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 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 -0.0002

PRO 2 VAL 3 -0.0237

VAL 3 VAL 4 -0.0000

VAL 4 VAL 5 0.0469

VAL 5 THR 6 -0.0003

THR 6 GLY 7 0.0017

GLY 7 ALA 8 0.0002

ALA 8 SER 9 -0.0118

SER 9 GLY 10 -0.0002

GLY 10 PHE 11 0.3234

PHE 11 VAL 12 -0.0001

VAL 12 GLY 13 0.1615

GLY 13 SER 14 -0.0000

SER 14 TRP 15 -0.0402

TRP 15 LEU 16 -0.0003

LEU 16 VAL 17 0.0165

VAL 17 MET 18 -0.0003

MET 18 LYS 19 -0.0117

LYS 19 LEU 20 -0.0000

LEU 20 LEU 21 -0.0348

LEU 21 GLN 22 0.0001

GLN 22 ALA 23 -0.0014

ALA 23 GLY 24 0.0003

GLY 24 TYR 25 0.0053

TYR 25 THR 26 -0.0001

THR 26 VAL 27 -0.0090

VAL 27 ARG 28 0.0001

ARG 28 ALA 29 0.0194

ALA 29 THR 30 -0.0003

THR 30 VAL 31 0.0024

VAL 31 ARG 32 0.0002

ARG 32 ASP 33 -0.0427

ASP 33 PRO 34 0.0001

PRO 34 GLU 35 0.0503

GLU 35 ASN 36 -0.0001

ASN 36 VAL 37 -0.0014

VAL 37 GLY 38 0.0001

GLY 38 LYS 39 0.1213

LYS 39 THR 40 -0.0000

THR 40 LYS 41 0.0239

LYS 41 PRO 42 0.0001

PRO 42 LEU 43 -0.0274

LEU 43 LEU 44 -0.0004

LEU 44 ASP 45 -0.0188

ASP 45 LEU 46 -0.0001

LEU 46 PRO 47 -0.0103

PRO 47 GLY 48 -0.0001

GLY 48 ALA 49 -0.0055

ALA 49 THR 50 0.0001

THR 50 GLU 51 0.0144

GLU 51 ARG 52 0.0000

ARG 52 LEU 53 -0.0104

LEU 53 SER 54 -0.0001

SER 54 ILE 55 -0.0309

ILE 55 TRP 56 0.0002

TRP 56 LYS 57 -0.0942

LYS 57 ALA 58 -0.0000

ALA 58 ASP 59 -0.0889

ASP 59 MET 60 -0.0004

MET 60 ALA 61 0.0013

ALA 61 ASP 62 0.0000

ASP 62 GLU 63 0.0052

GLU 63 ASP 64 -0.0002

ASP 64 SER 65 0.0126

SER 65 PHE 66 0.0001

PHE 66 ASP 67 -0.0019

ASP 67 GLU 68 -0.0002

GLU 68 ALA 69 0.0231

ALA 69 ILE 70 -0.0000

ILE 70 ARG 71 0.0032

ARG 71 GLY 72 -0.0004

GLY 72 CYS 73 -0.0344

CYS 73 THR 74 0.0001

THR 74 GLY 75 -0.0044

GLY 75 VAL 76 0.0001

VAL 76 PHE 77 0.0074

PHE 77 HIS 78 -0.0005

HIS 78 VAL 79 0.0017

VAL 79 ALA 80 0.0002

ALA 80 THR 81 -0.2823

THR 81 PRO 82 -0.0002

PRO 82 THR 83 -0.0032

THR 83 ASP 84 -0.0004

ASP 84 PHE 85 0.0590

PHE 85 GLU 86 -0.0000

GLU 86 SER 87 0.0471

SER 87 LYS 88 0.0003

LYS 88 ASP 89 0.0588

ASP 89 PRO 90 -0.0001

PRO 90 GLU 91 0.0170

GLU 91 ASN 92 0.0000

ASN 92 GLU 93 -0.0164

GLU 93 VAL 94 -0.0002

VAL 94 ILE 95 0.0206

ILE 95 LYS 96 0.0001

LYS 96 PRO 97 -0.1042

PRO 97 THR 98 -0.0002

THR 98 VAL 99 -0.0097

VAL 99 GLU 100 -0.0001

GLU 100 GLY 101 -0.0735

GLY 101 MET 102 -0.0002

MET 102 ILE 103 0.0276

ILE 103 ARG 104 -0.0000

ARG 104 ILE 105 0.0325

ILE 105 LEU 106 0.0000

LEU 106 ARG 107 -0.0448

ARG 107 ALA 108 -0.0002

ALA 108 CYS 109 -0.0072

CYS 109 LYS 110 0.0001

LYS 110 GLU 111 -0.0088

GLU 111 ALA 112 -0.0000

ALA 112 GLY 113 -0.0296

