ARG 315 GLU 316 0.0000

GLU 316 LYS 317 -0.0130

LYS 317 GLY 318 -0.0002

GLY 318 LEU 319 -0.0879

LEU 319 ILE 320 0.0001

ILE 320 PRO 321 -0.0095

PRO 321 LEU 322 0.0000

LEU 322 ALA 323 0.0076

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 8 ---

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 *