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 11 ---

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 0.0005

PRO 2 VAL 3 0.0079

VAL 3 VAL 4 0.0002

VAL 4 VAL 5 0.0286

VAL 5 THR 6 -0.0003

THR 6 GLY 7 0.0840

GLY 7 ALA 8 0.0000

ALA 8 SER 9 -0.0203

SER 9 GLY 10 -0.0002

GLY 10 PHE 11 -0.0408

PHE 11 VAL 12 -0.0003

VAL 12 GLY 13 -0.0183

GLY 13 SER 14 -0.0003

SER 14 TRP 15 0.0806

TRP 15 LEU 16 -0.0001

LEU 16 VAL 17 -0.0224

VAL 17 MET 18 -0.0000

MET 18 LYS 19 0.0177

LYS 19 LEU 20 -0.0004

LEU 20 LEU 21 0.0130

LEU 21 GLN 22 0.0003

GLN 22 ALA 23 0.0111

ALA 23 GLY 24 0.0001

GLY 24 TYR 25 -0.0124

TYR 25 THR 26 -0.0004

THR 26 VAL 27 0.0144

VAL 27 ARG 28 0.0001

ARG 28 ALA 29 0.0201

ALA 29 THR 30 -0.0002

THR 30 VAL 31 -0.0123

VAL 31 ARG 32 0.0004

ARG 32 ASP 33 0.0135

ASP 33 PRO 34 0.0003

PRO 34 GLU 35 0.0202

GLU 35 ASN 36 0.0002

ASN 36 VAL 37 0.0168

VAL 37 GLY 38 0.0000

GLY 38 LYS 39 0.0164

LYS 39 THR 40 -0.0002

THR 40 LYS 41 0.0104

LYS 41 PRO 42 0.0002

PRO 42 LEU 43 -0.0322

LEU 43 LEU 44 0.0002

LEU 44 ASP 45 0.0129

ASP 45 LEU 46 0.0000

LEU 46 PRO 47 0.0036

PRO 47 GLY 48 -0.0000

GLY 48 ALA 49 0.0113

ALA 49 THR 50 -0.0000

THR 50 GLU 51 -0.0046

GLU 51 ARG 52 -0.0002

ARG 52 LEU 53 0.0136

LEU 53 SER 54 0.0000

SER 54 ILE 55 0.0352

ILE 55 TRP 56 0.0001

TRP 56 LYS 57 0.0049

LYS 57 ALA 58 0.0003

ALA 58 ASP 59 0.0480

ASP 59 MET 60 0.0004

MET 60 ALA 61 0.0236

ALA 61 ASP 62 -0.0002

ASP 62 GLU 63 -0.0138

GLU 63 ASP 64 0.0000

ASP 64 SER 65 0.0568

SER 65 PHE 66 -0.0002

PHE 66 ASP 67 0.0237

ASP 67 GLU 68 -0.0001

GLU 68 ALA 69 0.0213

ALA 69 ILE 70 0.0002

ILE 70 ARG 71 0.0220

ARG 71 GLY 72 0.0001

GLY 72 CYS 73 -0.0170

CYS 73 THR 74 0.0000

THR 74 GLY 75 0.0108

GLY 75 VAL 76 0.0003

VAL 76 PHE 77 0.0088

PHE 77 HIS 78 0.0005

HIS 78 VAL 79 0.0972

VAL 79 ALA 80 0.0002

ALA 80 THR 81 0.0729

THR 81 PRO 82 -0.0001

PRO 82 THR 83 -0.1272

THR 83 ASP 84 0.0002

ASP 84 PHE 85 -0.0280

PHE 85 GLU 86 0.0000

GLU 86 SER 87 0.2243

SER 87 LYS 88 0.0000

LYS 88 ASP 89 -0.0369

ASP 89 PRO 90 0.0000

PRO 90 GLU 91 0.0210

GLU 91 ASN 92 -0.0002

ASN 92 GLU 93 0.0536

GLU 93 VAL 94 -0.0002

VAL 94 ILE 95 -0.0392

ILE 95 LYS 96 -0.0001

LYS 96 PRO 97 0.1061

PRO 97 THR 98 0.0000

THR 98 VAL 99 0.0334

VAL 99 GLU 100 -0.0005

GLU 100 GLY 101 0.0903

GLY 101 MET 102 -0.0001

MET 102 ILE 103 -0.0190

ILE 103 ARG 104 0.0000

ARG 104 ILE 105 -0.0024

ILE 105 LEU 106 0.0004

LEU 106 ARG 107 0.0019

ARG 107 ALA 108 -0.0000

ALA 108 CYS 109 -0.0433

CYS 109 LYS 110 0.0002

LYS 110 GLU 111 0.0499

GLU 111 ALA 112 0.0001

ALA 112 GLY 113 -0.0091