GLY 113 THR 114 0.0000

THR 114 VAL 115 -0.0285

VAL 115 ARG 116 0.0002

ARG 116 ARG 117 -0.0291

ARG 117 ILE 118 0.0002

ILE 118 VAL 119 -0.0081

VAL 119 PHE 120 -0.0003

PHE 120 THR 121 -0.0023

THR 121 SER 122 0.0001

SER 122 SER 123 0.0270

SER 123 ALA 124 -0.0002

ALA 124 GLY 125 -0.0197

GLY 125 THR 126 0.0002

THR 126 VAL 127 0.0150

VAL 127 CYS 128 -0.0001

CYS 128 VAL 129 0.0335

VAL 129 GLU 130 0.0002

GLU 130 GLU 131 -0.0481

GLU 131 ARG 132 -0.0001

ARG 132 ARG 133 -0.0025

ARG 133 ARG 134 -0.0003

ARG 134 PRO 135 0.0735

PRO 135 VAL 136 -0.0001

VAL 136 TYR 137 -0.0694

TYR 137 ASP 138 -0.0001

ASP 138 HIS 139 -0.0941

HIS 139 ASP 140 -0.0001

ASP 140 ASN 141 0.0636

ASN 141 TRP 142 -0.0005

TRP 142 SER 143 0.1105

SER 143 ASP 144 -0.0002

ASP 144 VAL 145 0.0192

VAL 145 ASP 146 -0.0000

ASP 146 PHE 147 -0.0420

PHE 147 CYS 148 -0.0000

CYS 148 ARG 149 0.0319

ARG 149 ARG 150 0.0003

ARG 150 VAL 151 -0.0637

VAL 151 LYS 152 0.0001

LYS 152 MET 153 -0.0599

MET 153 THR 154 0.0000

THR 154 GLY 155 0.2412

GLY 155 TRP 156 -0.0001

TRP 156 MET 157 0.0677

MET 157 TYR 158 -0.0001

TYR 158 PHE 159 0.0507

PHE 159 VAL 160 0.0001

VAL 160 SER 161 -0.0650

SER 161 LYS 162 -0.0003

LYS 162 SER 163 -0.0103

SER 163 LEU 164 0.0000

LEU 164 ALA 165 -0.0602

ALA 165 GLU 166 0.0001

GLU 166 LYS 167 0.0065

LYS 167 ALA 168 -0.0002

ALA 168 ALA 169 -0.0027

ALA 169 MET 170 -0.0001

MET 170 ALA 171 -0.0461

ALA 171 TYR 172 0.0000

TYR 172 ALA 173 0.0218

ALA 173 ALA 174 0.0003

ALA 174 GLU 175 0.0021

GLU 175 HIS 176 -0.0001

HIS 176 GLY 177 -0.0243

GLY 177 LEU 178 0.0001

LEU 178 ASP 179 -0.0951

ASP 179 LEU 180 -0.0003

LEU 180 VAL 181 -0.0504

VAL 181 SER 182 -0.0001

SER 182 VAL 183 -0.0109

VAL 183 ILE 184 0.0001

ILE 184 PRO 185 0.0191

PRO 185 THR 186 0.0002

THR 186 LEU 187 -0.0517

LEU 187 VAL 188 0.0001

VAL 188 VAL 189 -0.0615

VAL 189 GLY 190 0.0002

GLY 190 PRO 191 -0.0206

PRO 191 PHE 192 -0.0000

PHE 192 LEU 193 0.0355

LEU 193 SER 194 0.0002

SER 194 ALA 195 -0.0092

ALA 195 ALA 196 -0.0001

ALA 196 MET 197 0.0186

MET 197 PRO 198 -0.0002

PRO 198 PRO 199 -0.0637

PRO 199 SER 200 -0.0001

SER 200 LEU 201 -0.0581

LEU 201 VAL 202 -0.0002

VAL 202 THR 203 -0.0337

THR 203 ALA 204 0.0001

ALA 204 LEU 205 -0.0380

LEU 205 ALA 206 0.0003

ALA 206 LEU 207 -0.0033

LEU 207 VAL 208 -0.0000

VAL 208 THR 209 -0.0914

THR 209 GLY 210 0.0001

GLY 210 ASN 211 -0.0421

ASN 211 GLU 212 -0.0001

GLU 212 ALA 213 0.0731

ALA 213 HIS 214 -0.0001

HIS 214 TYR 215 -0.0090

TYR 215 SER 216 -0.0001

SER 216 ILE 217 -0.0923

ILE 217 LEU 218 -0.0001

LEU 218 LYS 219 0.0067

LYS 219 GLN 220 0.0001

