Should you encounter any unexpected behaviour,
please let us know.

* testNMAJB *

CA strain for 2404031516062184733

--- normal mode 13 ---

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
MET 1 GLY 2 0.0001

GLY 2 GLY 3 0.0148

GLY 3 GLN 4 0.0000

GLN 4 VAL 5 -0.0751

VAL 5 SER 6 0.0001

SER 6 ALA 7 -0.1064

ALA 7 SER 8 0.0001

SER 8 ASN 9 0.0435

ASN 9 SER 10 0.0001

SER 10 PHE 11 -0.0655

PHE 11 SER 12 -0.0002

SER 12 ARG 13 -0.2656

ARG 13 LEU 14 -0.0001

LEU 14 HIS 15 -0.0111

HIS 15 CYS 16 -0.0003

CYS 16 ARG 17 -0.0408

ARG 17 ASN 18 -0.0005

ASN 18 ALA 19 -0.0028

ALA 19 ASN 20 0.0002

ASN 20 GLU 21 0.0565

GLU 21 ASP 22 0.0001

ASP 22 TRP 23 -0.1403

TRP 23 MET 24 0.0001

MET 24 SER 25 0.0740

SER 25 ALA 26 0.0000

ALA 26 LEU 27 -0.1372

LEU 27 CYS 28 0.0002

CYS 28 PRO 29 0.0258

PRO 29 ARG 30 -0.0002

ARG 30 LEU 31 0.0389

LEU 31 TRP 32 0.0001

TRP 32 ASP 33 -0.0303

ASP 33 VAL 34 -0.0001

VAL 34 PRO 35 0.0884

PRO 35 LEU 36 -0.0003

LEU 36 HIS 37 -0.0394

HIS 37 HIS 38 -0.0005

HIS 38 LEU 39 -0.0830

LEU 39 SER 40 0.0004

SER 40 ILE 41 -0.0453

ILE 41 PRO 42 0.0001

PRO 42 GLY 43 -0.0212

GLY 43 SER 44 -0.0004

SER 44 HIS 45 -0.0030

HIS 45 ASP 46 0.0000

ASP 46 THR 47 0.0248

THR 47 MET 48 -0.0000

MET 48 THR 49 -0.0152

THR 49 TYR 50 -0.0000

TYR 50 CYS 51 -0.0070

CYS 51 LEU 52 -0.0001

LEU 52 ASN 53 -0.0124

ASN 53 LYS 54 -0.0002

LYS 54 LYS 55 0.0467

LYS 55 SER 56 0.0001

SER 56 PRO 57 0.1211

PRO 57 ILE 58 -0.0002

ILE 58 SER 59 0.2351

SER 59 HIS 60 0.0001

HIS 60 GLU 61 0.0301

GLU 61 GLU 62 0.0001

GLU 62 SER 63 -0.0161

SER 63 ARG 64 -0.0001

ARG 64 LEU 65 -0.1788

LEU 65 LEU 66 -0.0000

LEU 66 GLN 67 0.0118

GLN 67 LEU 68 -0.0000

LEU 68 LEU 69 -0.0103

LEU 69 ASN 70 0.0002

ASN 70 LYS 71 -0.0826

LYS 71 ALA 72 -0.0000

ALA 72 LEU 73 0.0494

LEU 73 PRO 74 0.0002

PRO 74 CYS 75 -0.0185

CYS 75 ILE 76 -0.0001

ILE 76 THR 77 0.0899

THR 77 ARG 78 0.0003

ARG 78 PRO 79 0.0058

PRO 79 VAL 80 0.0001

VAL 80 VAL 81 -0.0023

VAL 81 LEU 82 -0.0001

LEU 82 LYS 83 -0.1003

LYS 83 TRP 84 -0.0002

TRP 84 SER 85 0.0054

SER 85 VAL 86 0.0004

VAL 86 THR 87 -0.0176

THR 87 GLN 88 0.0001

GLN 88 ALA 89 0.0514

ALA 89 LEU 90 -0.0001

LEU 90 ASP 91 0.0246

ASP 91 VAL 92 0.0002

VAL 92 THR 93 -0.0433

THR 93 GLU 94 -0.0001

GLU 94 GLN 95 0.0010

GLN 95 LEU 96 -0.0000

LEU 96 ASP 97 0.0324

ASP 97 ALA 98 -0.0005

ALA 98 GLY 99 -0.0335

GLY 99 VAL 100 0.0000

VAL 100 ARG 101 0.0246

ARG 101 TYR 102 0.0002

TYR 102 LEU 103 -0.0264

LEU 103 ASP 104 0.0001

ASP 104 LEU 105 0.0333

LEU 105 ARG 106 0.0000

ARG 106 ILE 107 0.1208

ILE 107 ALA 108 0.0003

ALA 108 HIS 109 0.1030

HIS 109 MET 110 0.0000

MET 110 LEU 111 -0.1537

LEU 111 GLU 112 0.0001