GLY 113 THR 114 0.0002

THR 114 VAL 115 0.0154

VAL 115 ARG 116 0.0002

ARG 116 ARG 117 0.0137

ARG 117 ILE 118 -0.0003

ILE 118 VAL 119 0.0388

VAL 119 PHE 120 0.0003

PHE 120 THR 121 0.0426

THR 121 SER 122 -0.0001

SER 122 SER 123 -0.0507

SER 123 ALA 124 0.0000

ALA 124 GLY 125 -0.0005

GLY 125 THR 126 -0.0002

THR 126 VAL 127 0.0876

VAL 127 CYS 128 0.0002

CYS 128 VAL 129 0.0122

VAL 129 GLU 130 -0.0003

GLU 130 GLU 131 0.0643

GLU 131 ARG 132 0.0003

ARG 132 ARG 133 -0.1533

ARG 133 ARG 134 -0.0002

ARG 134 PRO 135 -0.0407

PRO 135 VAL 136 0.0001

VAL 136 TYR 137 -0.1180

TYR 137 ASP 138 -0.0002

ASP 138 HIS 139 -0.1150

HIS 139 ASP 140 0.0001

ASP 140 ASN 141 -0.0119

ASN 141 TRP 142 -0.0004

TRP 142 SER 143 -0.0205

SER 143 ASP 144 -0.0001

ASP 144 VAL 145 -0.0485

VAL 145 ASP 146 -0.0001

ASP 146 PHE 147 0.0781

PHE 147 CYS 148 -0.0005

CYS 148 ARG 149 0.0678

ARG 149 ARG 150 0.0003

ARG 150 VAL 151 -0.0194

VAL 151 LYS 152 0.0002

LYS 152 MET 153 -0.0282

MET 153 THR 154 0.0001

THR 154 GLY 155 -0.0781

GLY 155 TRP 156 -0.0001

TRP 156 MET 157 0.0559

MET 157 TYR 158 -0.0000

TYR 158 PHE 159 0.0166

PHE 159 VAL 160 0.0002

VAL 160 SER 161 0.1750

SER 161 LYS 162 0.0001

LYS 162 SER 163 -0.0703

SER 163 LEU 164 0.0000

LEU 164 ALA 165 0.1791

ALA 165 GLU 166 0.0001

GLU 166 LYS 167 -0.0043

LYS 167 ALA 168 -0.0002

ALA 168 ALA 169 0.0728

ALA 169 MET 170 0.0002

MET 170 ALA 171 -0.0004

ALA 171 TYR 172 -0.0000

TYR 172 ALA 173 -0.0549

ALA 173 ALA 174 -0.0000

ALA 174 GLU 175 0.0170

GLU 175 HIS 176 -0.0001

HIS 176 GLY 177 -0.0586

GLY 177 LEU 178 0.0000

LEU 178 ASP 179 -0.1236

ASP 179 LEU 180 -0.0002

LEU 180 VAL 181 -0.0396

VAL 181 SER 182 -0.0001

SER 182 VAL 183 -0.0071

VAL 183 ILE 184 -0.0000

ILE 184 PRO 185 -0.0635

PRO 185 THR 186 -0.0001

THR 186 LEU 187 -0.1131

LEU 187 VAL 188 -0.0001

VAL 188 VAL 189 0.0158

VAL 189 GLY 190 0.0003

GLY 190 PRO 191 -0.0586

PRO 191 PHE 192 0.0000

PHE 192 LEU 193 -0.0165

LEU 193 SER 194 -0.0001

SER 194 ALA 195 -0.0836

ALA 195 ALA 196 0.0001

ALA 196 MET 197 0.0250

MET 197 PRO 198 0.0001

PRO 198 PRO 199 0.1510

PRO 199 SER 200 0.0002

SER 200 LEU 201 0.0298

LEU 201 VAL 202 0.0002

VAL 202 THR 203 0.0966

THR 203 ALA 204 0.0002

ALA 204 LEU 205 0.0128

LEU 205 ALA 206 -0.0002

ALA 206 LEU 207 -0.0389

LEU 207 VAL 208 -0.0001

VAL 208 THR 209 -0.0069

THR 209 GLY 210 0.0001

GLY 210 ASN 211 -0.0688

ASN 211 GLU 212 0.0000

GLU 212 ALA 213 -0.1979

ALA 213 HIS 214 -0.0003

HIS 214 TYR 215 0.1638

TYR 215 SER 216 -0.0001

SER 216 ILE 217 -0.1352

ILE 217 LEU 218 -0.0002

LEU 218 LYS 219 0.1828

LYS 219 GLN 220 0.0001

