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 10 ---

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 0.0004

PRO 2 VAL 3 0.0202

VAL 3 VAL 4 -0.0000

VAL 4 VAL 5 0.0338

VAL 5 THR 6 -0.0002

THR 6 GLY 7 -0.0282

GLY 7 ALA 8 -0.0000

ALA 8 SER 9 0.0185

SER 9 GLY 10 -0.0003

GLY 10 PHE 11 -0.0119

PHE 11 VAL 12 -0.0002

VAL 12 GLY 13 0.0086

GLY 13 SER 14 -0.0002

SER 14 TRP 15 -0.1285

TRP 15 LEU 16 -0.0000

LEU 16 VAL 17 -0.0703

VAL 17 MET 18 -0.0003

MET 18 LYS 19 -0.0695

LYS 19 LEU 20 -0.0000

LEU 20 LEU 21 -0.0552

LEU 21 GLN 22 0.0002

GLN 22 ALA 23 -0.0130

ALA 23 GLY 24 0.0003

GLY 24 TYR 25 0.0167

TYR 25 THR 26 -0.0000

THR 26 VAL 27 0.0242

VAL 27 ARG 28 -0.0000

ARG 28 ALA 29 -0.0062

ALA 29 THR 30 0.0001

THR 30 VAL 31 -0.0525

VAL 31 ARG 32 -0.0000

ARG 32 ASP 33 0.0753

ASP 33 PRO 34 -0.0002

PRO 34 GLU 35 -0.0030

GLU 35 ASN 36 -0.0001

ASN 36 VAL 37 -0.0129

VAL 37 GLY 38 -0.0006

GLY 38 LYS 39 0.0267

LYS 39 THR 40 -0.0001

THR 40 LYS 41 0.0171

LYS 41 PRO 42 -0.0004

PRO 42 LEU 43 -0.0180

LEU 43 LEU 44 -0.0002

LEU 44 ASP 45 0.0268

ASP 45 LEU 46 0.0001

LEU 46 PRO 47 0.0216

PRO 47 GLY 48 0.0002

GLY 48 ALA 49 0.0229

ALA 49 THR 50 0.0000

THR 50 GLU 51 -0.0154

GLU 51 ARG 52 -0.0001

ARG 52 LEU 53 0.0383

LEU 53 SER 54 -0.0001

SER 54 ILE 55 0.0336

ILE 55 TRP 56 -0.0004

TRP 56 LYS 57 0.0971

LYS 57 ALA 58 0.0000

ALA 58 ASP 59 0.2229

ASP 59 MET 60 0.0004

MET 60 ALA 61 -0.0068

ALA 61 ASP 62 0.0001

ASP 62 GLU 63 0.0218

GLU 63 ASP 64 0.0003

ASP 64 SER 65 -0.0371

SER 65 PHE 66 -0.0002

PHE 66 ASP 67 0.0171

ASP 67 GLU 68 0.0002

GLU 68 ALA 69 -0.0404

ALA 69 ILE 70 0.0002

ILE 70 ARG 71 0.0030

ARG 71 GLY 72 0.0001

GLY 72 CYS 73 -0.0041

CYS 73 THR 74 0.0001

THR 74 GLY 75 0.0372

GLY 75 VAL 76 -0.0000

VAL 76 PHE 77 0.0405

PHE 77 HIS 78 -0.0002

HIS 78 VAL 79 0.0007

VAL 79 ALA 80 0.0003

ALA 80 THR 81 0.4171

THR 81 PRO 82 0.0003

PRO 82 THR 83 0.2226

THR 83 ASP 84 -0.0003

ASP 84 PHE 85 0.1041

PHE 85 GLU 86 -0.0001

GLU 86 SER 87 -0.0813

SER 87 LYS 88 0.0001

LYS 88 ASP 89 -0.1250

ASP 89 PRO 90 -0.0003

PRO 90 GLU 91 -0.1560

GLU 91 ASN 92 -0.0001

ASN 92 GLU 93 0.0749

GLU 93 VAL 94 0.0000

VAL 94 ILE 95 -0.1663

ILE 95 LYS 96 0.0001

LYS 96 PRO 97 0.3063

PRO 97 THR 98 -0.0004

THR 98 VAL 99 -0.0179

VAL 99 GLU 100 0.0001

GLU 100 GLY 101 0.0393

GLY 101 MET 102 -0.0000

MET 102 ILE 103 0.0035

ILE 103 ARG 104 -0.0000

ARG 104 ILE 105 -0.0521

ILE 105 LEU 106 0.0002

LEU 106 ARG 107 0.0058

ARG 107 ALA 108 -0.0001

ALA 108 CYS 109 -0.0343

CYS 109 LYS 110 0.0002

LYS 110 GLU 111 -0.0068

GLU 111 ALA 112 0.0000

ALA 112 GLY 113 -0.0011

