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

* testNMAJB *

CA strain for 2404031516062184733

--- normal mode 12 ---

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 0.0355

GLY 3 GLN 4 0.0002

GLN 4 VAL 5 -0.0970

VAL 5 SER 6 -0.0002

SER 6 ALA 7 -0.0470

ALA 7 SER 8 0.0004

SER 8 ASN 9 -0.0532

ASN 9 SER 10 -0.0002

SER 10 PHE 11 0.0766

PHE 11 SER 12 0.0002

SER 12 ARG 13 0.3592

ARG 13 LEU 14 -0.0003

LEU 14 HIS 15 0.1724

HIS 15 CYS 16 -0.0000

CYS 16 ARG 17 0.0039

ARG 17 ASN 18 -0.0000

ASN 18 ALA 19 -0.2366

ALA 19 ASN 20 -0.0003

ASN 20 GLU 21 0.0113

GLU 21 ASP 22 -0.0003

ASP 22 TRP 23 -0.0460

TRP 23 MET 24 -0.0003

MET 24 SER 25 0.0182

SER 25 ALA 26 -0.0003

ALA 26 LEU 27 -0.0604

LEU 27 CYS 28 0.0002

CYS 28 PRO 29 -0.0073

PRO 29 ARG 30 -0.0002

ARG 30 LEU 31 -0.0006

LEU 31 TRP 32 -0.0004

TRP 32 ASP 33 -0.0299

ASP 33 VAL 34 0.0001

VAL 34 PRO 35 0.0987

PRO 35 LEU 36 0.0000

LEU 36 HIS 37 -0.0381

HIS 37 HIS 38 -0.0003

HIS 38 LEU 39 -0.0619

LEU 39 SER 40 0.0003

SER 40 ILE 41 -0.0020

ILE 41 PRO 42 0.0001

PRO 42 GLY 43 -0.0206

GLY 43 SER 44 -0.0000

SER 44 HIS 45 -0.0036

HIS 45 ASP 46 0.0000

ASP 46 THR 47 -0.0019

THR 47 MET 48 -0.0001

MET 48 THR 49 0.0506

THR 49 TYR 50 0.0002

TYR 50 CYS 51 -0.0877

CYS 51 LEU 52 -0.0002

LEU 52 ASN 53 0.0239

ASN 53 LYS 54 -0.0001

LYS 54 LYS 55 -0.1012

LYS 55 SER 56 0.0001

SER 56 PRO 57 -0.0374

PRO 57 ILE 58 -0.0002

ILE 58 SER 59 -0.1354

SER 59 HIS 60 0.0000

HIS 60 GLU 61 -0.0319

GLU 61 GLU 62 -0.0000

GLU 62 SER 63 0.0326

SER 63 ARG 64 -0.0000

ARG 64 LEU 65 0.0377

LEU 65 LEU 66 -0.0003

LEU 66 GLN 67 0.0104

GLN 67 LEU 68 0.0002

LEU 68 LEU 69 -0.0173

LEU 69 ASN 70 0.0001

ASN 70 LYS 71 0.1158

LYS 71 ALA 72 0.0002

ALA 72 LEU 73 -0.0230

LEU 73 PRO 74 -0.0002

PRO 74 CYS 75 -0.0063

CYS 75 ILE 76 0.0000

ILE 76 THR 77 -0.1089

THR 77 ARG 78 -0.0000

ARG 78 PRO 79 0.0191

PRO 79 VAL 80 0.0001

VAL 80 VAL 81 0.0009

VAL 81 LEU 82 -0.0000

LEU 82 LYS 83 -0.0251

LYS 83 TRP 84 -0.0003

TRP 84 SER 85 0.0292

SER 85 VAL 86 0.0003

VAL 86 THR 87 -0.1045

THR 87 GLN 88 0.0001

GLN 88 ALA 89 0.0495

ALA 89 LEU 90 -0.0001

LEU 90 ASP 91 0.0039

ASP 91 VAL 92 -0.0001

VAL 92 THR 93 0.0403

THR 93 GLU 94 0.0002

GLU 94 GLN 95 0.0179

GLN 95 LEU 96 -0.0000

LEU 96 ASP 97 -0.0029

ASP 97 ALA 98 -0.0003

ALA 98 GLY 99 -0.0728

GLY 99 VAL 100 -0.0005

VAL 100 ARG 101 -0.0106

ARG 101 TYR 102 -0.0002

TYR 102 LEU 103 0.0468

LEU 103 ASP 104 -0.0003

ASP 104 LEU 105 0.0279

LEU 105 ARG 106 0.0000

ARG 106 ILE 107 0.0283

ILE 107 ALA 108 -0.0002

ALA 108 HIS 109 -0.0155

HIS 109 MET 110 -0.0001

MET 110 LEU 111 0.2198

LEU 111 GLU 112 0.0003

