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 9 ---

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 0.0434

VAL 3 VAL 4 -0.0001

VAL 4 VAL 5 0.1380

VAL 5 THR 6 -0.0004

THR 6 GLY 7 0.0258

GLY 7 ALA 8 0.0001

ALA 8 SER 9 0.0039

SER 9 GLY 10 0.0001

GLY 10 PHE 11 0.2826

PHE 11 VAL 12 0.0000

VAL 12 GLY 13 0.1491

GLY 13 SER 14 0.0003

SER 14 TRP 15 -0.0592

TRP 15 LEU 16 0.0000

LEU 16 VAL 17 0.0742

VAL 17 MET 18 -0.0002

MET 18 LYS 19 -0.0512

LYS 19 LEU 20 -0.0003

LEU 20 LEU 21 -0.0610

LEU 21 GLN 22 -0.0003

GLN 22 ALA 23 -0.0537

ALA 23 GLY 24 0.0003

GLY 24 TYR 25 0.0121

TYR 25 THR 26 0.0000

THR 26 VAL 27 0.0353

VAL 27 ARG 28 -0.0001

ARG 28 ALA 29 -0.0327

ALA 29 THR 30 0.0004

THR 30 VAL 31 -0.1004

VAL 31 ARG 32 0.0001

ARG 32 ASP 33 0.0675

ASP 33 PRO 34 0.0003

PRO 34 GLU 35 0.0335

GLU 35 ASN 36 -0.0002

ASN 36 VAL 37 -0.0211

VAL 37 GLY 38 -0.0002

GLY 38 LYS 39 0.1473

LYS 39 THR 40 0.0001

THR 40 LYS 41 0.0841

LYS 41 PRO 42 -0.0000

PRO 42 LEU 43 -0.0247

LEU 43 LEU 44 -0.0002

LEU 44 ASP 45 -0.0408

ASP 45 LEU 46 0.0002

LEU 46 PRO 47 -0.0087

PRO 47 GLY 48 0.0003

GLY 48 ALA 49 0.0073

ALA 49 THR 50 0.0000

THR 50 GLU 51 0.0215

GLU 51 ARG 52 -0.0001

ARG 52 LEU 53 0.0172

LEU 53 SER 54 -0.0003

SER 54 ILE 55 0.0174

ILE 55 TRP 56 -0.0002

TRP 56 LYS 57 0.0291

LYS 57 ALA 58 0.0002

ALA 58 ASP 59 0.0708

ASP 59 MET 60 0.0002

MET 60 ALA 61 -0.0198

ALA 61 ASP 62 -0.0001

ASP 62 GLU 63 0.0134

GLU 63 ASP 64 -0.0002

ASP 64 SER 65 0.0101

SER 65 PHE 66 -0.0001

PHE 66 ASP 67 0.0607

ASP 67 GLU 68 0.0000

GLU 68 ALA 69 0.0159

ALA 69 ILE 70 -0.0004

ILE 70 ARG 71 0.0132

ARG 71 GLY 72 -0.0001

GLY 72 CYS 73 0.0328

CYS 73 THR 74 0.0000

THR 74 GLY 75 0.0325

GLY 75 VAL 76 0.0000

VAL 76 PHE 77 0.0879

PHE 77 HIS 78 0.0000

HIS 78 VAL 79 0.1355

VAL 79 ALA 80 0.0003

ALA 80 THR 81 0.3200

THR 81 PRO 82 0.0002

PRO 82 THR 83 0.1554

THR 83 ASP 84 0.0000

ASP 84 PHE 85 0.0116

PHE 85 GLU 86 -0.0002

GLU 86 SER 87 -0.0558

SER 87 LYS 88 -0.0002

LYS 88 ASP 89 -0.0610

ASP 89 PRO 90 -0.0004

PRO 90 GLU 91 -0.0210

GLU 91 ASN 92 0.0001

ASN 92 GLU 93 0.0093

GLU 93 VAL 94 -0.0002

VAL 94 ILE 95 -0.0248

ILE 95 LYS 96 -0.0004

LYS 96 PRO 97 0.0900

PRO 97 THR 98 -0.0001

THR 98 VAL 99 0.0352

VAL 99 GLU 100 0.0000

GLU 100 GLY 101 0.0442

GLY 101 MET 102 0.0002

MET 102 ILE 103 0.0333

ILE 103 ARG 104 -0.0001

ARG 104 ILE 105 -0.0354

ILE 105 LEU 106 0.0001

LEU 106 ARG 107 0.0262

ARG 107 ALA 108 -0.0003

ALA 108 CYS 109 0.0109

CYS 109 LYS 110 0.0000

LYS 110 GLU 111 -0.0431

GLU 111 ALA 112 0.0003

ALA 112 GLY 113 0.0348

GLY 113 THR 114 -0.0001