GLY 113 THR 114 0.0001

THR 114 VAL 115 0.0080

VAL 115 ARG 116 -0.0002

ARG 116 ARG 117 0.0263

ARG 117 ILE 118 -0.0000

ILE 118 VAL 119 0.0138

VAL 119 PHE 120 -0.0001

PHE 120 THR 121 0.0364

THR 121 SER 122 0.0002

SER 122 SER 123 0.0320

SER 123 ALA 124 -0.0000

ALA 124 GLY 125 -0.0036

GLY 125 THR 126 -0.0001

THR 126 VAL 127 0.0218

VAL 127 CYS 128 -0.0001

CYS 128 VAL 129 -0.0214

VAL 129 GLU 130 -0.0000

GLU 130 GLU 131 0.0238

GLU 131 ARG 132 0.0003

ARG 132 ARG 133 -0.0222

ARG 133 ARG 134 -0.0001

ARG 134 PRO 135 -0.0064

PRO 135 VAL 136 0.0001

VAL 136 TYR 137 -0.0043

TYR 137 ASP 138 -0.0004

ASP 138 HIS 139 -0.0232

HIS 139 ASP 140 0.0001

ASP 140 ASN 141 -0.0703

ASN 141 TRP 142 -0.0000

TRP 142 SER 143 -0.1088

SER 143 ASP 144 0.0003

ASP 144 VAL 145 -0.0582

VAL 145 ASP 146 -0.0002

ASP 146 PHE 147 0.0239

PHE 147 CYS 148 0.0001

CYS 148 ARG 149 -0.0337

ARG 149 ARG 150 0.0000

ARG 150 VAL 151 0.1033

VAL 151 LYS 152 0.0001

LYS 152 MET 153 0.3950

MET 153 THR 154 -0.0002

THR 154 GLY 155 0.2402

GLY 155 TRP 156 -0.0003

TRP 156 MET 157 0.1591

MET 157 TYR 158 0.0003

TYR 158 PHE 159 0.0045

PHE 159 VAL 160 -0.0000

VAL 160 SER 161 0.1325

SER 161 LYS 162 -0.0000

LYS 162 SER 163 -0.0169

SER 163 LEU 164 0.0001

LEU 164 ALA 165 0.1297

ALA 165 GLU 166 0.0000

GLU 166 LYS 167 -0.0059

LYS 167 ALA 168 0.0000

ALA 168 ALA 169 -0.0111

ALA 169 MET 170 -0.0004

MET 170 ALA 171 0.0377

ALA 171 TYR 172 0.0004

TYR 172 ALA 173 -0.0450

ALA 173 ALA 174 -0.0001

ALA 174 GLU 175 0.0024

GLU 175 HIS 176 0.0001

HIS 176 GLY 177 -0.0061

GLY 177 LEU 178 0.0001

LEU 178 ASP 179 -0.0550

ASP 179 LEU 180 -0.0003

LEU 180 VAL 181 -0.0209

VAL 181 SER 182 0.0001

SER 182 VAL 183 -0.0241

VAL 183 ILE 184 0.0001

ILE 184 PRO 185 0.0104

PRO 185 THR 186 -0.0000

THR 186 LEU 187 -0.0412

LEU 187 VAL 188 0.0001

VAL 188 VAL 189 -0.0256

VAL 189 GLY 190 0.0000

GLY 190 PRO 191 0.0167

PRO 191 PHE 192 0.0000

PHE 192 LEU 193 -0.0225

LEU 193 SER 194 0.0004

SER 194 ALA 195 0.0218

ALA 195 ALA 196 -0.0001

ALA 196 MET 197 0.0136

MET 197 PRO 198 -0.0000

PRO 198 PRO 199 0.0230

PRO 199 SER 200 -0.0001

SER 200 LEU 201 0.0103

LEU 201 VAL 202 0.0001

VAL 202 THR 203 -0.0183

THR 203 ALA 204 -0.0001

ALA 204 LEU 205 -0.0320

LEU 205 ALA 206 -0.0002

ALA 206 LEU 207 0.0638

LEU 207 VAL 208 0.0000

VAL 208 THR 209 -0.0192

THR 209 GLY 210 0.0002

GLY 210 ASN 211 0.0458

ASN 211 GLU 212 0.0001

GLU 212 ALA 213 0.2716

ALA 213 HIS 214 -0.0002

HIS 214 TYR 215 0.0773

TYR 215 SER 216 -0.0001

SER 216 ILE 217 -0.0373

ILE 217 LEU 218 -0.0001

LEU 218 LYS 219 0.1046

LYS 219 GLN 220 -0.0003

GLN 220 VAL 221 -0.0197