GLU 112 GLY 113 0.0099

GLY 113 SER 114 0.0002

SER 114 GLU 115 0.0163

GLU 115 LYS 116 -0.0001

LYS 116 ASN 117 -0.1108

ASN 117 LEU 118 0.0003

LEU 118 HIS 119 0.0027

HIS 119 PHE 120 -0.0000

PHE 120 VAL 121 0.0916

VAL 121 HIS 122 -0.0002

HIS 122 MET 123 0.0642

MET 123 VAL 124 -0.0001

VAL 124 TYR 125 -0.0194

TYR 125 THR 126 -0.0003

THR 126 THR 127 0.0963

THR 127 ALA 128 -0.0001

ALA 128 LEU 129 0.0447

LEU 129 VAL 130 0.0002

VAL 130 GLU 131 0.0537

GLU 131 ASP 132 0.0004

ASP 132 THR 133 -0.0563

THR 133 LEU 134 -0.0001

LEU 134 THR 135 -0.0118

THR 135 GLU 136 0.0004

GLU 136 ILE 137 0.0482

ILE 137 SER 138 0.0001

SER 138 GLU 139 -0.0332

GLU 139 TRP 140 -0.0001

TRP 140 LEU 141 0.0278

LEU 141 GLU 142 -0.0001

GLU 142 ARG 143 -0.0131

ARG 143 HIS 144 -0.0001

HIS 144 PRO 145 0.0153

PRO 145 ARG 146 0.0002

ARG 146 GLU 147 0.0087

GLU 147 VAL 148 -0.0003

VAL 148 VAL 149 0.0216

VAL 149 ILE 150 -0.0002

ILE 150 LEU 151 0.0584

LEU 151 ALA 152 -0.0001

ALA 152 CYS 153 0.0724

CYS 153 ARG 154 -0.0001

ARG 154 ASN 155 0.0283

ASN 155 PHE 156 -0.0000

PHE 156 GLU 157 0.0927

GLU 157 GLY 158 0.0002

GLY 158 LEU 159 -0.0414

LEU 159 SER 160 0.0004

SER 160 GLU 161 0.0280

GLU 161 ASP 162 0.0000

ASP 162 LEU 163 -0.0195

LEU 163 HIS 164 0.0004

HIS 164 GLU 165 0.0244

GLU 165 TYR 166 0.0000

TYR 166 LEU 167 0.0063

LEU 167 VAL 168 -0.0000

VAL 168 ALA 169 0.0240

ALA 169 CYS 170 0.0001

CYS 170 ILE 171 0.0797

ILE 171 LYS 172 -0.0005

LYS 172 ASN 173 0.0330

ASN 173 ILE 174 0.0001

ILE 174 PHE 175 0.0862

PHE 175 GLY 176 0.0001

GLY 176 ASP 177 0.1302

ASP 177 MET 178 0.0002

MET 178 LEU 179 -0.0335

LEU 179 CYS 180 0.0001

CYS 180 PRO 181 0.0051

PRO 181 ARG 182 0.0000

ARG 182 GLY 183 0.0856

GLY 183 GLU 184 0.0001

GLU 184 VAL 185 0.0042

VAL 185 PRO 186 -0.0005

PRO 186 THR 187 0.1268

THR 187 LEU 188 0.0003

LEU 188 ARG 189 -0.0313

ARG 189 GLN 190 -0.0003

GLN 190 LEU 191 0.0494

LEU 191 TRP 192 0.0000

TRP 192 SER 193 -0.0027

SER 193 ARG 194 -0.0000

ARG 194 GLY 195 0.0367

GLY 195 GLN 196 -0.0001

GLN 196 GLN 197 0.0042

GLN 197 VAL 198 -0.0001

VAL 198 ILE 199 -0.0125

ILE 199 VAL 200 -0.0004

VAL 200 SER 201 -0.0125

SER 201 TYR 202 -0.0002

TYR 202 GLU 203 -0.0367

GLU 203 ASP 204 -0.0001

ASP 204 GLU 205 -0.0018

GLU 205 SER 206 0.0002

SER 206 SER 207 -0.0300

SER 207 LEU 208 -0.0002

LEU 208 ARG 209 0.0164

ARG 209 ARG 210 -0.0002

ARG 210 HIS 211 -0.0186

HIS 211 HIS 212 0.0002

HIS 212 GLU 213 -0.0299

GLU 213 LEU 214 0.0001

LEU 214 TRP 215 0.0674

TRP 215 PRO 216 -0.0002

PRO 216 GLY 217 0.0376

GLY 217 VAL 218 0.0002

VAL 218 PRO 219 0.0144

PRO 219 TYR 220 0.0003