GLU 112 GLY 113 0.1097

GLY 113 SER 114 -0.0000

SER 114 GLU 115 -0.0522

GLU 115 LYS 116 0.0002

LYS 116 ASN 117 -0.1836

ASN 117 LEU 118 0.0001

LEU 118 HIS 119 -0.0411

HIS 119 PHE 120 -0.0001

PHE 120 VAL 121 -0.1023

VAL 121 HIS 122 -0.0002

HIS 122 MET 123 -0.1367

MET 123 VAL 124 0.0002

VAL 124 TYR 125 0.0238

TYR 125 THR 126 0.0001

THR 126 THR 127 0.0694

THR 127 ALA 128 0.0004

ALA 128 LEU 129 -0.0118

LEU 129 VAL 130 -0.0001

VAL 130 GLU 131 0.0108

GLU 131 ASP 132 -0.0000

ASP 132 THR 133 0.0297

THR 133 LEU 134 0.0002

LEU 134 THR 135 0.0119

THR 135 GLU 136 0.0001

GLU 136 ILE 137 -0.0179

ILE 137 SER 138 -0.0000

SER 138 GLU 139 0.0660

GLU 139 TRP 140 -0.0002

TRP 140 LEU 141 0.0228

LEU 141 GLU 142 -0.0000

GLU 142 ARG 143 0.0370

ARG 143 HIS 144 -0.0002

HIS 144 PRO 145 0.0734

PRO 145 ARG 146 0.0003

ARG 146 GLU 147 0.0680

GLU 147 VAL 148 0.0001

VAL 148 VAL 149 -0.0597

VAL 149 ILE 150 -0.0000

ILE 150 LEU 151 -0.0101

LEU 151 ALA 152 -0.0002

ALA 152 CYS 153 0.0439

CYS 153 ARG 154 0.0001

ARG 154 ASN 155 -0.0098

ASN 155 PHE 156 -0.0000

PHE 156 GLU 157 -0.0859

GLU 157 GLY 158 0.0003

GLY 158 LEU 159 -0.0916

LEU 159 SER 160 -0.0001

SER 160 GLU 161 -0.0506

GLU 161 ASP 162 -0.0001

ASP 162 LEU 163 -0.0225

LEU 163 HIS 164 -0.0001

HIS 164 GLU 165 0.0059

GLU 165 TYR 166 -0.0000

TYR 166 LEU 167 0.0485

LEU 167 VAL 168 -0.0002

VAL 168 ALA 169 0.0402

ALA 169 CYS 170 -0.0002

CYS 170 ILE 171 0.0010

ILE 171 LYS 172 0.0001

LYS 172 ASN 173 0.0649

ASN 173 ILE 174 -0.0003

ILE 174 PHE 175 -0.0546

PHE 175 GLY 176 -0.0000

GLY 176 ASP 177 -0.0494

ASP 177 MET 178 -0.0002

MET 178 LEU 179 0.0029

LEU 179 CYS 180 0.0001

CYS 180 PRO 181 0.0537

PRO 181 ARG 182 0.0001

ARG 182 GLY 183 0.0491

GLY 183 GLU 184 -0.0002

GLU 184 VAL 185 0.0277

VAL 185 PRO 186 -0.0001

PRO 186 THR 187 0.1468

THR 187 LEU 188 0.0001

LEU 188 ARG 189 0.0035

ARG 189 GLN 190 0.0000

GLN 190 LEU 191 -0.0242

LEU 191 TRP 192 -0.0001

TRP 192 SER 193 0.0676

SER 193 ARG 194 0.0001

ARG 194 GLY 195 -0.0096

GLY 195 GLN 196 0.0004

GLN 196 GLN 197 0.0309

GLN 197 VAL 198 0.0002

VAL 198 ILE 199 0.0065

ILE 199 VAL 200 -0.0002

VAL 200 SER 201 0.0209

SER 201 TYR 202 0.0000

TYR 202 GLU 203 -0.0168

GLU 203 ASP 204 -0.0003

ASP 204 GLU 205 -0.0724

GLU 205 SER 206 0.0001

SER 206 SER 207 -0.0216

SER 207 LEU 208 0.0001

LEU 208 ARG 209 0.0078

ARG 209 ARG 210 -0.0001

ARG 210 HIS 211 0.0150

HIS 211 HIS 212 0.0003

HIS 212 GLU 213 0.0008

GLU 213 LEU 214 0.0001

LEU 214 TRP 215 0.0665

TRP 215 PRO 216 -0.0002

PRO 216 GLY 217 0.0638

GLY 217 VAL 218 0.0001

VAL 218 PRO 219 0.0507

PRO 219 TYR 220 0.0003

TYR 220 TRP 221 0.0580

TRP 221 TRP 222 -0.0001