VAL 221 GLN 222 -0.0003

GLN 222 PHE 223 -0.0638

PHE 223 VAL 224 0.0002

VAL 224 HIS 225 -0.0659

HIS 225 LEU 226 0.0002

LEU 226 ASP 227 -0.0067

ASP 227 ASP 228 0.0003

ASP 228 LEU 229 0.0071

LEU 229 CYS 230 -0.0001

CYS 230 ASP 231 0.0425

ASP 231 ALA 232 -0.0002

ALA 232 GLU 233 -0.0364

GLU 233 ILE 234 0.0002

ILE 234 PHE 235 -0.0091

PHE 235 LEU 236 -0.0005

LEU 236 PHE 237 -0.0816

PHE 237 GLU 238 -0.0001

GLU 238 HIS 239 -0.0622

HIS 239 PRO 240 0.0000

PRO 240 ALA 241 -0.0011

ALA 241 ALA 242 -0.0004

ALA 242 ALA 243 -0.0066

ALA 243 GLY 244 0.0000

GLY 244 ARG 245 -0.0147

ARG 245 TYR 246 -0.0003

TYR 246 VAL 247 -0.0540

VAL 247 CYS 248 0.0001

CYS 248 SER 249 -0.0764

SER 249 SER 250 0.0000

SER 250 HIS 251 -0.1964

HIS 251 ASP 252 0.0002

ASP 252 ALA 253 -0.1922

ALA 253 THR 254 -0.0000

THR 254 ILE 255 -0.0783

ILE 255 HIS 256 0.0000

HIS 256 GLY 257 -0.0505

GLY 257 LEU 258 -0.0002

LEU 258 ALA 259 -0.0297

ALA 259 ALA 260 0.0002

ALA 260 MET 261 -0.1087

MET 261 LEU 262 0.0001

LEU 262 ARG 263 -0.0155

ARG 263 ASP 264 -0.0001

ASP 264 ARG 265 -0.0700

ARG 265 TYR 266 0.0000

TYR 266 PRO 267 -0.0607

PRO 267 GLU 268 -0.0001

GLU 268 TYR 269 0.0127

TYR 269 ASP 270 -0.0001

ASP 270 ILE 271 0.0306

ILE 271 PRO 272 -0.0001

PRO 272 GLN 273 0.0157

GLN 273 LYS 274 0.0001

LYS 274 LEU 275 0.0824

LEU 275 ARG 276 -0.0002

ARG 276 GLY 277 -0.0356

GLY 277 ILE 278 0.0002

ILE 278 GLU 279 0.1444

GLU 279 ASP 280 0.0002

ASP 280 ASP 281 -0.0329

ASP 281 LEU 282 -0.0003

LEU 282 GLN 283 -0.0990

GLN 283 PRO 284 -0.0001

PRO 284 VAL 285 -0.0130

VAL 285 HIS 286 -0.0002

HIS 286 PHE 287 -0.1367

PHE 287 SER 288 -0.0002

SER 288 SER 289 -0.1210

SER 289 LYS 290 -0.0000

LYS 290 LYS 291 -0.0013

LYS 291 LEU 292 0.0001

LEU 292 LEU 293 0.0249

LEU 293 ASP 294 -0.0000

ASP 294 HIS 295 -0.0230

HIS 295 GLY 296 0.0001

GLY 296 PHE 297 0.0111

PHE 297 THR 298 0.0000

THR 298 PHE 299 -0.0592

PHE 299 ARG 300 0.0001

ARG 300 TYR 301 -0.1083

TYR 301 THR 302 0.0001

THR 302 VAL 303 -0.2132

VAL 303 GLU 304 0.0002

GLU 304 ASP 305 0.0148

ASP 305 MET 306 -0.0003

MET 306 PHE 307 -0.0274

PHE 307 ASP 308 0.0002

ASP 308 ALA 309 -0.0119

ALA 309 GLY 310 -0.0002

GLY 310 ILE 311 -0.0229

ILE 311 ARG 312 -0.0001

ARG 312 THR 313 -0.0270

THR 313 CYS 314 0.0001

CYS 314 ARG 315 0.0052

ARG 315 GLU 316 0.0001

GLU 316 LYS 317 -0.0239

LYS 317 GLY 318 0.0001

GLY 318 LEU 319 -0.0464

LEU 319 ILE 320 0.0002

ILE 320 PRO 321 0.0376

PRO 321 LEU 322 0.0001

LEU 322 ALA 323 0.0065

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 10 ---

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 *