GLN 220 VAL 221 0.0224

VAL 221 GLN 222 0.0000

GLN 222 PHE 223 0.0022

PHE 223 VAL 224 0.0000

VAL 224 HIS 225 0.0059

HIS 225 LEU 226 0.0001

LEU 226 ASP 227 0.0084

ASP 227 ASP 228 0.0000

ASP 228 LEU 229 -0.0419

LEU 229 CYS 230 -0.0003

CYS 230 ASP 231 0.0478

ASP 231 ALA 232 0.0002

ALA 232 GLU 233 -0.0383

GLU 233 ILE 234 0.0003

ILE 234 PHE 235 -0.0006

PHE 235 LEU 236 -0.0000

LEU 236 PHE 237 -0.0613

PHE 237 GLU 238 0.0002

GLU 238 HIS 239 -0.0478

HIS 239 PRO 240 -0.0004

PRO 240 ALA 241 0.0058

ALA 241 ALA 242 -0.0003

ALA 242 ALA 243 0.0475

ALA 243 GLY 244 -0.0002

GLY 244 ARG 245 0.0171

ARG 245 TYR 246 -0.0000

TYR 246 VAL 247 -0.0922

VAL 247 CYS 248 -0.0003

CYS 248 SER 249 -0.0507

SER 249 SER 250 0.0002

SER 250 HIS 251 -0.1205

HIS 251 ASP 252 0.0004

ASP 252 ALA 253 -0.0937

ALA 253 THR 254 -0.0003

THR 254 ILE 255 -0.0406

ILE 255 HIS 256 -0.0001

HIS 256 GLY 257 -0.0124

GLY 257 LEU 258 -0.0003

LEU 258 ALA 259 -0.0085

ALA 259 ALA 260 0.0000

ALA 260 MET 261 -0.0368

MET 261 LEU 262 0.0001

LEU 262 ARG 263 0.0113

ARG 263 ASP 264 -0.0000

ASP 264 ARG 265 -0.0135

ARG 265 TYR 266 -0.0003

TYR 266 PRO 267 -0.0112

PRO 267 GLU 268 -0.0003

GLU 268 TYR 269 -0.0124

TYR 269 ASP 270 0.0004

ASP 270 ILE 271 -0.0148

ILE 271 PRO 272 -0.0000

PRO 272 GLN 273 0.0364

GLN 273 LYS 274 0.0000

LYS 274 LEU 275 0.0385

LEU 275 ARG 276 0.0000

ARG 276 GLY 277 -0.0098

GLY 277 ILE 278 0.0001

ILE 278 GLU 279 0.0557

GLU 279 ASP 280 -0.0003

ASP 280 ASP 281 0.0088

ASP 281 LEU 282 -0.0001

LEU 282 GLN 283 -0.1041

GLN 283 PRO 284 -0.0000

PRO 284 VAL 285 -0.0370

VAL 285 HIS 286 -0.0004

HIS 286 PHE 287 -0.1604

PHE 287 SER 288 -0.0003

SER 288 SER 289 -0.0223

SER 289 LYS 290 0.0003

LYS 290 LYS 291 -0.0749

LYS 291 LEU 292 0.0001

LEU 292 LEU 293 0.0286

LEU 293 ASP 294 -0.0002

ASP 294 HIS 295 -0.0394

HIS 295 GLY 296 0.0003

GLY 296 PHE 297 0.0145

PHE 297 THR 298 -0.0001

THR 298 PHE 299 -0.0487

PHE 299 ARG 300 0.0003

ARG 300 TYR 301 -0.0570

TYR 301 THR 302 -0.0001

THR 302 VAL 303 -0.1065

VAL 303 GLU 304 -0.0001

GLU 304 ASP 305 0.0253

ASP 305 MET 306 0.0001

MET 306 PHE 307 -0.0092

PHE 307 ASP 308 0.0001

ASP 308 ALA 309 0.0149

ALA 309 GLY 310 -0.0003

GLY 310 ILE 311 0.0701

ILE 311 ARG 312 -0.0001

ARG 312 THR 313 0.0216

THR 313 CYS 314 -0.0003

CYS 314 ARG 315 -0.0109

ARG 315 GLU 316 -0.0002

GLU 316 LYS 317 0.0146

LYS 317 GLY 318 -0.0002

GLY 318 LEU 319 -0.0977

LEU 319 ILE 320 0.0003

ILE 320 PRO 321 0.0723

PRO 321 LEU 322 -0.0000

LEU 322 ALA 323 0.0221

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 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 DHK *