TYR 220 TRP 221 0.0141

TRP 221 TRP 222 0.0000

TRP 222 GLY 223 -0.0640

GLY 223 ASN 224 0.0003

ASN 224 ARG 225 -0.0057

ARG 225 VAL 226 -0.0001

VAL 226 LYS 227 -0.0557

LYS 227 THR 228 0.0001

THR 228 GLU 229 -0.0386

GLU 229 ALA 230 -0.0003

ALA 230 LEU 231 0.0082

LEU 231 ILE 232 0.0005

ILE 232 ARG 233 0.0141

ARG 233 TYR 234 0.0000

TYR 234 LEU 235 -0.0063

LEU 235 GLU 236 0.0002

GLU 236 THR 237 0.0209

THR 237 MET 238 -0.0003

MET 238 LYS 239 -0.0048

LYS 239 SER 240 0.0000

SER 240 CYS 241 -0.0560

CYS 241 GLY 242 -0.0003

GLY 242 ARG 243 0.0309

ARG 243 PRO 244 -0.0001

PRO 244 GLY 245 -0.1010

GLY 245 GLY 246 0.0000

GLY 246 LEU 247 -0.0176

LEU 247 PHE 248 -0.0002

PHE 248 VAL 249 -0.0390

VAL 249 ALA 250 0.0001

ALA 250 GLY 251 -0.0457

GLY 251 ILE 252 0.0002

ILE 252 ASN 253 -0.0927

ASN 253 LEU 254 -0.0003

LEU 254 THR 255 -0.2964

THR 255 GLU 256 -0.0001

GLU 256 ASN 257 -0.0784

ASN 257 LEU 258 -0.0003

LEU 258 GLN 259 -0.0652

GLN 259 TYR 260 0.0003

TYR 260 VAL 261 0.0822

VAL 261 LEU 262 0.0000

LEU 262 ALA 263 0.0504

ALA 263 HIS 264 0.0002

HIS 264 PRO 265 0.1129

PRO 265 SER 266 0.0000

SER 266 GLU 267 0.1176

GLU 267 SER 268 -0.0004

SER 268 LEU 269 -0.1115

LEU 269 GLU 270 -0.0003

GLU 270 LYS 271 0.1268

LYS 271 MET 272 0.0004

MET 272 THR 273 -0.2904

THR 273 LEU 274 0.0004

LEU 274 PRO 275 0.1593

PRO 275 ASN 276 -0.0001

ASN 276 LEU 277 0.0059

LEU 277 PRO 278 0.0002

PRO 278 ARG 279 0.0305

ARG 279 LEU 280 0.0003

LEU 280 SER 281 0.0299

SER 281 ALA 282 -0.0000

ALA 282 TRP 283 -0.0156

TRP 283 VAL 284 -0.0004

VAL 284 ARG 285 0.0492

ARG 285 GLU 286 -0.0002

GLU 286 GLN 287 -0.0351

GLN 287 CYS 288 -0.0000

CYS 288 PRO 289 -0.0327

PRO 289 GLY 290 0.0003

GLY 290 PRO 291 -0.0732

PRO 291 GLY 292 0.0005

GLY 292 SER 293 -0.0657

SER 293 ARG 294 -0.0000

ARG 294 CYS 295 -0.0225

CYS 295 THR 296 0.0001

THR 296 ASN 297 0.0401

ASN 297 ILE 298 0.0004

ILE 298 ILE 299 -0.0421

ILE 299 ALA 300 0.0001

ALA 300 GLY 301 -0.0690

GLY 301 ASP 302 -0.0001

ASP 302 PHE 303 0.0408

PHE 303 ILE 304 0.0001

ILE 304 GLY 305 -0.0443

GLY 305 ALA 306 0.0002

ALA 306 ASP 307 -0.0608

ASP 307 GLY 308 0.0001

GLY 308 PHE 309 -0.0606

PHE 309 VAL 310 0.0004

VAL 310 SER 311 -0.0302

SER 311 ASP 312 -0.0002

ASP 312 VAL 313 -0.0080

VAL 313 ILE 314 -0.0001

ILE 314 ALA 315 -0.0311

ALA 315 LEU 316 0.0001

LEU 316 ASN 317 0.0001

ASN 317 GLN 318 0.0001

GLN 318 LYS 319 -0.0513

LYS 319 LEU 320 0.0003

LEU 320 LEU 321 0.0424

LEU 321 TRP 322 0.0004

TRP 322 CYS 323 -0.0584

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 12 ---

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

* testNMAJB *