GLN 220 VAL 221 -0.0571

VAL 221 GLN 222 0.0002

GLN 222 PHE 223 -0.1082

PHE 223 VAL 224 0.0003

VAL 224 HIS 225 -0.0621

HIS 225 LEU 226 -0.0001

LEU 226 ASP 227 -0.0138

ASP 227 ASP 228 -0.0001

ASP 228 LEU 229 0.0668

LEU 229 CYS 230 -0.0001

CYS 230 ASP 231 -0.0172

ASP 231 ALA 232 -0.0003

ALA 232 GLU 233 0.0449

GLU 233 ILE 234 0.0003

ILE 234 PHE 235 -0.0004

PHE 235 LEU 236 0.0002

LEU 236 PHE 237 -0.0460

PHE 237 GLU 238 0.0001

GLU 238 HIS 239 -0.0051

HIS 239 PRO 240 -0.0001

PRO 240 ALA 241 0.0358

ALA 241 ALA 242 0.0002

ALA 242 ALA 243 0.0419

ALA 243 GLY 244 0.0001

GLY 244 ARG 245 0.0296

ARG 245 TYR 246 0.0001

TYR 246 VAL 247 -0.0729

VAL 247 CYS 248 -0.0002

CYS 248 SER 249 0.0037

SER 249 SER 250 0.0004

SER 250 HIS 251 0.0391

HIS 251 ASP 252 0.0003

ASP 252 ALA 253 0.0604

ALA 253 THR 254 -0.0001

THR 254 ILE 255 -0.0380

ILE 255 HIS 256 -0.0002

HIS 256 GLY 257 -0.0917

GLY 257 LEU 258 0.0001

LEU 258 ALA 259 0.0375

ALA 259 ALA 260 -0.0004

ALA 260 MET 261 0.1048

MET 261 LEU 262 0.0003

LEU 262 ARG 263 0.0443

ARG 263 ASP 264 0.0003

ASP 264 ARG 265 0.0144

ARG 265 TYR 266 0.0000

TYR 266 PRO 267 0.1234

PRO 267 GLU 268 -0.0002

GLU 268 TYR 269 0.0207

TYR 269 ASP 270 0.0000

ASP 270 ILE 271 -0.0440

ILE 271 PRO 272 -0.0001

PRO 272 GLN 273 -0.0944

GLN 273 LYS 274 0.0003

LYS 274 LEU 275 -0.0636

LEU 275 ARG 276 -0.0002

ARG 276 GLY 277 -0.2587

GLY 277 ILE 278 -0.0003

ILE 278 GLU 279 -0.2647

GLU 279 ASP 280 0.0000

ASP 280 ASP 281 -0.0969

ASP 281 LEU 282 -0.0000

LEU 282 GLN 283 -0.1423

GLN 283 PRO 284 -0.0002

PRO 284 VAL 285 0.0342

VAL 285 HIS 286 -0.0003

HIS 286 PHE 287 -0.1221

PHE 287 SER 288 -0.0003

SER 288 SER 289 -0.1983

SER 289 LYS 290 -0.0002

LYS 290 LYS 291 -0.0469

LYS 291 LEU 292 -0.0001

LEU 292 LEU 293 0.0292

LEU 293 ASP 294 0.0001

ASP 294 HIS 295 -0.0419

HIS 295 GLY 296 0.0000

GLY 296 PHE 297 0.0418

PHE 297 THR 298 0.0004

THR 298 PHE 299 0.0599

PHE 299 ARG 300 0.0001

ARG 300 TYR 301 0.1141

TYR 301 THR 302 -0.0003

THR 302 VAL 303 0.0497

VAL 303 GLU 304 -0.0002

GLU 304 ASP 305 0.0786

ASP 305 MET 306 0.0002

MET 306 PHE 307 0.0486

PHE 307 ASP 308 0.0003

ASP 308 ALA 309 0.0451

ALA 309 GLY 310 -0.0002

GLY 310 ILE 311 0.0287

ILE 311 ARG 312 -0.0002

ARG 312 THR 313 0.0258

THR 313 CYS 314 -0.0003

CYS 314 ARG 315 0.0423

ARG 315 GLU 316 -0.0003

GLU 316 LYS 317 0.0259

LYS 317 GLY 318 0.0002

GLY 318 LEU 319 0.0687

LEU 319 ILE 320 0.0002

ILE 320 PRO 321 -0.0259

PRO 321 LEU 322 0.0003

LEU 322 ALA 323 -0.0171

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 11 ---

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 *