THR 114 VAL 115 -0.0011

VAL 115 ARG 116 0.0003

ARG 116 ARG 117 -0.0661

ARG 117 ILE 118 -0.0001

ILE 118 VAL 119 0.0257

VAL 119 PHE 120 -0.0002

PHE 120 THR 121 0.0623

THR 121 SER 122 -0.0002

SER 122 SER 123 0.0041

SER 123 ALA 124 -0.0002

ALA 124 GLY 125 0.0062

GLY 125 THR 126 0.0003

THR 126 VAL 127 -0.0054

VAL 127 CYS 128 -0.0001

CYS 128 VAL 129 0.0049

VAL 129 GLU 130 -0.0000

GLU 130 GLU 131 0.0016

GLU 131 ARG 132 -0.0004

ARG 132 ARG 133 -0.0527

ARG 133 ARG 134 -0.0001

ARG 134 PRO 135 -0.0500

PRO 135 VAL 136 0.0004

VAL 136 TYR 137 -0.0435

TYR 137 ASP 138 -0.0002

ASP 138 HIS 139 -0.1029

HIS 139 ASP 140 0.0002

ASP 140 ASN 141 -0.0644

ASN 141 TRP 142 -0.0002

TRP 142 SER 143 -0.0395

SER 143 ASP 144 -0.0002

ASP 144 VAL 145 -0.0194

VAL 145 ASP 146 -0.0000

ASP 146 PHE 147 0.0085

PHE 147 CYS 148 -0.0002

CYS 148 ARG 149 -0.0041

ARG 149 ARG 150 0.0001

ARG 150 VAL 151 0.0158

VAL 151 LYS 152 -0.0003

LYS 152 MET 153 -0.0037

MET 153 THR 154 -0.0003

THR 154 GLY 155 -0.1368

GLY 155 TRP 156 0.0001

TRP 156 MET 157 -0.0351

MET 157 TYR 158 0.0002

TYR 158 PHE 159 -0.0036

PHE 159 VAL 160 -0.0002

VAL 160 SER 161 0.0517

SER 161 LYS 162 0.0002

LYS 162 SER 163 0.0419

SER 163 LEU 164 0.0001

LEU 164 ALA 165 -0.0184

ALA 165 GLU 166 -0.0003

GLU 166 LYS 167 0.0798

LYS 167 ALA 168 -0.0001

ALA 168 ALA 169 -0.0421

ALA 169 MET 170 -0.0002

MET 170 ALA 171 0.0335

ALA 171 TYR 172 -0.0001

TYR 172 ALA 173 0.0314

ALA 173 ALA 174 0.0004

ALA 174 GLU 175 0.0030

GLU 175 HIS 176 0.0004

HIS 176 GLY 177 0.0606

GLY 177 LEU 178 0.0002

LEU 178 ASP 179 0.0929

ASP 179 LEU 180 0.0003

LEU 180 VAL 181 0.0119

VAL 181 SER 182 0.0003

SER 182 VAL 183 -0.0337

VAL 183 ILE 184 0.0001

ILE 184 PRO 185 -0.0146

PRO 185 THR 186 -0.0002

THR 186 LEU 187 0.0757

LEU 187 VAL 188 0.0002

VAL 188 VAL 189 0.0840

VAL 189 GLY 190 -0.0003

GLY 190 PRO 191 -0.0719

PRO 191 PHE 192 0.0001

PHE 192 LEU 193 0.0303

LEU 193 SER 194 0.0003

SER 194 ALA 195 -0.0694

ALA 195 ALA 196 -0.0000

ALA 196 MET 197 0.0657

MET 197 PRO 198 -0.0000

PRO 198 PRO 199 0.1613

PRO 199 SER 200 0.0003

SER 200 LEU 201 -0.0081

LEU 201 VAL 202 -0.0001

VAL 202 THR 203 0.0454

THR 203 ALA 204 -0.0002

ALA 204 LEU 205 -0.0341

LEU 205 ALA 206 0.0000

ALA 206 LEU 207 0.0432

LEU 207 VAL 208 -0.0002

VAL 208 THR 209 0.0190

THR 209 GLY 210 0.0000

GLY 210 ASN 211 0.0307

ASN 211 GLU 212 -0.0000

GLU 212 ALA 213 -0.0829

ALA 213 HIS 214 -0.0000

HIS 214 TYR 215 0.0397

TYR 215 SER 216 0.0005

SER 216 ILE 217 -0.0182

ILE 217 LEU 218 0.0001

LEU 218 LYS 219 -0.0292

LYS 219 GLN 220 -0.0001

GLN 220 VAL 221 -0.0027