TRP 222 GLY 223 0.0671

GLY 223 ASN 224 0.0002

ASN 224 ARG 225 -0.0832

ARG 225 VAL 226 -0.0001

VAL 226 LYS 227 -0.0146

LYS 227 THR 228 0.0004

THR 228 GLU 229 0.0320

GLU 229 ALA 230 0.0000

ALA 230 LEU 231 -0.0194

LEU 231 ILE 232 0.0001

ILE 232 ARG 233 0.0061

ARG 233 TYR 234 0.0000

TYR 234 LEU 235 0.0499

LEU 235 GLU 236 -0.0003

GLU 236 THR 237 -0.0251

THR 237 MET 238 -0.0000

MET 238 LYS 239 0.0811

LYS 239 SER 240 0.0004

SER 240 CYS 241 -0.1360

CYS 241 GLY 242 0.0002

GLY 242 ARG 243 0.0229

ARG 243 PRO 244 -0.0000

PRO 244 GLY 245 -0.0849

GLY 245 GLY 246 -0.0000

GLY 246 LEU 247 -0.0231

LEU 247 PHE 248 0.0000

PHE 248 VAL 249 -0.0053

VAL 249 ALA 250 -0.0003

ALA 250 GLY 251 0.0370

GLY 251 ILE 252 -0.0002

ILE 252 ASN 253 0.0717

ASN 253 LEU 254 -0.0002

LEU 254 THR 255 0.1475

THR 255 GLU 256 -0.0001

GLU 256 ASN 257 -0.0630

ASN 257 LEU 258 -0.0001

LEU 258 GLN 259 0.1180

GLN 259 TYR 260 -0.0001

TYR 260 VAL 261 -0.0529

VAL 261 LEU 262 -0.0003

LEU 262 ALA 263 0.0348

ALA 263 HIS 264 -0.0002

HIS 264 PRO 265 -0.1473

PRO 265 SER 266 0.0004

SER 266 GLU 267 -0.1960

GLU 267 SER 268 -0.0000

SER 268 LEU 269 0.0654

LEU 269 GLU 270 0.0000

GLU 270 LYS 271 -0.1362

LYS 271 MET 272 0.0001

MET 272 THR 273 0.1054

THR 273 LEU 274 -0.0002

LEU 274 PRO 275 0.0612

PRO 275 ASN 276 0.0003

ASN 276 LEU 277 0.0185

LEU 277 PRO 278 -0.0003

PRO 278 ARG 279 -0.0180

ARG 279 LEU 280 -0.0002

LEU 280 SER 281 0.0498

SER 281 ALA 282 -0.0004

ALA 282 TRP 283 -0.0609

TRP 283 VAL 284 -0.0001

VAL 284 ARG 285 0.0552

ARG 285 GLU 286 0.0001

GLU 286 GLN 287 -0.0524

GLN 287 CYS 288 0.0004

CYS 288 PRO 289 0.0266

PRO 289 GLY 290 0.0001

GLY 290 PRO 291 -0.0787

PRO 291 GLY 292 -0.0002

GLY 292 SER 293 -0.0441

SER 293 ARG 294 -0.0000

ARG 294 CYS 295 -0.0739

CYS 295 THR 296 -0.0001

THR 296 ASN 297 0.0099

ASN 297 ILE 298 0.0003

ILE 298 ILE 299 0.0131

ILE 299 ALA 300 -0.0001

ALA 300 GLY 301 0.0332

GLY 301 ASP 302 -0.0001

ASP 302 PHE 303 0.0738

PHE 303 ILE 304 -0.0003

ILE 304 GLY 305 0.0247

GLY 305 ALA 306 -0.0000

ALA 306 ASP 307 -0.1081

ASP 307 GLY 308 0.0003

GLY 308 PHE 309 -0.0086

PHE 309 VAL 310 0.0003

VAL 310 SER 311 -0.0182

SER 311 ASP 312 0.0002

ASP 312 VAL 313 0.0322

VAL 313 ILE 314 -0.0003

ILE 314 ALA 315 -0.0665

ALA 315 LEU 316 0.0000

LEU 316 ASN 317 0.0892

ASN 317 GLN 318 -0.0004

GLN 318 LYS 319 -0.1501

LYS 319 LEU 320 0.0000

LEU 320 LEU 321 0.0384

LEU 321 TRP 322 -0.0002

TRP 322 CYS 323 -0.0709

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** testNMAJB ***

CA strain for 2404031516062184733

--- normal mode 13 ---

Should you encounter any unexpected behaviour,
please let us know.

* testNMAJB *