VAL 221 GLN 222 -0.0000

GLN 222 PHE 223 0.0461

PHE 223 VAL 224 0.0001

VAL 224 HIS 225 0.0947

HIS 225 LEU 226 0.0002

LEU 226 ASP 227 0.0075

ASP 227 ASP 228 0.0000

ASP 228 LEU 229 0.0221

LEU 229 CYS 230 0.0000

CYS 230 ASP 231 -0.0281

ASP 231 ALA 232 -0.0004

ALA 232 GLU 233 -0.0007

GLU 233 ILE 234 0.0000

ILE 234 PHE 235 -0.1061

PHE 235 LEU 236 0.0001

LEU 236 PHE 237 -0.0846

PHE 237 GLU 238 0.0002

GLU 238 HIS 239 -0.1371

HIS 239 PRO 240 -0.0001

PRO 240 ALA 241 -0.0521

ALA 241 ALA 242 -0.0003

ALA 242 ALA 243 -0.0411

ALA 243 GLY 244 0.0001

GLY 244 ARG 245 -0.1178

ARG 245 TYR 246 -0.0003

TYR 246 VAL 247 -0.0908

VAL 247 CYS 248 0.0000

CYS 248 SER 249 -0.0728

SER 249 SER 250 0.0002

SER 250 HIS 251 0.0331

HIS 251 ASP 252 0.0001

ASP 252 ALA 253 0.0634

ALA 253 THR 254 -0.0001

THR 254 ILE 255 -0.0112

ILE 255 HIS 256 0.0003

HIS 256 GLY 257 0.0388

GLY 257 LEU 258 0.0002

LEU 258 ALA 259 -0.0520

ALA 259 ALA 260 0.0001

ALA 260 MET 261 0.1162

MET 261 LEU 262 0.0001

LEU 262 ARG 263 0.0184

ARG 263 ASP 264 0.0001

ASP 264 ARG 265 0.1040

ARG 265 TYR 266 -0.0002

TYR 266 PRO 267 0.0591

PRO 267 GLU 268 0.0001

GLU 268 TYR 269 0.0206

TYR 269 ASP 270 -0.0001

ASP 270 ILE 271 -0.0547

ILE 271 PRO 272 -0.0001

PRO 272 GLN 273 -0.0510

GLN 273 LYS 274 -0.0001

LYS 274 LEU 275 0.0050

LEU 275 ARG 276 0.0003

ARG 276 GLY 277 0.0155

GLY 277 ILE 278 0.0000

ILE 278 GLU 279 -0.0865

GLU 279 ASP 280 0.0002

ASP 280 ASP 281 0.0226

ASP 281 LEU 282 -0.0003

LEU 282 GLN 283 0.0068

GLN 283 PRO 284 -0.0003

PRO 284 VAL 285 -0.0651

VAL 285 HIS 286 0.0002

HIS 286 PHE 287 -0.0457

PHE 287 SER 288 -0.0001

SER 288 SER 289 -0.0190

SER 289 LYS 290 0.0003

LYS 290 LYS 291 -0.0158

LYS 291 LEU 292 -0.0002

LEU 292 LEU 293 0.0128

LEU 293 ASP 294 0.0001

ASP 294 HIS 295 -0.0249

HIS 295 GLY 296 -0.0002

GLY 296 PHE 297 -0.0028

PHE 297 THR 298 -0.0003

THR 298 PHE 299 -0.0138

PHE 299 ARG 300 -0.0001

ARG 300 TYR 301 -0.0235

TYR 301 THR 302 -0.0002

THR 302 VAL 303 0.0852

VAL 303 GLU 304 -0.0001

GLU 304 ASP 305 0.0038

ASP 305 MET 306 0.0000

MET 306 PHE 307 -0.0125

PHE 307 ASP 308 0.0000

ASP 308 ALA 309 0.0431

ALA 309 GLY 310 0.0003

GLY 310 ILE 311 0.1589

ILE 311 ARG 312 -0.0004

ARG 312 THR 313 0.0641

THR 313 CYS 314 -0.0001

CYS 314 ARG 315 0.0675

ARG 315 GLU 316 -0.0001

GLU 316 LYS 317 0.0472

LYS 317 GLY 318 -0.0001

GLY 318 LEU 319 -0.0316

LEU 319 ILE 320 -0.0002

ILE 320 PRO 321 0.0632

PRO 321 LEU 322 -0.0000

LEU 322 ALA 323 0.0538

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 9 ---

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 *